substrate_name: N-phenyltaurine

column_label: JBC full-table HTML Table IV row N-Phenyltaurine (50-500 microM) column K m (microM) reports 237, converted to 0.237 mM.

raw_value_unit_evidence: Km raw_value=237 raw_unit=microM

row_label: N-Phenyltaurine (50-500 microM)

substrate: N-phenyltaurine


enzyme_display_name: Alkanesulfonate monooxygenase

organism: Escherichia coli (strain K12)

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

assay_conditions_summary: pH 9.1; cofactor NADPH

column_label: JBC full-table HTML Table IV row 4-Phenyl-1-butanesulfonic acid (70-500 microM) column K m (microM) reports 110, converted to 0.11 mM.

raw_value_unit_evidence: Km raw_value=110 raw_unit=microM

table_label: Table IV. Kinetic parameters of alkanesulfonate monooxygenase

data_origin: experimental

enzyme: Alkanesulfonate monooxygenase

status: verified

source: uniprot


substrate_name: MOPS

column_label: JBC full-table HTML Table IV row MOPS (70-1000 microM) column K m (microM) reports 617, converted to 0.617 mM.

raw_value_unit_evidence: Km raw_value=617 raw_unit=microM

row_label: MOPS (70-1000 microM)

substrate: MOPS


substrate_name: butanesulfonate

column_label: JBC full-table HTML Table IV row Butanesulfonic acid (250-1000 microM) column K m (microM) reports 870, converted to 0.87 mM.

raw_value_unit_evidence: Km raw_value=870 raw_unit=microM

row_label: Butanesulfonic acid (250-1000 microM)

substrate: butanesulfonate


substrate_name: PIPES

column_label: JBC full-table HTML Table IV row PIPES (333-3000 microM) column K m (microM) reports 1110, converted to 1.11 mM.

raw_value_unit_evidence: Km raw_value=1110 raw_unit=microM

row_label: PIPES (333-3000 microM)

substrate: PIPES


enzyme_display_name: FMN reductase (NADH)

organism: Aminobacter aminovorans

substrate_name: Nitrilotriacetic acid; O2; H+; NADH

verification_status: unverified

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

assay_conditions_summary: cofactor NADH

enzyme: FMN reductase (NADH)

substrate: Nitrilotriacetic acid; O2; H+; NADH

status: unverified


enzyme_display_name: 4-hydroxyphenylacetate 3-monooxygenase

organism: Acinetobacter baumannii

substrate_name: 4-Hydroxyphenylacetate; O2; H+; NADH

enzyme: 4-hydroxyphenylacetate 3-monooxygenase

substrate: 4-Hydroxyphenylacetate; O2; H+; NADH


organism: Escherichia coli

substrate_name: naringenin

source_db: oed

kcat_over_km_origin: calculated

substrate: naringenin

source: oed


substrate_name: 4-coumaric acid

substrate: 4-coumaric acid


substrate_name: umbelliferone

substrate: umbelliferone


substrate_name: resveratrol

substrate: resveratrol


enzyme_display_name: UniProt A0A140NG21

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A0A140NG21

source: skid


enzyme_display_name: alkanesulfonate monooxygenase

substrate_name: octanesulfonate

sequence_variant_note: Mutation signature R263A matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

smiles: CCCCCCCCS(=O)(=O)O

mutation_type: substitution

enzyme: alkanesulfonate monooxygenase

substrate: octanesulfonate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R263A/R271A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R271A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D251A/D252A/E253A to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

substrate_name: NADH

source_db: brenda

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

substrate: NADH

source: brenda


enzyme_display_name: Nitrilotriacetate monooxygenase component A

substrate_name: nitriloacetate

smiles: C(C(=O)O)N(CC(=O)O)CC(=O)O

column_label: PMID 1735711 abstract/PMC prose, Mg(2+)-NTA metric phrase, Km = 0.5 mM.

normalized_value_unit_evidence: Km for Mg(2+)-NTA = 0.5 mM.

raw_value_unit_evidence: The Km values for Mg(2+)-NTA, FMN, and NADH were determined as 0.5 mM, 1.3 microM, and 0.35 mM, respectively.

row_label: Mg(2+)-NTA substrate

table_label: PubMed abstract / official PMC abstract prose

substrate: nitriloacetate


column_label: PubMed abstract metric sentence gives Km for NADH as 0.35 mM

normalized_value_unit_evidence: PubMed abstract NADH Km normalized_value=0.35 normalized_unit=mM

raw_value_unit_evidence: PubMed abstract: The Km values for Mg(2+)-NTA, FMN, and NADH were determined as 0.5 mM, 1.3 microM, and 0.35 mM, respectively

row_label: NTA-Mo substrate/cofactor Km sentence

table_label: PubMed abstract

enzyme: Nitrilotriacetate monooxygenase component A


substrate_name: decanesulfonic acid

smiles: CCCCCCCCCCS(=O)(=O)O

substrate: decanesulfonic acid


substrate_name: octanesulfonic acid

smiles: CCCCCCCCS(=O)(=O)[O-]

substrate: octanesulfonic acid


substrate_name: hexanesulfonic acid

smiles: CCCCCCS(=O)(=O)O

substrate: hexanesulfonic acid


substrate_name: 4-phenyl-1-butanesulfonic acid

substrate: 4-phenyl-1-butanesulfonic acid


substrate_name: 2-(4-pyridyl)ethanesulfonic acid

substrate: 2-(4-pyridyl)ethanesulfonic acid


substrate_name: pentanesulfonic acid

smiles: CCCCCS(=O)(=O)[O-]

substrate: pentanesulfonic acid


substrate_name: N-phenyltaurine

substrate: N-phenyltaurine


substrate_name: MOPS

substrate: MOPS


substrate_name: butanesulfonic acid

smiles: CCCCS(=O)(=O)O

substrate: butanesulfonic acid


substrate_name: PIPES

substrate: PIPES


km_display: Not reported


substrate_name: FMN

assay_conditions_summary: cofactor FMN

substrate: FMN


substrate_name: riboflavin

substrate: riboflavin


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: naringenin

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines:
mutant XS4, pH 7, 30°C
mutant XS2, pH 7, 30°C
mutant XS5, pH 7, 30°C

substrate: naringenin


substrate_name: 4-coumaric acid

proof_lines:
mutant XS2, pH 7, 30°C
mutant XS6, pH 7, 30°C
mutant XS5, pH 7, 30°C

substrate: 4-coumaric acid


substrate_name: umbelliferone

proof_lines:
mutant XS5, pH 7, 30°C
mutant XS3, pH 7, 30°C
mutant XS2, pH 7, 30°C

substrate: umbelliferone


substrate_name: resveratrol

proof_lines:
mutant XS5, pH 7, 30°C
mutant XS2, pH 7, 30°C
mutant XS6, pH 7, 30°C

substrate: resveratrol


enzyme_display_name: UniProt A7U483

organism: Danio rerio

substrate_name: progesterone

enzyme: UniProt A7U483

substrate: progesterone


substrate_name: pregnenolone

substrate: pregnenolone


enzyme_display_name: UniProt B3DH80

enzyme: UniProt B3DH80


substrate_name: methyl 4-hydroxybenzoate

substrate: methyl 4-hydroxybenzoate


substrate_name: phenol

substrate: phenol


substrate_name: DL-4-hydroxymandelic acid

substrate: DL-4-hydroxymandelic acid


substrate_name: octanesulfonate

proof_lines: mutant E20A, pH 7.5, temperature not specified in the publication

substrate: octanesulfonate


proof_lines: mutant D111A, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication


enzyme_display_name: DNA oxidative demethylase

assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines: at 25°C, pH not specified in the publication

proof_lines: apparent value, at 37°C, pH not specified in the publication

enzyme: DNA oxidative demethylase


proof_lines: at 37°C, pH not specified in the publication


enzyme_display_name: UniProt Q9LAG2

organism: Parageobacillus thermoglucosidasius

enzyme: UniProt Q9LAG2


enzyme_display_name: UniProt Q9LBX2

organism: Paenibacillus sp.

substrate_name: benzothiophene

enzyme: UniProt Q9LBX2

substrate: benzothiophene


enzyme_display_name: UniProt P22680

organism: Homo sapiens

enzyme: UniProt P22680


enzyme_display_name: UniProt C4B644

organism: Pseudonocardia autotrophica

substrate_name: vitamin D3

enzyme: UniProt C4B644

substrate: vitamin D3


enzyme_display_name: UniProt Q9Y6A2

substrate_name: cholesterol 3-sulfate

enzyme: UniProt Q9Y6A2

substrate: cholesterol 3-sulfate


enzyme_display_name: 3-carboxyethylcatechol 2,3-dioxygenase

substrate_name: catechol

enzyme: 3-carboxyethylcatechol 2,3-dioxygenase

substrate: catechol


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: mitomycin C

assay_conditions_summary: cofactor NADPH

proof_lines: full-length enzyme, absence of calmodulin

enzyme: nitric-oxide synthase (NADPH)

substrate: mitomycin C


substrate_name: adriamycin

substrate: adriamycin


substrate_name: menadione

substrate: menadione


enzyme_display_name: gentisate 1,2-dioxygenase

enzyme: gentisate 1,2-dioxygenase


enzyme_display_name: taurine dioxygenase

substrate_name: N-methyltaurine

smiles: CNCCS(=O)(=O)O

proof_lines:
deuterated substrate
commercially available substrate

enzyme: taurine dioxygenase

substrate: N-methyltaurine


smiles: O=O

proof_lines: commercially available substrate 2-methyltaurine


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonate

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonate


enzyme_display_name: arachidonate 15-lipoxygenase

enzyme: arachidonate 15-lipoxygenase


enzyme_display_name: Hexahomomethionine N-hydroxylase

organism: Arabidopsis thaliana

substrate_name: pentahomomethionine

smiles: CSCCCCCCCC(C(=O)O)N

enzyme: Hexahomomethionine N-hydroxylase

substrate: pentahomomethionine


substrate_name: hexahomomethionine

smiles: CSCCCCCCCCC(C(=O)O)N

substrate: hexahomomethionine


substrate_name: L-arginine

smiles: C(CC(C(=O)O)N)CN=C(N)N

substrate: L-arginine


substrate_name: Unknown

ki_unit: mM

proof_lines:
wild type nNOS
wild type eNOS

substrate: Unknown


enzyme_display_name: UniProt O34453

organism: Bacillus subtilis

substrate_name: tetrahydrobiopterin

enzyme: UniProt O34453

substrate: tetrahydrobiopterin


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


enzyme_display_name: Cytochrome P450 71D178

organism: Origanum vulgare

substrate_name: gamma-terpinene

enzyme: Cytochrome P450 71D178

substrate: gamma-terpinene


enzyme_display_name: indoleamine 2,3-dioxygenase

substrate_name: L-tryptophan

enzyme: indoleamine 2,3-dioxygenase

substrate: L-tryptophan


enzyme_display_name: phenylacetaldehyde oxime monooxygenase

organism: Prunus mume

assay_conditions_summary: pH 7.6; cofactor NADPH

proof_lines: kcat is 46.3 min(-1) with phenylacetaldoxime as substrate (in the presence of NADPH at pH 7.6 and 30 degrees Celsius) (PubMed:25015725). kcat is 24.2 min(-1) with phenylacetonitrile as substrate (in the presence of NADPH at pH 7.6 and 30 de

source_databases_merged: brenda uniprot

enzyme: phenylacetaldehyde oxime monooxygenase


substrate_name: phenylacetonitrile

substrate: phenylacetonitrile


substrate_name: (E)-phenylacetaldehyde oxime

substrate: (E)-phenylacetaldehyde oxime


enzyme_display_name: Cytochrome P450 71D180

organism: Thymus vulgaris

proof_lines: kcat is 1.24 sec(-1) with gamma-terpinene as substrate (Ref.1). kcat is 0.08 sec(-1) with (4R)-limonene as substrate (Ref.1). kcat is 0.15 sec(-1) with (4S)-limonene as substrate (Ref.1).

enzyme: Cytochrome P450 71D180


enzyme_display_name: aromatic aldoxime N-monooxygenase

substrate_name: (E)-p-hydroxyphenylacetaldehyde oxime

sequence_source: multiple

proof_lines: kcat is 52 min(-1) with indole-3-acetaldoxime as substrate. kcat is 14 min(-1) with p-hydroxyphenylacetaldoxime as substrate. kcat is 47 min(-1) with phenylacetaldoxime as substrate.

enzyme: aromatic aldoxime N-monooxygenase

substrate: (E)-p-hydroxyphenylacetaldehyde oxime


substrate_name: (E)-indol-3-ylacetaldehyde oxime

substrate: (E)-indol-3-ylacetaldehyde oxime


enzyme_display_name: Cytochrome P450 2U1

substrate_name: arachidonic acid

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)O

enzyme: Cytochrome P450 2U1

substrate: arachidonic acid


enzyme_display_name: flavonoid 3'-monooxygenase

organism: Citrus sinensis

substrate_name: naringenin

enzyme: flavonoid 3'-monooxygenase

substrate: naringenin


enzyme_display_name: Tabersonine 3-oxygenase

organism: Catharanthus roseus

substrate_name: tabersonine

proof_lines: The KM is measured in the presence of a saturating amount of tabersonine 3-reductase, the enzyme converting the unstable intermediate produced by the reaction.

enzyme: Tabersonine 3-oxygenase

substrate: tabersonine


substrate_name: Phenylacetaldoxime; NADPH; O2

assay_conditions_summary: cofactor NADP+

substrate: Phenylacetaldoxime; NADPH; O2


substrate_name: 4-Hydroxyphenylacetaldoxime; NADPH; 2-Mercaptoethanol; O2; H+


enzyme_display_name: nitric-oxide synthase [NAD(P)H]

substrate_name: O2; L-Arginine; NADPH; H+

enzyme: nitric-oxide synthase [NAD(P)H]

substrate: O2; L-Arginine; NADPH; H+


enzyme_display_name: tabersonine 3-oxygenase

substrate_name: Tabersonine; O2; NADPH

enzyme: tabersonine 3-oxygenase

substrate: Tabersonine; O2; NADPH


enzyme_display_name: Cytochrome P450 2C9

enzyme: Cytochrome P450 2C9


enzyme_display_name: UniProt Q00456

organism: Pseudomonas mendocina

substrate_name: Benzene

enzyme: UniProt Q00456

substrate: Benzene


substrate_name: Toluene

proof_lines:
Raw SKiD Env: Temp=4°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: Toluene


substrate_name: anisole

substrate: anisole


substrate_name: chlorobenzene

substrate: chlorobenzene


substrate_name: nitrobenzene

substrate: nitrobenzene


substrate_name: methyl phenyl sulfide

substrate: methyl phenyl sulfide


enzyme_display_name: UniProt Q00459

enzyme: UniProt Q00459


enzyme_display_name: nitric-oxide synthase (flavodoxin)

proof_lines:
Bacillus subtilis
nitric-oxide synthase-like protein
l-Arg

enzyme: nitric-oxide synthase (flavodoxin)


smiles: CCC=CCC=CCC=CCC=CCC=CCCCC(=O)O


smiles: CCC=CCC=CCC=CCC=CCCCCCCC(=O)[O-]


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Helianthus tuberosus

substrate_name: NADPH

enzyme: trans-cinnamate 4-monooxygenase

substrate: NADPH


substrate_name: (E)-phenylacetaldehyde oxime


substrate_name: (E)-p-hydroxyphenylacetaldehyde oxime


substrate_name: tolbutamide

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

substrate: tolbutamide


substrate_name: diclofenac

substrate: diclofenac


substrate_name: losartan

substrate: losartan


enzyme_display_name: syn-pimaradiene 3-monooxygenase

organism: Oryza sativa subsp. japonica

substrate_name: ent-sandaracopimaradiene

proof_lines: kcat is 1.4 sec(-1) with syn-pimaradiene as substrate.

enzyme: syn-pimaradiene 3-monooxygenase

substrate: ent-sandaracopimaradiene


substrate_name: ent-kaurene

substrate: ent-kaurene


enzyme_display_name: dimethylamine monooxygenase

organism: Cyberlindnera jadinii

substrate_name: diethylmethylamine

smiles: CCN(C)CC

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines: with NADH as cosubstrate, at pH 7.0 and 25°C

enzyme: dimethylamine monooxygenase

substrate: diethylmethylamine


substrate_name: trimethylamine

smiles: CN(C)C

substrate: trimethylamine


substrate_name: dimethylethylamine

smiles: CCN(C)C

substrate: dimethylethylamine


substrate_name: triethylamine

smiles: CCN(CC)CC

substrate: triethylamine


substrate_name: Diethylamine

smiles: CCNCC

substrate: Diethylamine


substrate_name: dibutylamine

smiles: CCCCNCCCC

substrate: dibutylamine


substrate_name: NADH

substrate: NADH


substrate_name: methylbutylamine

smiles: CCCCNC

substrate: methylbutylamine


substrate_name: Dimethylamine

smiles: CNC

substrate: Dimethylamine


substrate_name: methyloctylamine

smiles: CCCCCCCCNC

substrate: methyloctylamine


substrate_name: Methylpropylamine

smiles: CCCNC

substrate: Methylpropylamine


substrate_name: methylethylamine

smiles: CCNC

substrate: methylethylamine


organism: Aminobacter aminovorans

assay_conditions_summary: pH 6.8; 301.15 K; cofactor NADH


substrate_name: NADPH

assay_conditions_summary: pH 6.8; 301.15 K; cofactor NADPH

substrate: NADPH


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


proof_lines: pH and temperature not specified in the publication


substrate_name: methyl-n-propylamine

substrate: methyl-n-propylamine


substrate_name: N-Methylethanolamine

smiles: CNCCO

substrate: N-Methylethanolamine


substrate_name: ethyl-n-propylamine

smiles: CCCNCC

substrate: ethyl-n-propylamine


substrate_name: n-butylmethylamine

substrate: n-butylmethylamine


organism: Sorghum bicolor

substrate_name: 2-Naphthoic acid; H+; NADPH; O2

substrate: 2-Naphthoic acid; H+; NADPH; O2


enzyme_display_name: toluene 4-monooxygenase

organism: Burkholderia cepacia

substrate_name: methyl 4-tolyl sulfide

proof_lines: whole-cell assay, 25°C, pH not specified in the publication

enzyme: toluene 4-monooxygenase

substrate: methyl 4-tolyl sulfide


substrate_name: methyl phenyl sulfide

substrate: methyl phenyl sulfide


substrate_name: ethylbutylamine

smiles: CCCCNCC

substrate: ethylbutylamine


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


substrate_name: methylisopropylamine

smiles: CC(C)NC

substrate: methylisopropylamine


substrate_name: dipropylamine

smiles: CCCNCCC

substrate: dipropylamine


substrate_name: Methylethanolamine

substrate: Methylethanolamine


substrate_name: propylbutylamine

smiles: CCCCNCCC

substrate: propylbutylamine


substrate_name: ethylpropylamine

substrate: ethylpropylamine


enzyme_display_name: 5-pyridoxate monooxygenase

organism: Pseudomonas sp.

substrate_name: 5-pyridoxic acid

enzyme: 5-pyridoxate monooxygenase

substrate: 5-pyridoxic acid


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: isoflavone 3'-hydroxylase

organism: Cicer arietinum

substrate_name: formononetin

enzyme: isoflavone 3'-hydroxylase

substrate: formononetin


substrate_name: Biochanin A

substrate: Biochanin A


enzyme_display_name: 4'-methoxyisoflavone 2'-hydroxylase

enzyme: 4'-methoxyisoflavone 2'-hydroxylase


enzyme_display_name: ent-kaurene monooxygenase

organism: Montanoa tomentosa

enzyme: ent-kaurene monooxygenase


organism: Physcomitrium patens

proof_lines: pH 7.5, 30°C, recombinant His-tagged enzyme


enzyme_display_name: 7-deoxyloganate 7-hydroxylase

organism: Lonicera japonica

enzyme: 7-deoxyloganate 7-hydroxylase


organism: Arthrobacter sp.

substrate_name: NADPH

substrate: NADPH


smiles: O=O


enzyme_display_name: Isoflavone 2'-hydroxylase

organism: Medicago truncatula

proof_lines: kcat is 0.015 sec(-1) with formononetin as substrate. kcat is 0.033 sec(-1) with biochanin A as substrate.

enzyme: Isoflavone 2'-hydroxylase


substrate_name: biochanin A

substrate: biochanin A


enzyme_display_name: Isoflavone 3'-hydroxylase

proof_lines: kcat is 0.028 sec(-1) with formononetin as substrate. kcat is 0.1 sec(-1) with biochanin A as substrate.

enzyme: Isoflavone 3'-hydroxylase


enzyme_display_name: 2-hydroxyisoflavanone synthase

organism: Glycyrrhiza echinata

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S310T to reconstruct the assayed variant sequence.

enzyme: 2-hydroxyisoflavanone synthase


organism: Ectopseudomonas mendocina

substrate_name: Toluene

verification_status: corrected

sequence_variant_note: Mutation signature ΔN7 is validated as an N-terminal deletion of the first 7 mature-chain residue(s) from ncbi_protein:AAS66663.1_mature_chain_2-103; the provided variant sequence equals the exact canonical suffix after that deletion.

mutation_type: deletion

assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Official ACS Table 4; row DeltaN7; columns kcat (s^-1), KM (uM), and kcat/KM (uM^-1 s^-1); captured publisher HTML table segment; footnotes a and c preserve assay and mature-chain deletion context.

normalized_value_unit_evidence: Official ACS Table 4 normalizes to kcat 2.8 s^-1, Km 0.0053 mM, and kcat/Km 530 s^-1 mM^-1.

raw_value_unit_evidence: Official ACS Table 4 row DeltaN7: kcat 2.8 (0.1) s^-1; Km 5.3 (0.5) uM; kcat/Km 0.53 (0.2) uM^-1 s^-1.

row_label: DeltaN7 T4moD

table_label: Official ACS Table 4

substrate: Toluene

status: corrected


sequence_variant_note: Mutation signature ΔN4 is validated as an N-terminal deletion of the first 4 mature-chain residue(s) from ncbi_protein:AAS66663.1_mature_chain_2-103; the provided variant sequence equals the exact canonical suffix after that deletion.

column_label: Official ACS Table 4; row DeltaN4; columns kcat (s^-1), KM (uM), and kcat/KM (uM^-1 s^-1); captured publisher HTML table segment; footnotes a and c preserve assay and mature-chain deletion context.

normalized_value_unit_evidence: Official ACS Table 4 normalizes to kcat 3.4 s^-1, Km 0.0023 mM, and kcat/Km 1470 s^-1 mM^-1.

raw_value_unit_evidence: Official ACS Table 4 row DeltaN4: kcat 3.4 (0.2) s^-1; Km 2.3 (0.3) uM; kcat/Km 1.47 (0.6) uM^-1 s^-1.

row_label: DeltaN4 T4moD


enzyme_display_name: Heme-dependent oxidative N-demethylase alpha subunit

organism: Ectopseudomonas mendocina (strain ymp)

substrate_name: dimethylamine

substrate: dimethylamine


enzyme_display_name: Indole-3-acetate monooxygenase

organism: Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81)

substrate_name: indole

proof_lines: kcat is 0.88 min(-1) with indole as substrate.

enzyme: Indole-3-acetate monooxygenase

substrate: indole


substrate_name: NADH

substrate: NADH


enzyme_display_name: linalool 8-monooxygenase

organism: Pseudomonas putida

proof_lines: substrate-stimulated NADH oxidation using excess amounts of P-450 and FAD component of the enzyme

proof_lines: substrate-stimulated NADH oxidation using excess amounts of iron-sulfur and FAD component of the enzyme

proof_lines: substrate-stimulated NADH oxidation using excess amounts of iron sulfur and P-450 component of the enzyme

enzyme: linalool 8-monooxygenase


organism: Anthoceros agrestis

substrate_name: trans-cinnamate

substrate: trans-cinnamate


organism: Glycine max

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: trans-Cinnamate; NADPH; O2; H+

substrate: trans-Cinnamate; NADPH; O2; H+


enzyme_display_name: UniProt Q00456

organism: Pseudomonas mendocina

substrate_name: methyl 4-tolyl sulfide

enzyme: UniProt Q00456

substrate: methyl 4-tolyl sulfide


organism: Catharanthus roseus

substrate_name: H+; NADPH; 7-Deoxyloganate; O2

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

substrate: H+; NADPH; 7-Deoxyloganate; O2


substrate_name: O2; H+; NADPH; Liquiritigenin

substrate: O2; H+; NADPH; Liquiritigenin


substrate_name: H+; NADPH; O2; Biochanin A

assay_conditions_summary: pH 8; cofactor NADP+

column_label: Article prose states MtI3H kcat for biochanin A.

row_label: MtI3H / biochanin A

table_label: Kinetic properties prose section

substrate: H+; NADPH; O2; Biochanin A


substrate_name: O2; Formononetin; H+; NADPH

column_label: Article prose states MtI3H Km for formononetin.

raw_value_unit_evidence: Km 49.7 uM

row_label: MtI3H / formononetin

substrate: O2; Formononetin; H+; NADPH


enzyme_display_name: isoflavone 2'-hydroxylase

substrate_name: H+; Formononetin; NADPH; O2

enzyme: isoflavone 2'-hydroxylase

substrate: H+; Formononetin; NADPH; O2


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Helianthus tuberosus

substrate_name: H+; trans-Cinnamate; O2; NADPH

assay_conditions_summary: pH 7.4; cofactor NADPH

substrate: H+; trans-Cinnamate; O2; NADPH


enzyme_display_name: Ent-kaurene oxidase, chloroplastic

organism: Arabidopsis thaliana

substrate_name: ent-kaurene

column_label: Table 1 row ent-Kaurene (1), Km column: 1.8 +/- 0.6 uM

raw_value_unit_evidence: Km raw_value=1.8 +/- 0.6 raw_unit=uM

row_label: ent-Kaurene (1)

table_label: Table 1

enzyme: Ent-kaurene oxidase, chloroplastic

substrate: ent-kaurene


substrate_name: ent-kaurenol

column_label: Table 1 row ent-Kaurenol (2), Km column: 6 +/- 1 uM

raw_value_unit_evidence: Km raw_value=6 +/- 1 raw_unit=uM

row_label: ent-Kaurenol (2)

substrate: ent-kaurenol


substrate_name: ent-kaurenal

column_label: Table 1 row ent-Kaurenal (3), Km column: 1.9 +/- 0.2 uM

raw_value_unit_evidence: Km raw_value=1.9 +/- 0.2 raw_unit=uM

row_label: ent-Kaurenal (3)

substrate: ent-kaurenal


substrate_name: ent-isokaurene

column_label: Table 2 row ent-Isokaurene (5), Km column: 10 +/- 2 uM

raw_value_unit_evidence: Km raw_value=10 +/- 2 raw_unit=uM

row_label: ent-Isokaurene (5)

table_label: Table 2

substrate: ent-isokaurene


substrate_name: ent-beyerene

column_label: Table 2 row ent-Beyerene (9), Km column: 28 +/- 7 uM

raw_value_unit_evidence: Km raw_value=28 +/- 7 raw_unit=uM

row_label: ent-Beyerene (9)

substrate: ent-beyerene


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature ΔN7 with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature ΔN4 with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


substrate_name: H+; ent-Kaurene; NADPH; O2

unit: lgwedgeoneswedgeone

substrate: H+; ent-Kaurene; NADPH; O2


organism: Oryza sativa


substrate_name: trans-Cinnamate; H+; O2; NADPH

enzyme: trans-cinnamate 4-monooxygenase

substrate: trans-Cinnamate; H+; O2; NADPH


organism: Petroselinum crispum


substrate_name: Toluene

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T201A to reconstruct the assayed variant sequence.

substrate: Toluene


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T201G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T201S to reconstruct the assayed variant sequence.


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


enzyme_display_name: 7-deoxyloganic acid hydroxylase

substrate_name: 7-deoxyloganic acid

enzyme: 7-deoxyloganic acid hydroxylase

substrate: 7-deoxyloganic acid


substrate_name: NADPH

proof_lines:
CrDL7H
7-deoxyloganic acid
secologanin biosynthesis

substrate: NADPH


substrate_name: Biochanin A

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

column_label: PDF page 6 / journal page 476; row_label=MtI3'H (MtCYP81E9) / Biochanin A; column_label=Km and kcat kinetic prose; raw_value=112.6 uM and 0.1 s^-1; normalized_value=0.1126 mM and 0.1 s^-1; condition_label=2 mM NADPH, pH 8.0; captured_paper_segment=the kinetic paragraph pairs both values with MtI3'H Biochanin A.

normalized_value_unit_evidence: kcat normalized_value=0.1 normalized_unit=s^-1; Km normalized_value=0.1126 normalized_unit=mM; same-row kcat/Km normalized_value=0.8880994671403197 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Journal page 476 row MtI3'H/Biochanin A: Km raw_value=112.6 raw_unit=uM; kcat raw_value=0.1 raw_unit=s^-1.

row_label: MtI3'H (MtCYP81E9) / Biochanin A

table_label: Journal page 476, Kinetic properties of MtI2'H and MtI3'H; Table 1 enzyme/substrate context

substrate: Biochanin A


substrate_name: formononetin

substrate: formononetin


organism: Papaver somniferum


enzyme_display_name: Trans-cinnamate 4-monooxygenase

organism: Sorghum bicolor

substrate_name: trans-cinnamate

enzyme: Trans-cinnamate 4-monooxygenase

substrate: trans-cinnamate


substrate_name: 2-naphthoic acid

substrate: 2-naphthoic acid


substrate_name: chlorotoluron

column_label: Table 5; row Chlorotoluron; column Turnover (min^-1) = 0.014.

normalized_value_unit_evidence: kcat 0.000233 s^-1 from 0.014 min^-1 / 60; Km not required for this row.

raw_value_unit_evidence: Table 5 row Chlorotoluron reports Turnover 0.014 min^-1 and Kmapp 200 uM.

row_label: Chlorotoluron

table_label: Table 5. CYP73 kinetic constants for various substrates

substrate: chlorotoluron


column_label: Table 5; row 7-Methoxycoumarin; column Kmapp (uM) = 4000; column Turnover (min^-1) = 11.4.

normalized_value_unit_evidence: Km 4.0 mM; kcat 0.19 s^-1 from 11.4 min^-1 / 60; kcat/Km 0.0475 s^-1 mM^-1 from same-row central values.

raw_value_unit_evidence: Table 5 row 7-Methoxycoumarin reports Kmapp 4000 uM and Turnover 11.4 min^-1.


substrate_name: p-chloro-N-methylaniline

column_label: Table 5; row p-Chloro-N-methylaniline; column Kmapp (uM) = 1919; column Turnover (min^-1) = 142.

raw_value_unit_evidence: Table 5 row p-Chloro-N-methylaniline reports Kmapp 1919 uM and Turnover 142 min^-1.

row_label: p-Chloro-N-methylaniline

substrate: p-chloro-N-methylaniline


enzyme_display_name: benzoate 4-monooxygenase

organism: Cystobasidium minutum

substrate_name: cinnamate

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

proof_lines: reconstituted enzyme system consisting of benzoate 4-hydroxylase i.e. P450rm, cytochrome P450 reductase, NADPH and dilauroylphosphatidylcholine

enzyme: benzoate 4-monooxygenase

substrate: cinnamate


substrate_name: benzoate

substrate: benzoate


enzyme_display_name: toluene 4-monooxygenase

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Official ACS Table 4; row Native; columns kcat (s^-1), KM (uM), and kcat/KM (uM^-1 s^-1); captured publisher HTML table segment; footnote a preserves the assay condition.

normalized_value_unit_evidence: Official ACS Table 4 normalizes to kcat 3.3 s^-1, Km 0.007 mM, and kcat/Km 470 s^-1 mM^-1.

raw_value_unit_evidence: Official ACS Table 4 row Native: kcat 3.3 (0.1) s^-1; Km 7.0 (0.7) uM; kcat/Km 0.47 (0.1) uM^-1 s^-1.

row_label: Native T4moD

enzyme: toluene 4-monooxygenase


organism: Medicago truncatula

assay_conditions_summary: pH 8; cofactor NADPH

column_label: PDF page 6 / journal page 476; row_label=MtI2'H (MtCYP81E7) / formononetin; column_label=Km and kcat kinetic prose; raw_value=67 uM and 0.015 s^-1; normalized_value=0.067 mM and 0.015 s^-1; condition_label=2 mM NADPH, pH 8.0; captured_paper_segment=the kinetic paragraph pairs both values with MtI2'H formononetin.

normalized_value_unit_evidence: kcat normalized_value=0.015 normalized_unit=s^-1; Km normalized_value=0.067 normalized_unit=mM; same-row kcat/Km normalized_value=0.22388059701492535 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Journal page 476 row MtI2'H/formononetin: Km raw_value=67 raw_unit=uM; kcat raw_value=0.015 raw_unit=s^-1.

row_label: MtI2'H (MtCYP81E7) / formononetin


column_label: PDF page 6 / journal page 476; row_label=MtI2'H (MtCYP81E7) / Biochanin A; column_label=Km and kcat kinetic prose; raw_value=51 uM and 0.033 s^-1; normalized_value=0.051 mM and 0.033 s^-1; condition_label=2 mM NADPH, pH 8.0; captured_paper_segment=the kinetic paragraph pairs both values with MtI2'H Biochanin A.

normalized_value_unit_evidence: kcat normalized_value=0.033 normalized_unit=s^-1; Km normalized_value=0.051 normalized_unit=mM; same-row kcat/Km normalized_value=0.6470588235294118 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Journal page 476 row MtI2'H/Biochanin A: Km raw_value=51 raw_unit=uM; kcat raw_value=0.033 raw_unit=s^-1.

row_label: MtI2'H (MtCYP81E7) / Biochanin A


organism: Pseudomonas sp.

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Rhodotorula graminis


organism: Corydalis vaginans

substrate_name: cis-N-methylcanadine

substrate: cis-N-methylcanadine


enzyme_display_name: (S)-limonene 3-monooxygenase

organism: Mentha x piperita

substrate_name: (-)-limonene

enzyme: (S)-limonene 3-monooxygenase

substrate: (-)-limonene


organism: Cytospora rhizophorae

substrate_name: thioanisole

substrate: thioanisole


enzyme_display_name: Benzoate 4-monooxygenase bphA

organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)

enzyme: Benzoate 4-monooxygenase bphA


enzyme_display_name: Cytochrome P450 2C9

organism: Homo sapiens

substrate_name: S-mephenytoin

column_label: Abstract reports the Km value for S-mephenytoin was 1.25 mM with all five purified cytochrome P-450 preparations in the presence of cytochrome b5.

raw_value_unit_evidence: Km raw_value=1.25 mM raw_unit=mM

row_label: human liver microsomal cytochrome P-450 / S-mephenytoin

table_label: PubMed XML abstract PMID 3079764

enzyme: Cytochrome P450 2C9

substrate: S-mephenytoin


enzyme_display_name: Cytochrome P450 4F2

smiles: CCCCCCC(CCCCCCCCCCC(=O)[O-])O

proof_lines: kcat is 0.067 min(-1) with menaquinone-4 (MK-4) as substrate (PubMed:24138531). The omega-hydroxylation of VLCFAs follows dual-enzyme Michaelis-Menten kinetics, suggesting simultaneous binding of two substrate molecules. The high affinity M

enzyme: Cytochrome P450 4F2


smiles: CCCCCC=CCC=CC=CC(CC=CCCCC(=O)O)O


smiles: CCCCCC=CCC(C=CC=CCC=CCCCC(=O)O)O


substrate_name: leukotriene B4

smiles: CCCCCC=CCC(C=CC=CC=CC(CCCC(=O)O)O)O

substrate: leukotriene B4


substrate_name: lipoxin A4

smiles: CCCCCC(C=CC=CC=CC=CC(C(CCCC(=O)O)O)O)O

substrate: lipoxin A4


enzyme_display_name: Cytochrome P450 4F3

substrate_name: arachidonate

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

proof_lines: The omega-hydroxylation of VLCFAs follows dual-enzyme Michaelis-Menten kinetics, suggesting simultaneous binding of two substrate molecules. The high affinity Michaelis-Menten constants are shown.

enzyme: Cytochrome P450 4F3

substrate: arachidonate


organism: Aspergillus niger


smiles: C(CCCCCCCCCCC(=O)[O-])CCCCCCCCCCO


smiles: C(CCCCCCCCCCCCC(=O)[O-])CCCCCCCCCCCCO


substrate_name: docosanoate

smiles: CCCCCCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: docosanoate


substrate_name: tetracosanoate

smiles: CCCCCCCCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: tetracosanoate


substrate_name: hexacosanoate

smiles: CCCCCCCCCCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexacosanoate


enzyme_display_name: protopine 6-monooxygenase

organism: Eschscholzia californica

enzyme: protopine 6-monooxygenase


organism: Glycine max

proof_lines: enzyme from elicitor-treated soybean cells


substrate_name: H+; Benzoate; O2; NADPH

substrate: H+; Benzoate; O2; NADPH


enzyme_display_name: leukotriene-B4 20-monooxygenase

organism: Rattus norvegicus

substrate_name: H+; NADH; Leukotriene B4; O2

enzyme: leukotriene-B4 20-monooxygenase

substrate: H+; NADH; Leukotriene B4; O2


substrate_name: menaquinone-4 (MK-4)

substrate: menaquinone-4 (MK-4)


enzyme_display_name: Cytochrome P450 4F1

smiles: CCCCCC=CCC=CC=CC(CC=CCCCC(=O)[O-])O

enzyme: Cytochrome P450 4F1


organism: Curvularia lunata

substrate_name: Unknown

substrate: Unknown


substrate_name: H+; 20-CHO-Leukotriene B4; NADPH; O2

substrate: H+; 20-CHO-Leukotriene B4; NADPH; O2


enzyme_display_name: Cytochrome P450 4F4

enzyme: Cytochrome P450 4F4


substrate_name: H+; O2; NADPH; Protopine

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

substrate: H+; O2; NADPH; Protopine


substrate_name: 20-hydroxy-leukotriene B4

smiles: C(CCC=CCC(C=CC=CC=CC(CCCC(=O)O)O)O)CCO

column_label: Primary paper Table I has row 20-OH-LTB4, column Km (uM), value 6.5.

raw_value_unit_evidence: Table I row 20-OH-LTB4, column Km (uM): 6.5 uM.

table_label: Table I: Kinetic Parameters of P450 4F3-Catalyzed omega-Hydroxylation of Various Substrates

substrate: 20-hydroxy-leukotriene B4


substrate_name: lipoxin B4

smiles: CCCCCC(C(C=CC=CC=CC=CC(CCCC(=O)O)O)O)O

column_label: Primary paper Table I has row Lipoxin B4, column Km (uM), value 17.9.

raw_value_unit_evidence: Table I row Lipoxin B4, column Km (uM): 17.9 uM.

row_label: Lipoxin B4

substrate: lipoxin B4


smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)O)O

column_label: Primary paper Table I has row 5-HETE, column Km (uM), value 25.7.

raw_value_unit_evidence: Table I row 5-HETE, column Km (uM): 25.7 uM.


column_label: Primary paper Table I has row 12-HETE, column Km (uM), value 40.9.

raw_value_unit_evidence: Table I row 12-HETE, column Km (uM): 40.9 uM.


smiles: CCC=CCC=CCC=CCC=CC=CC(CCCC(=O)O)O

column_label: Primary paper Table I has row 5-HEPE, column Km (uM), value 49.5.

raw_value_unit_evidence: Table I reports 5-HEPE Km raw_value=49.5 raw_unit=uM.


column_label: Primary paper Table I has row 12-OH-C18:0, column Km (uM), value 14.2; results prose expands this row as 12-hydroxy-stearate.

raw_value_unit_evidence: Table I row 12-OH-C18:0, column Km (uM): 14.2 uM; adjacent results prose names the substrate 12-hydroxy-stearate.

row_label: 12-OH-C18:0 (12-hydroxy-stearate)


smiles: CCCCCCC(CC=CCCCCCCCC(=O)[O-])O

column_label: Primary paper Table I has row 12-OH-C18:1, column Km (uM), value 22.8; results prose expands this row as 12-hydroxy-oleate.

raw_value_unit_evidence: Table I row 12-OH-C18:1, column Km (uM): 22.8 uM; adjacent results prose names the substrate 12-hydroxy-oleate.

row_label: 12-OH-C18:1 (12-hydroxy-oleate)


substrate_name: alpha-tocopherol

substrate: alpha-tocopherol


substrate_name: gamma-tocopherol

substrate: gamma-tocopherol


enzyme_display_name: (S)-limonene 6-monooxygenase

organism: Mentha spicata

substrate_name: (-)-limonene

proof_lines:
Mentha spicata
(-)-limonene
trans-carveol

enzyme: (S)-limonene 6-monooxygenase

substrate: (-)-limonene


organism: Ammi majus

substrate_name: trans-cinnamate

substrate: trans-cinnamate


enzyme_display_name: amorpha-4,11-diene 12-monooxygenase

organism: Artemisia annua

substrate_name: artemisinic aldehyde

enzyme: amorpha-4,11-diene 12-monooxygenase

substrate: artemisinic aldehyde


substrate_name: dihydroartemisinic aldehyde

substrate: dihydroartemisinic aldehyde


enzyme_display_name: amorpha-4,11-diene 12 monooxygenase

enzyme: amorpha-4,11-diene 12 monooxygenase


substrate_name: protopine

substrate: protopine


enzyme_display_name: Protopine 6-monooxygenase

substrate_name: allocryptopine

enzyme: Protopine 6-monooxygenase

substrate: allocryptopine


substrate_name: picolinate

substrate: picolinate


substrate_name: nicotinate

substrate: nicotinate


enzyme_display_name: 2-hydroxyisoflavanone synthase

organism: Glycyrrhiza echinata

substrate_name: liquiritigenin

proof_lines:
Glycyrrhiza echinata
2-hydroxyisoflavanone synthase
liquiritigenin

enzyme: 2-hydroxyisoflavanone synthase

substrate: liquiritigenin


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Anthoceros agrestis

substrate_name: NADPH

column_label: Abstract reports apparent Km values were determined to be 60 microM and 5 microM for NADPH and cinnamic acid, respectively.

raw_value_unit_evidence: Km raw_value=60 microM raw_unit=microM

row_label: Anthoceros agrestis cinnamic acid 4-hydroxylase / NADPH

table_label: PubMed XML abstract PMID 12721853

enzyme: trans-cinnamate 4-monooxygenase

substrate: NADPH


enzyme_display_name: Trans-cinnamate 4-monooxygenase

organism: Helianthus tuberosus

substrate_name: 2-naphthoic acid

enzyme: Trans-cinnamate 4-monooxygenase

substrate: 2-naphthoic acid


enzyme_display_name: indoleamine 2,3-dioxygenase

proof_lines: 1 mM, competitive inhibition, 52% inhibition relative to L-tryptophan, 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37°C, 10 min

enzyme: indoleamine 2,3-dioxygenase


organism: Arabidopsis thaliana

assay_conditions_summary: 303.15 K; cofactor NADPH

proof_lines: 0.0005-0.04 mM substrate and 1 mM NADPH, at 30°C


substrate_name: 2-chlorocinnamic acid

substrate: 2-chlorocinnamic acid


substrate_name: 2-fluorocinnamic acid

substrate: 2-fluorocinnamic acid


substrate_name: 3-hydroxycinnamic acid

substrate: 3-hydroxycinnamic acid


substrate_name: (2E)-3-(2-nitrophenyl)prop-2-enoic acid

substrate: (2E)-3-(2-nitrophenyl)prop-2-enoic acid


enzyme_display_name: ent-kaurene monooxygenase

proof_lines: pH and temperature not specified in the publication

enzyme: ent-kaurene monooxygenase


proof_lines: pH not specified in the publication, temperature not specified in the publication


substrate_name: ent-sandaracopimaradiene

substrate: ent-sandaracopimaradiene


substrate_name: ent-cassadiene

substrate: ent-cassadiene


enzyme_display_name: methyl farnesoate epoxidase

organism: Locusta migratoria

substrate_name: methyl (2E,6E)-farnesoate

smiles: CC(=CCCC(=CCCC(=CC(=O)OC)C)C)C

enzyme: methyl farnesoate epoxidase

substrate: methyl (2E,6E)-farnesoate


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Pseudomonas aeruginosa

enzyme: protocatechuate 3,4-dioxygenase


substrate_name: protocatechuate

substrate: protocatechuate


smiles: O=O


enzyme_display_name: catechol 1,2-dioxygenase

enzyme: catechol 1,2-dioxygenase


substrate_name: catechol

substrate: catechol


enzyme_display_name: 6-hydroxynicotinate 3-monooxygenase

organism: Pseudomonas fluorescens

enzyme: 6-hydroxynicotinate 3-monooxygenase


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: catechol 2,3-dioxygenase

organism: Pseudomonas putida

enzyme: catechol 2,3-dioxygenase


enzyme_display_name: UniProt A2TEF2

organism: Leishmania infantum

substrate_name: obtusifoliol

enzyme: UniProt A2TEF2

substrate: obtusifoliol


substrate_name: lanosterol

substrate: lanosterol


enzyme_display_name: benzoate 1,2-dioxygenase

enzyme: benzoate 1,2-dioxygenase


substrate_name: NADH

substrate: NADH


substrate_name: NADH-cytochrome c reductase component

substrate: NADH-cytochrome c reductase component


enzyme_display_name: phenylacetyl-CoA 1,2-epoxidase

organism: Pseudomonas sp.

enzyme: phenylacetyl-CoA 1,2-epoxidase


substrate_name: epoxyphenylacetyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: epoxyphenylacetyl-CoA


substrate_name: NADPH

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: tryptophan 2-monooxygenase

organism: Pseudomonas savastanoi

substrate_name: L-tryptophan

proof_lines: pH 8.3, 25°C, cosubstrate: O2, mutant K365M

enzyme: tryptophan 2-monooxygenase

substrate: L-tryptophan


proof_lines: pH 8.3, 25°C, cosubstrate: O2, mutant W466F


enzyme_display_name: sterol 14alpha-demethylase

enzyme: sterol 14alpha-demethylase


organism: Malassezia globosa


substrate_name: eburicol

substrate: eburicol


enzyme_display_name: angelicin synthase

organism: Kitagawia praeruptora

substrate_name: (+)-columbianetin

enzyme: angelicin synthase

substrate: (+)-columbianetin


organism: Trypanosoma brucei


organism: Naegleria fowleri

proof_lines: recombinant His-tagged enzyme, pH 7.4, 37°C


organism: Aspergillus fumigatus

proof_lines: isozyme CYP51A, pH not specified in the publication, temperature not specified in the publication


organism: Pastinaca sativa

assay_conditions_summary: pH 7

proof_lines: pH 7.0, isopropyloxy-hydroxylation of substrate


enzyme_display_name: 5-epiaristolochene 1,3-dihydroxylase

organism: Nicotiana tabacum

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature S368T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368T, Substrate EA, Product CD; column Km (uM) = 15.18; column kcat (s^-1) = 0.037; column kcat/Km (s^-1/uM) = 0.0024. captured primary segment: Table II | enzyme S368T | substrate EA | product CD | Km 15.18 +/- 1.55 uM | kcat 0.037 +/- 0.001 s^-1 | kcat/Km 0.0024 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 15.18 uM; 1 uM is 1/1000 mM, so 15.18 / 1000 = 0.01518 mM; the exported value is 0.01518 mM. kcat: printed Table II kcat cell 0.037 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.037 s^(-1); the exported value is 0.037 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0024 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0024 x 1000 = 2.4 s^(-1)*mM^(-1); the exported value is 2.437417654808959 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.037 / 0.01518 = 2.437417654808959 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368T, Substrate EA, Product CD: Km = 15.18 uM; kcat = 0.037 s^-1; printed kcat/Km = 0.0024 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368T, Substrate EA, Product CD

enzyme: 5-epiaristolochene 1,3-dihydroxylase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature I486A to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row I486A, Substrate 1b(OH)EA, Product CD; column Km (uM) = 21.24; column kcat (s^-1) = 0.132; column kcat/Km (s^-1/uM) = 0.0062. captured primary segment: Table II | enzyme I486A | substrate 1b(OH)EA | product CD | Km 21.24 +/- 2.84 uM | kcat 0.132 +/- 0.008 s^-1 | kcat/Km 0.0062 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 21.24 uM; 1 uM is 1/1000 mM, so 21.24 / 1000 = 0.02124 mM; the exported value is 0.02124 mM. kcat: printed Table II kcat cell 0.132 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.132 s^(-1); the exported value is 0.132 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0062 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0062 x 1000 = 6.2 s^(-1)*mM^(-1); the exported value is 6.214689265536724 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.132 / 0.02124 = 6.214689265536724 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row I486A, Substrate 1b(OH)EA, Product CD: Km = 21.24 uM; kcat = 0.132 s^-1; printed kcat/Km = 0.0062 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row I486A, Substrate 1b(OH)EA, Product CD


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature S368A to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368A, Substrate EA, Product CD; column Km (uM) = 22.67; column kcat (s^-1) = 0.154; column kcat/Km (s^-1/uM) = 0.0068. captured primary segment: Table II | enzyme S368A | substrate EA | product CD | Km 22.67 +/- 4.00 uM | kcat 0.154 +/- 0.009 s^-1 | kcat/Km 0.0068 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 22.67 uM; 1 uM is 1/1000 mM, so 22.67 / 1000 = 0.022670000000000003 mM; the exported value is 0.02267 mM. kcat: printed Table II kcat cell 0.154 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.154 s^(-1); the exported value is 0.154 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0068 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0068 x 1000 = 6.8 s^(-1)*mM^(-1); the exported value is 6.793118659020732 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.154 / 0.022670000000000003 = 6.793118659020731 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368A, Substrate EA, Product CD: Km = 22.67 uM; kcat = 0.154 s^-1; printed kcat/Km = 0.0068 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368A, Substrate EA, Product CD


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -10, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme S386C, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row I486A, Substrate EA, Product 1b(OH)EA; column Km (uM) = 68.80; column kcat (s^-1) = 0.293; column kcat/Km (s^-1/uM) = 0.0043. captured primary segment: Table II | enzyme I486A | substrate EA | product 1b(OH)EA | Km 68.80 +/- 4.04 uM | kcat 0.293 +/- 0.010 s^-1 | kcat/Km 0.0043 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 68.80 uM; 1 uM is 1/1000 mM, so 68.80 / 1000 = 0.0688 mM; the exported value is 0.0688 mM. kcat: printed Table II kcat cell 0.293 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.293 s^(-1); the exported value is 0.293 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0043 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0043 x 1000 = 4.3 s^(-1)*mM^(-1); the exported value is 4.258720930232558 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.293 / 0.0688 = 4.258720930232558 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row I486A, Substrate EA, Product 1b(OH)EA: Km = 68.80 uM; kcat = 0.293 s^-1; printed kcat/Km = 0.0043 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row I486A, Substrate EA, Product 1b(OH)EA


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368T, Substrate 1b(OH)EA, Product CD; column Km (uM) = 9.97; column kcat (s^-1) = 0.482; column kcat/Km (s^-1/uM) = 0.0483. captured primary segment: Table II | enzyme S368T | substrate 1b(OH)EA | product CD | Km 9.97 +/- 1.14 uM | kcat 0.482 +/- 0.019 s^-1 | kcat/Km 0.0483 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 9.97 uM; 1 uM is 1/1000 mM, so 9.97 / 1000 = 0.009970000000000001 mM; the exported value is 0.00997 mM. kcat: printed Table II kcat cell 0.482 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.482 s^(-1); the exported value is 0.482 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0483 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0483 x 1000 = 48.300000000000004 s^(-1)*mM^(-1); the exported value is 48.34503510531595 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.482 / 0.009970000000000001 = 48.34503510531594 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368T, Substrate 1b(OH)EA, Product CD: Km = 9.97 uM; kcat = 0.482 s^-1; printed kcat/Km = 0.0483 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368T, Substrate 1b(OH)EA, Product CD


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row Wild-type, Substrate EA, Product CD; column Km (uM) = 19.18; column kcat (s^-1) = 0.493; column kcat/Km (s^-1/uM) = 0.0257. captured primary segment: Table II | enzyme Wild-type | substrate EA | product CD | Km 19.18 +/- 2.90 uM | kcat 0.493 +/- 0.039 s^-1 | kcat/Km 0.0257 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 19.18 uM; 1 uM is 1/1000 mM, so 19.18 / 1000 = 0.01918 mM; the exported value is 0.01918 mM. kcat: printed Table II kcat cell 0.493 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.493 s^(-1); the exported value is 0.493 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0257 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0257 x 1000 = 25.7 s^(-1)*mM^(-1); the exported value is 25.703858185610013 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.493 / 0.01918 = 25.703858185610013 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row Wild-type, Substrate EA, Product CD: Km = 19.18 uM; kcat = 0.493 s^-1; printed kcat/Km = 0.0257 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row Wild-type, Substrate EA, Product CD


sequence_variant_note: Mutation signature S386V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme S386V, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368A, Substrate 1b(OH)EA, Product CD; column Km (uM) = 6.20; column kcat (s^-1) = 0.581; column kcat/Km (s^-1/uM) = 0.0937. captured primary segment: Table II | enzyme S368A | substrate 1b(OH)EA | product CD | Km 6.20 +/- 0.47 uM | kcat 0.581 +/- 0.012 s^-1 | kcat/Km 0.0937 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 6.20 uM; 1 uM is 1/1000 mM, so 6.20 / 1000 = 0.006200000000000001 mM; the exported value is 0.0062 mM. kcat: printed Table II kcat cell 0.581 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.581 s^(-1); the exported value is 0.581 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0937 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0937 x 1000 = 93.7 s^(-1)*mM^(-1); the exported value is 93.70967741935483 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.581 / 0.006200000000000001 = 93.70967741935482 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368A, Substrate 1b(OH)EA, Product CD: Km = 6.20 uM; kcat = 0.581 s^-1; printed kcat/Km = 0.0937 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368A, Substrate 1b(OH)EA, Product CD


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row Wild-type, Substrate 1b(OH)EA, Product CD; column Km (uM) = 1.74; column kcat (s^-1) = 0.582; column kcat/Km (s^-1/uM) = 0.3344. captured primary segment: Table II | enzyme Wild-type | substrate 1b(OH)EA | product CD | Km 1.74 +/- 0.08 uM | kcat 0.582 +/- 0.006 s^-1 | kcat/Km 0.3344 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 1.74 uM; 1 uM is 1/1000 mM, so 1.74 / 1000 = 0.00174 mM; the exported value is 0.00174 mM. kcat: printed Table II kcat cell 0.582 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.582 s^(-1); the exported value is 0.582 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.3344 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.3344 x 1000 = 334.4 s^(-1)*mM^(-1); the exported value is 334.48275862068965 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.582 / 0.00174 = 334.48275862068965 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row Wild-type, Substrate 1b(OH)EA, Product CD: Km = 1.74 uM; kcat = 0.582 s^-1; printed kcat/Km = 0.3344 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row Wild-type, Substrate 1b(OH)EA, Product CD


organism: Zea mays

substrate_name: indole

proof_lines: native enzyme, in 50 mM potassium phosphate, pH 7.5, at 25°C

proof_lines: recombinant enzyme, in 50 mM potassium phosphate, pH 7.5, at 25°C

substrate: indole


proof_lines: isozyme CYP51B, pH not specified in the publication, temperature not specified in the publication


substrate_name: NADPH; O2; H+; Columbianetin

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: pH 7.0, anti-3'-hydroxylation of substrate

source_databases_merged: sabio_rk brenda uniprot

substrate: NADPH; O2; H+; Columbianetin


substrate_name: NADPH; H+; O2; 5-Epiaristolochene

assay_conditions_summary: cofactor NADPH

substrate: NADPH; H+; O2; 5-Epiaristolochene


enzyme_display_name: Lanosterol 14-alpha demethylase

organism: Homo sapiens

enzyme: Lanosterol 14-alpha demethylase


enzyme_display_name: Lanosterol 14-alpha demethylase CYP51

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Lanosterol 14-alpha demethylase CYP51


enzyme_display_name: premnaspirodiene oxygenase

organism: Hyoscyamus muticus

column_label: Table 1; row label HPO | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | EA | 2beta-(OH)EA': Km 3.3 uM; kcat 0.2 s^-1; kcat/Km 0.06 s^-1 uM^-1.

row_label: HPO | EA | 2beta-(OH)EA

enzyme: premnaspirodiene oxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V480I/A484I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V480I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V480I/A484I | EA | 2beta-(OH)EA': Km 2.5 uM; kcat 0.7 s^-1; kcat/Km 0.28 s^-1 uM^-1.

row_label: HPO, V480I/A484I | EA | 2beta-(OH)EA

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:A6YIH8 and applied mutation signature V482I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V482I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | EA | 2beta-(OH)EA': Km 17.9 uM; kcat 1.4 s^-1; kcat/Km 0.08 s^-1 uM^-1.

row_label: HPO, V482I | EA | 2beta-(OH)EA


substrate_name: valencene

column_label: Table 1; row label HPO | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | Valencene | beta-Nootkatol': Km 7.4 uM; kcat 1.9 s^-1; kcat/Km 0.26 s^-1 uM^-1.

row_label: HPO | Valencene | beta-Nootkatol

substrate: valencene


substrate_name: (-)-vetispiradiene

column_label: Table 1; row label HPO | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | PSD | Solavetivol': Km 14 uM; kcat 2.1 s^-1; kcat/Km 0.15 s^-1 uM^-1.

row_label: HPO | PSD | Solavetivol

substrate: (-)-vetispiradiene


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:A6YIH8 and applied mutation signature V482I/A484I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V482I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | EA | 2beta-(OH)EA': Km 4.3 uM; kcat 2.8 s^-1; kcat/Km 0.65 s^-1 uM^-1.

row_label: HPO, V482I/A484I | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | PSD | Solavetivol': Km 6.2 uM; kcat 3.8 s^-1; kcat/Km 0.61 s^-1 uM^-1.

row_label: HPO, V482I | PSD | Solavetivol


column_label: Table 3; row label HPO, V482I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | Valencene | beta-Nootkatol': Km 6.9 uM; kcat 5.1 s^-1; kcat/Km 0.74 s^-1 uM^-1.

row_label: HPO, V482I | Valencene | beta-Nootkatol


proof_lines: mutant enzyme V480I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30°C


proof_lines: mutant enzyme V480I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30°C


column_label: Table 3; row label HPO, V482I/A484I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | Valencene | beta-Nootkatol': Km 12.1 uM; kcat 15.9 s^-1; kcat/Km 1.31 s^-1 uM^-1.


column_label: Table 3; row label HPO, V482I/A484I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | PSD | Solavetivol': Km 13 uM; kcat 20.7 s^-1; kcat/Km 1.59 s^-1 uM^-1.

row_label: HPO, V482I/A484I | PSD | Solavetivol


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

column_label: Table 1 row Lanosterol; column group C. albicans; metric column K_M^a; footnote a gives uM.

normalized_value_unit_evidence: 15.0 uM = 0.015 mM, which does not match package Km 0.0063 mM.

raw_value_unit_evidence: Table 1 row Lanosterol, C. albicans CYP51 orthologue, K_M^a column: 15.0; footnote a = uM.

row_label: Lanosterol


column_label: Table 1 row Dihydrolanosterol; column group C. albicans; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Dihydrolanosterol, C. albicans CYP51 orthologue, K_M^a column: 25.0; footnote a = uM.

row_label: Dihydrolanosterol


column_label: Table 1 row 24-methyleneDHL; column group C. albicans; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row 24-methyleneDHL, C. albicans CYP51 orthologue, K_M^a column: 11.0; footnote a = uM.


column_label: Table 1 row Obtusifoliol; column group C. albicans; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Obtusifoliol, C. albicans CYP51 orthologue, K_M^a column: 28.5; footnote a = uM.

row_label: Obtusifoliol


substrate_name: NADPH; O2; Vetispiradiene

substrate: NADPH; O2; Vetispiradiene


substrate_name: NADPH; Vetispiradiene; O2

assay_conditions_summary: cofactor NADP+

substrate: NADPH; Vetispiradiene; O2


substrate_name: Obtusifoliol; NADPH; H+; O2

substrate: Obtusifoliol; NADPH; H+; O2


substrate_name: NADPH; H+; O2; Eburicol

substrate: NADPH; H+; O2; Eburicol


organism: Candida albicans

substrate_name: H+; Lanosterol; NADPH; O2

substrate: H+; Lanosterol; NADPH; O2


organism: Rattus norvegicus

substrate_name: Lanosterol; H+; NADPH; O2

substrate: Lanosterol; H+; NADPH; O2


substrate_name: lanosterol

column_label: Table 1 row Lanosterol; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Lanosterol, Human CYP51 orthologue, K_M^a column: 29; footnote a = uM.

substrate: lanosterol


column_label: Table 1 row Dihydrolanosterol; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Dihydrolanosterol, Human CYP51 orthologue, K_M^a column: 27; footnote a = uM.


column_label: Table 1 row 24-methyleneDHL; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row 24-methyleneDHL, Human CYP51 orthologue, K_M^a column: 32; footnote a = uM.


substrate_name: obtusifoliol

column_label: Table 1 row Obtusifoliol; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Obtusifoliol, Human CYP51 orthologue, K_M^a column: 32; footnote a = uM.

substrate: obtusifoliol


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row EA -> CD; raw Km cell 19.18 +/- 2.90 uM; normalized Km 0.01918 mM. EA is 5-epiaristolochene in the article text.

raw_value_unit_evidence: Km raw_value=19.18 +/- 2.90 raw_unit=uM

row_label: EA -> CD


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row 3alpha(OH)EA -> CD; raw Km cell 6.38 +/- 0.42 uM; normalized Km 0.00638 mM. 3alpha-hydroxy-EA is the 1-deoxycapsidiol monohydroxylated intermediate of capsidiol.

raw_value_unit_evidence: Km raw_value=6.38 +/- 0.42 raw_unit=uM

row_label: 3alpha(OH)EA -> CD


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row 1beta(OH)EA -> CD; raw Km cell 1.74 +/- 0.08 uM; normalized Km 0.00174 mM. 1beta-hydroxy-EA is the 3-deoxycapsidiol monohydroxylated intermediate of capsidiol.

raw_value_unit_evidence: Km raw_value=1.74 +/- 0.08 raw_unit=uM

row_label: 1beta(OH)EA -> CD


enzyme_display_name: UniProt P00183

organism: Pseudomonas putida

substrate_name: NADH

enzyme: UniProt P00183

substrate: NADH


substrate_name: imidazole

substrate: imidazole


enzyme_display_name: ecgonone synthase

organism: Atropa belladonna

enzyme: ecgonone synthase


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row I486A, Substrate 1b(OH)EA, Product CD; column Km (uM) = 21.24; column kcat (s^-1) = 0.132; column kcat/Km (s^-1/uM) = 0.0062. captured primary segment: Table II | enzyme I486A | substrate 1b(OH)EA | product CD | Km 21.24 +/- 2.84 uM | kcat 0.132 +/- 0.008 s^-1 | kcat/Km 0.0062 s^-1/uM

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row I486A, Substrate 1b(OH)EA, Product CD: Km = 21.24 uM; kcat = 0.132 s^-1; printed kcat/Km = 0.0062 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row I486A, Substrate 1b(OH)EA, Product CD


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368A, Substrate 1b(OH)EA, Product CD; column Km (uM) = 6.20; column kcat (s^-1) = 0.581; column kcat/Km (s^-1/uM) = 0.0937. captured primary segment: Table II | enzyme S368A | substrate 1b(OH)EA | product CD | Km 6.20 +/- 0.47 uM | kcat 0.581 +/- 0.012 s^-1 | kcat/Km 0.0937 s^-1/uM

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368A, Substrate 1b(OH)EA, Product CD: Km = 6.20 uM; kcat = 0.581 s^-1; printed kcat/Km = 0.0937 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368A, Substrate 1b(OH)EA, Product CD


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368T, Substrate 1b(OH)EA, Product CD; column Km (uM) = 9.97; column kcat (s^-1) = 0.482; column kcat/Km (s^-1/uM) = 0.0483. captured primary segment: Table II | enzyme S368T | substrate 1b(OH)EA | product CD | Km 9.97 +/- 1.14 uM | kcat 0.482 +/- 0.019 s^-1 | kcat/Km 0.0483 s^-1/uM

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368T, Substrate 1b(OH)EA, Product CD: Km = 9.97 uM; kcat = 0.482 s^-1; printed kcat/Km = 0.0483 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368T, Substrate 1b(OH)EA, Product CD


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row 1beta(OH)EA -> CD; raw cells kcat 0.582 +/- 0.006, Km 1.74 +/- 0.08 uM, kcat/Km 0.3344 s^-1/uM; normalized cells kcat 0.582 s^-1, Km 0.00174 mM, kcat/Km 334.4 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.582 normalized_unit=s^-1; Km normalized_value=0.00174 normalized_unit=mM; kcat/Km normalized_value=334.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.582 +/- 0.006 raw_unit=s^-1; Km raw_value=1.74 +/- 0.08 raw_unit=uM; kcat/Km raw_value=0.3344 raw_unit=s^-1*uM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature S368C to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368C, Substrate EA, Product 1b(OH)EA; column Km (uM) = 38.63; column kcat (s^-1) = 0.278; column kcat/Km (s^-1/uM) = 0.0072. captured primary segment: Table II | enzyme S368C | substrate EA | product 1b(OH)EA | Km 38.63 +/- 2.64 uM | kcat 0.278 +/- 0.008 s^-1 | kcat/Km 0.0072 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 38.63 uM; 1 uM is 1/1000 mM, so 38.63 / 1000 = 0.038630000000000005 mM; the exported value is 0.03863 mM. kcat: printed Table II kcat cell 0.278 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.278 s^(-1); the exported value is 0.278 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0072 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0072 x 1000 = 7.2 s^(-1)*mM^(-1); the exported value is 7.196479420139789 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.278 / 0.038630000000000005 = 7.196479420139788 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368C, Substrate EA, Product 1b(OH)EA: Km = 38.63 uM; kcat = 0.278 s^-1; printed kcat/Km = 0.0072 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368C, Substrate EA, Product 1b(OH)EA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature S368V to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368V, Substrate EA, Product 1b(OH)EA; column Km (uM) = 16.72; column kcat (s^-1) = 0.553; column kcat/Km (s^-1/uM) = 0.0331. captured primary segment: Table II | enzyme S368V | substrate EA | product 1b(OH)EA | Km 16.72 +/- 2.21 uM | kcat 0.553 +/- 0.025 s^-1 | kcat/Km 0.0331 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 16.72 uM; 1 uM is 1/1000 mM, so 16.72 / 1000 = 0.01672 mM; the exported value is 0.01672 mM. kcat: printed Table II kcat cell 0.553 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.553 s^(-1); the exported value is 0.553 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0331 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0331 x 1000 = 33.099999999999994 s^(-1)*mM^(-1); the exported value is 33.07416267942584 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.553 / 0.01672 = 33.07416267942584 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368V, Substrate EA, Product 1b(OH)EA: Km = 16.72 uM; kcat = 0.553 s^-1; printed kcat/Km = 0.0331 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368V, Substrate EA, Product 1b(OH)EA


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row I486A, Substrate EA, Product 1b(OH)EA; column Km (uM) = 68.80; column kcat (s^-1) = 0.293; column kcat/Km (s^-1/uM) = 0.0043. captured primary segment: Table II | enzyme I486A | substrate EA | product 1b(OH)EA | Km 68.80 +/- 4.04 uM | kcat 0.293 +/- 0.010 s^-1 | kcat/Km 0.0043 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 68.80 uM; 1 uM is 1/1000 mM, so 68.80 / 1000 = 0.0688 mM; the exported value is 0.069 mM. kcat: printed Table II kcat cell 0.293 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.293 s^(-1); the exported value is 0.293 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0043 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0043 x 1000 = 4.3 s^(-1)*mM^(-1); the exported value is 4.246376811594202 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.293 / 0.0688 = 4.258720930232558 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row I486A, Substrate EA, Product 1b(OH)EA: Km = 68.80 uM; kcat = 0.293 s^-1; printed kcat/Km = 0.0043 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row I486A, Substrate EA, Product 1b(OH)EA


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368A, Substrate EA, Product CD; column Km (uM) = 22.67; column kcat (s^-1) = 0.154; column kcat/Km (s^-1/uM) = 0.0068. captured primary segment: Table II | enzyme S368A | substrate EA | product CD | Km 22.67 +/- 4.00 uM | kcat 0.154 +/- 0.009 s^-1 | kcat/Km 0.0068 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 22.67 uM; 1 uM is 1/1000 mM, so 22.67 / 1000 = 0.022670000000000003 mM; the exported value is 0.023 mM. kcat: printed Table II kcat cell 0.154 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.154 s^(-1); the exported value is 0.154 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0068 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0068 x 1000 = 6.8 s^(-1)*mM^(-1); the exported value is 6.695652173913044 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.154 / 0.022670000000000003 = 6.793118659020731 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368A, Substrate EA, Product CD: Km = 22.67 uM; kcat = 0.154 s^-1; printed kcat/Km = 0.0068 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368A, Substrate EA, Product CD


normalized_value_unit_evidence: Km: printed Table II Km cell 38.63 uM; 1 uM is 1/1000 mM, so 38.63 / 1000 = 0.038630000000000005 mM; the exported value is 0.039 mM. kcat: printed Table II kcat cell 0.278 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.278 s^(-1); the exported value is 0.278 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0072 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0072 x 1000 = 7.2 s^(-1)*mM^(-1); the exported value is 7.128205128205129 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.278 / 0.038630000000000005 = 7.196479420139788 s^-1 mM^-1.

table_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM)


normalized_value_unit_evidence: Km: printed Table II Km cell 16.72 uM; 1 uM is 1/1000 mM, so 16.72 / 1000 = 0.01672 mM; the exported value is 0.017 mM. kcat: printed Table II kcat cell 0.553 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.553 s^(-1); the exported value is 0.553 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0331 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0331 x 1000 = 33.099999999999994 s^(-1)*mM^(-1); the exported value is 32.529411764705884 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.553 / 0.01672 = 33.07416267942584 s^-1 mM^-1.


enzyme_display_name: taxoid 7beta-hydroxylase

organism: Taxus cuspidata

substrate_name: (+)-taxusin

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: taxoid 7beta-hydroxylase

substrate: (+)-taxusin


enzyme_display_name: UniProt Q06069

organism: Priestia megaterium

enzyme: UniProt Q06069


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V480I/A484I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V480I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V480I/A484I | EA | 2beta-(OH)EA': Km 2.5 uM; kcat 0.7 s^-1; kcat/Km 0.28 s^-1 uM^-1.

row_label: HPO, V480I/A484I | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | EA | 2beta-(OH)EA': Km 17.9 uM; kcat 1.4 s^-1; kcat/Km 0.08 s^-1 uM^-1.

row_label: HPO, V482I | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | EA | 2beta-(OH)EA': Km 4.3 uM; kcat 2.8 s^-1; kcat/Km 0.65 s^-1 uM^-1.

row_label: HPO, V482I/A484I | EA | 2beta-(OH)EA


column_label: Table 1; row label HPO | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | EA | 2beta-(OH)EA': Km 3.3 uM; kcat 0.2 s^-1; kcat/Km 0.06 s^-1 uM^-1.

row_label: HPO | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | Valencene | beta-Nootkatol': Km 6.9 uM; kcat 5.1 s^-1; kcat/Km 0.74 s^-1 uM^-1.

row_label: HPO, V482I | Valencene | beta-Nootkatol


column_label: Table 3; row label HPO, V482I/A484I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | Valencene | beta-Nootkatol': Km 12.1 uM; kcat 15.9 s^-1; kcat/Km 1.31 s^-1 uM^-1.


column_label: Table 1; row label HPO | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | Valencene | beta-Nootkatol': Km 7.4 uM; kcat 1.9 s^-1; kcat/Km 0.26 s^-1 uM^-1.

row_label: HPO | Valencene | beta-Nootkatol


column_label: Table 3; row label HPO, V482I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | PSD | Solavetivol': Km 6.2 uM; kcat 3.8 s^-1; kcat/Km 0.61 s^-1 uM^-1.

row_label: HPO, V482I | PSD | Solavetivol


enzyme_display_name: taxoid 2alpha-hydroxylase

substrate_name: taxusin

enzyme: taxoid 2alpha-hydroxylase

substrate: taxusin


enzyme_display_name: Sterol 14-alpha demethylase cyp51B

organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

enzyme: Sterol 14-alpha demethylase cyp51B


column_label: PDF text lines 285-303 contain Table I. Rendered PDF page 4 visually confirms the Lanosterol row and Km (uM) column value 165.

normalized_value_unit_evidence: Lanosterol Km 165 uM normalizes to 0.165 mM, not the current 0.0105 mM.

raw_value_unit_evidence: Table I Lanosterol row reports Km 165 uM, Ki 100 uM, Vmax 3390 pmol/min/mg, Vmax/Km 20.5, accumulated oxysterol 25%.

row_label: Lanosterol

table_label: Table I. Kinetic constants and effect of mutual competitive inhibitors upon accumulation of oxysterol demethylation intermediates


column_label: PDF text lines 285-303 contain Table I. Rendered PDF page 4 visually confirms the Dihydrolanosterol row and Km (uM) column value 312.

normalized_value_unit_evidence: Dihydrolanosterol Km 312 uM normalizes to 0.312 mM, not the current 0.02 mM.

raw_value_unit_evidence: Table I Dihydrolanosterol row reports Km 312 uM, Ki 298 uM, Vmax 645 pmol/min/mg, Vmax/Km 2.1, accumulated oxysterol 15%.

row_label: Dihydrolanosterol


substrate_name: eburicol

substrate: eburicol


enzyme_display_name: UniProt P9WPP3

organism: Mycobacterium tuberculosis

substrate_name: 15-methylpalmitic acid

smiles: CC(C)CCCCCCCCCCCCCC(=O)O

enzyme: UniProt P9WPP3

substrate: 15-methylpalmitic acid


substrate_name: phytanic acid

smiles: CC(C)CCCC(C)CCCC(C)CCCC(C)CC(=O)O

substrate: phytanic acid


enzyme_display_name: UniProt P10614

organism: Saccharomyces cerevisiae

source_license: CC BY 4.0; CC BY-NC-ND 4.0

proof_lines: Yeast P-45014DM shows substrate-specific 14a-demethylation of 24-methylene-24,25-dihydrolanosterol and lanosterol.

source_databases_merged: skid uniprot

enzyme: UniProt P10614


organism: Papaver somniferum

substrate_name: (S)-N-methylcanadine

substrate: (S)-N-methylcanadine


substrate_name: (-)-vetispiradiene

column_label: Table 3; row label HPO, V482I/A484I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | PSD | Solavetivol': Km 13 uM; kcat 20.7 s^-1; kcat/Km 1.59 s^-1 uM^-1.

row_label: HPO, V482I/A484I | PSD | Solavetivol

substrate: (-)-vetispiradiene


column_label: Table 1; row label HPO | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | PSD | Solavetivol': Km 14 uM; kcat 2.1 s^-1; kcat/Km 0.15 s^-1 uM^-1.

row_label: HPO | PSD | Solavetivol


enzyme_display_name: Premnaspirodiene oxygenase

substrate_name: premnaspirodiene

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

column_label: Table 1; row label HPO | PSD | Solavetivol; required column Km (uM); substrate PSD; product/readout Solavetivol.

normalized_value_unit_evidence: Km 0.014 mM for the required metric; table also reports kcat 2.1 s^-1 and kcat/Km 150 s^-1 mM^-1.

enzyme: Premnaspirodiene oxygenase

substrate: premnaspirodiene


substrate_name: solavetivol

column_label: Table 1; row label HPO | Solavetivol | Solavetivone; required column Km (uM); substrate Solavetivol; product/readout Solavetivone.

normalized_value_unit_evidence: Km 0.0012 mM for the required metric; table also reports kcat 0.1 s^-1 and kcat/Km 80 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 'HPO | Solavetivol | Solavetivone': Km 1.2 uM; kcat 0.1 s^-1; kcat/Km 0.08 s^-1 uM^-1.

row_label: HPO | Solavetivol | Solavetivone

substrate: solavetivol


substrate_name: valencene

column_label: Table 1; row label HPO | Valencene | alpha-Nootkatol; required column Km (uM); substrate Valencene; product/readout alpha-Nootkatol.

normalized_value_unit_evidence: Km 0.0115 mM for the required metric; table also reports kcat 0.1 s^-1 and kcat/Km 10 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 'HPO | Valencene | alpha-Nootkatol': Km 11.5 uM; kcat 0.1 s^-1; kcat/Km 0.01 s^-1 uM^-1.

row_label: HPO | Valencene | alpha-Nootkatol

substrate: valencene


column_label: Table 1; row label HPO | EA | 2beta-(OH)EA; required column Km (uM); substrate EA; product/readout 2beta-(OH)EA.

normalized_value_unit_evidence: Km 0.0033 mM for the required metric; table also reports kcat 0.2 s^-1 and kcat/Km 60 s^-1 mM^-1.


column_label: Table 1; row label HPO | Cedr-8-ene | Cedr-8-en-15-ol; required column Km (uM); substrate Cedr-8-ene; product/readout Cedr-8-en-15-ol.

normalized_value_unit_evidence: Km 0.0265 mM for the required metric; table also reports kcat 0.1 s^-1 and kcat/Km 0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 'HPO | Cedr-8-ene | Cedr-8-en-15-ol': Km 26.5 uM; kcat 0.1 s^-1; kcat/Km 0 s^-1 uM^-1.

row_label: HPO | Cedr-8-ene | Cedr-8-en-15-ol


enzyme_display_name: UniProt P18326

organism: Streptomyces griseolus

substrate_name: 1alpha,25-dihydroxyvitamin D3

enzyme: UniProt P18326

substrate: 1alpha,25-dihydroxyvitamin D3


enzyme_display_name: UniProt P9WPP1

enzyme: UniProt P9WPP1


enzyme_display_name: (S)-N-methylcanadine 1-hydroxylase

substrate_name: (S)-N-Methylcanadine; H+; O2; NADPH

enzyme: (S)-N-methylcanadine 1-hydroxylase

substrate: (S)-N-Methylcanadine; H+; O2; NADPH


enzyme_display_name: UniProt F1CMX0

organism: Rhodococcus rhodochrous

enzyme: UniProt F1CMX0


enzyme_display_name: UniProt F1CMY8

enzyme: UniProt F1CMY8


enzyme_display_name: UniProt P71875

enzyme: UniProt P71875


substrate_name: testosterone

substrate: testosterone


enzyme_display_name: UniProt Q00441

organism: Saccharopolyspora erythraea

enzyme: UniProt Q00441


substrate_name: androstenedione

substrate: androstenedione


substrate_name: dehydroepiandrostenedione

substrate: dehydroepiandrostenedione


enzyme_display_name: sterol 14alpha-demethylase

substrate_name: lanosterol

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


substrate_name: obtusifoliol

substrate: obtusifoliol


enzyme_display_name: Rhazimal synthase

organism: Alstonia scholaris

substrate_name: geissoschizine

enzyme: Rhazimal synthase

substrate: geissoschizine


enzyme_display_name: 6-deoxyerythronolide B hydroxylase

organism: Actinopolyspora erythraea

substrate_name: 6-Deoxyerythronolide b

proof_lines: 30°C, pH not specified in the publication

enzyme: 6-deoxyerythronolide B hydroxylase

substrate: 6-Deoxyerythronolide b


enzyme_display_name: 3-ketosteroid 9alpha-monooxygenase

substrate_name: 3-oxo-23,24-bisnorchol-4-en-22-oic acid

enzyme: 3-ketosteroid 9alpha-monooxygenase

substrate: 3-oxo-23,24-bisnorchol-4-en-22-oic acid


assay_conditions_summary: pH 7; 295.15 K; cofactor CoA


enzyme_display_name: sterol 14alpha-demethylase (ferredoxin)

organism: Nocardia farcinica

proof_lines: wild-type, pH 7.0, temperature not specified in the publication

enzyme: sterol 14alpha-demethylase (ferredoxin)


proof_lines: FprD fusion construct F1, pH 7.0, temperature not specified in the publication

proof_lines: FprD fusion construct F2, pH 7.0, temperature not specified in the publication


organism: Sinomonas cyclohexanicum

proof_lines: pH and temperature not specified in the publication


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.9


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A245T to reconstruct the assayed variant sequence.

proof_lines: mutant A245T, pH 7.5, 37°C, S50 value, Hill coefficient 1.7


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.2


proof_lines: mutant A245T, pH 7.5, 37°C, S50 value, Hill coefficient 1.09


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.64


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.55


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 4-BNC (at pH 7 and at 22 degrees Celsius)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 2.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574). kcat is 0.8 sec(-1) for ADD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303). kcat is 0.61 sec(-1) for 4-BNC-CoA as su


substrate_name: 4-BNC-CoA (at pH 7 and at 22 degrees Celsius)


substrate_name: 1,4-BNC-CoA (at pH 7 and at 22 degrees Celsius)

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.


substrate_name: 1,4-BNC (at pH 7 and at 22 degrees Celsius)

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


enzyme_display_name: 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component

substrate: 4-BNC (at pH 7 and at 22 degrees Celsius)


enzyme: 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component

substrate: 4-BNC-CoA (at pH 7 and at 22 degrees Celsius)


substrate: 1,4-BNC-CoA (at pH 7 and at 22 degrees Celsius)


substrate: 1,4-BNC (at pH 7 and at 22 degrees Celsius)


substrate_name: AD (at pH 7 and at 25 degrees Celsius)

substrate: AD (at pH 7 and at 25 degrees Celsius)


proof_lines: kcat is 1.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.8 sec(-1) for 5alpha-androstan-3,17-dione, AD and testosterone as substrates (at pH 7.0 and 22 degrees Celsius). kcat is 0.7 sec(-1) for ADD as s


proof_lines: kcat is 2.6 sec(-1) for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.4 sec(-1) for testosterone as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.3 sec(-1) for ADD as substrate (at pH 7.0 and 22 degrees Celsius)


enzyme_display_name: Pentalenene oxygenase

organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

substrate_name: active enantiomer of pentalenene

proof_lines: kcat is 0.503 min(-1) with active enantiomer of pentalenene as substrate.

enzyme: Pentalenene oxygenase

substrate: active enantiomer of pentalenene


enzyme_display_name: L-tyrosine 3-nitrase

organism: Streptomyces atratus

substrate_name: Nle-RYLH

proof_lines: kcat is 0.25 min(-1) with Nle-RYLH as substrate.

enzyme: L-tyrosine 3-nitrase

substrate: Nle-RYLH


enzyme_display_name: pentalenene oxygenase

organism: Streptomyces avermitilis

substrate_name: (+/-)-pentalenene

assay_conditions_summary: pH 7.4; 295.15 K; buffer phosphate

proof_lines: recombinant enzyme, in 50 mM phosphate buffer, 10% (v/v) glycerol, pH 7.4, at 22°C

enzyme: pentalenene oxygenase

substrate: (+/-)-pentalenene


enzyme_display_name: UniProt P04176

organism: Rattus norvegicus

substrate_name: L-phenylalanine

enzyme: UniProt P04176

substrate: L-phenylalanine


enzyme_display_name: UniProt P30967

organism: Chromobacterium violaceum

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P30967


substrate_name: L-tryptophan

substrate: L-tryptophan


enzyme_display_name: UniProt P00439

organism: Homo sapiens

substrate_name: S-carboxymethyl-L-cysteine

smiles: C(C(C(=O)O)N)SCC(=O)O

enzyme: UniProt P00439

substrate: S-carboxymethyl-L-cysteine


substrate_name: (S)-methyl-L-cysteine

smiles: CNC(CS)C(=O)O

substrate: (S)-methyl-L-cysteine


substrate_name: S-methyl-L-cysteine

smiles: CSCC(C(=O)O)N

substrate: S-methyl-L-cysteine


substrate_name: N-acetyl-S-carboxymethyl-L-cysteine

smiles: CC(=O)NC(CSCC(=O)O)C(=O)O

substrate: N-acetyl-S-carboxymethyl-L-cysteine


substrate_name: N-acetyl-S-methyl-L-cysteine

smiles: CC(=O)NC(CSC)C(=O)O

substrate: N-acetyl-S-methyl-L-cysteine


enzyme_display_name: UniProt P17752

enzyme: UniProt P17752


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


enzyme_display_name: UniProt P70080

organism: Gallus gallus

enzyme: UniProt P70080


organism: Aeromicrobium erythreum

substrate_name: 6-Deoxyerythronolide b

proof_lines: 30°C, pH not specified in the publication

substrate: 6-Deoxyerythronolide b


enzyme_display_name: Cytochrome P450 monooxygenase PikC

organism: Streptomyces venezuelae

substrate_name: narbomycin

enzyme: Cytochrome P450 monooxygenase PikC

substrate: narbomycin


organism: Mycobacterium tuberculosis


organism: Rhodococcus rhodochrous

column_label: Table 2 identifies 5alpha-androstane-3,17-dione substrate row; adjacent Results prose reports Km = 23 +/- 2 uM

raw_value_unit_evidence: Results prose adjacent to Table 2; 5alpha-androstane-3,17-dione Km = 23 +/- 2 uM

table_label: Table 2. Steroid substrate range of the KSH enzyme of R. rhodochrous DSM 43269


organism: Saccharopolyspora erythraea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I379V to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH not specified in the publication, mutant enzyme I379V


proof_lines: 30°C, pH not specified in the publication, wild-type enzyme


column_label: Table 2 identifies 19-nor-AD / nordion substrate row; adjacent Results prose reports Km = 10 +/- 1 uM

raw_value_unit_evidence: Results prose adjacent to Table 2; 19-nor-AD / nordion Km = 10 +/- 1 uM


substrate_name: nordion

substrate: nordion


substrate_name: 3-oxo-23,24-bisnorchol-4-en-22-oic acid

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

proof_lines: in 0.1 M potassium phosphate, pH 7.0, at 22°C

substrate: 3-oxo-23,24-bisnorchol-4-en-22-oic acid


proof_lines: apparent Km value, in the presence of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA, in 0.1 M potassium phosphate, pH 7.0, at 22°C

proof_lines: in the presence of 1,4-androstadiene-3,17-dione, kcat above 7 1/sec, in 0.1 M potassium phosphate, pH 7.0, at 25°C

proof_lines: in the presence of 1,4-androstadiene-3,17-dione, Km above 1.2 mM, in 0.1 M potassium phosphate, pH 7.0, at 25°C


assay_conditions_summary: pH 7; 295.15 K; buffer 50mMTris-HCl

proof_lines:
pH 7.0, 22°C
isoform KshA5, at pH 7.0 and 22°C
isoform KshA1, at pH 7.0 and 22°C


substrate_name: testosterone

substrate: testosterone


enzyme_display_name: catechol 1,2-dioxygenase

organism: Ralstonia sp.

enzyme: catechol 1,2-dioxygenase


substrate_name: catechol

substrate: catechol


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: NADPH

enzyme: nitric-oxide synthase (NADPH)

substrate: NADPH


enzyme_display_name: catechol 2,3-dioxygenase

organism: Stutzerimonas stutzeri

enzyme: catechol 2,3-dioxygenase


organism: Sus scrofa

substrate_name: dichlorophenolindophenol

substrate: dichlorophenolindophenol


substrate_name: nitroblue tetrazolium

substrate: nitroblue tetrazolium


substrate_name: L-arginine

smiles: C(CC(C(=O)O)N)CN=C(N)N

substrate: L-arginine


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase

organism: Zea mays

enzyme: 9-cis-epoxycarotenoid dioxygenase


enzyme_display_name: homogentisate 1,2-dioxygenase

organism: Aspergillus niger

substrate_name: homogentisate

enzyme: homogentisate 1,2-dioxygenase

substrate: homogentisate


enzyme_display_name: gibberellin 3beta-dioxygenase

organism: Arabidopsis sp.

substrate_name: gibberellin a9

enzyme: gibberellin 3beta-dioxygenase

substrate: gibberellin a9


substrate_name: gibberellin a20

substrate: gibberellin a20


enzyme_display_name: indole-3-pyruvate monooxygenase

organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: in the presence of phenylpyruvate, in 50 mM sodium phosphate, pH 8.0, 500 mM NaCl, and 30% (v/v) glycerol, at 25°C

enzyme: indole-3-pyruvate monooxygenase


substrate_name: phenylpyruvate

proof_lines: in the presence of NADPH, in 50 mM sodium phosphate, pH 8.0, 500 mM NaCl, and 30% (v/v) glycerol, at 25°C

substrate: phenylpyruvate


enzyme_display_name: nitric-oxide synthase (flavodoxin)

organism: Bacillus subtilis

enzyme: nitric-oxide synthase (flavodoxin)


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


enzyme_display_name: peptide-aspartate beta-dioxygenase

organism: Bos taurus

proof_lines:
56 kDa protein
52 kDa protein

enzyme: peptide-aspartate beta-dioxygenase


enzyme_display_name: taurine dioxygenase

organism: Escherichia coli

proof_lines: wild type enzyme, in the presence of taurine

enzyme: taurine dioxygenase


substrate_name: taurine

proof_lines:
wild type enzyme
wild-type, 30°C

substrate: taurine


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Desulfovibrio desulfuricans

substrate_name: ferrocytochrome c3

proof_lines:
H2-evolution assay
tetraheme cytochrome c3
nonaheme cytochrome c

enzyme: cytochrome-c3 hydrogenase

substrate: ferrocytochrome c3