substrate_name: reduced methyl viologen

substrate: reduced methyl viologen


enzyme_display_name: alkanesulfonate monooxygenase

organism: Escherichia coli

substrate_name: octanesulfonate

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

enzyme: alkanesulfonate monooxygenase

substrate: octanesulfonate

status: unverified

source: brenda


substrate_name: NADH

mutation_signature: Unknown

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

assay_conditions_summary: pH 7.4; 295.15 K; cofactor NADH

proof_lines: pH 7.4, 22°C, recombinant wild-type enzyme

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 295.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Felis catus

substrate_name: L-arginine

kcat_display: Not reported

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

assay_conditions_summary: cofactor FAD

proof_lines:
with FAD and tetrahydropterin
without tetrahydropterin and FAD

enzyme: nitric-oxide synthase (NADPH)

substrate: L-arginine


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: cysteine dioxygenase

organism: Histoplasma capsulatum

substrate_name: L-cysteine

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

enzyme: cysteine dioxygenase

substrate: L-cysteine


substrate_name: beta-mercaptoethanol

smiles: C(CS)O

substrate: beta-mercaptoethanol


organism: Homo sapiens


enzyme_display_name: arachidonate 15-lipoxygenase

substrate_name: lipoic acid

enzyme: arachidonate 15-lipoxygenase

substrate: lipoic acid


substrate_name: arachidonic acid

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

proof_lines:
splice variant 15-LOb1
splice variant 15-LOb2

substrate: arachidonic acid


enzyme_display_name: UniProt P14925

organism: Rattus norvegicus

substrate_name: N-(Phenylacetyl)glycine

source_db: skid

protein_accession_database: UniProt

source_license: CC BY-NC-ND 4.0

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

data_origin: experimental

enzyme: UniProt P14925

substrate: N-(Phenylacetyl)glycine

source: skid


substrate_name: hippuryl-Gly-Gly

substrate: hippuryl-Gly-Gly


substrate_name: hippuric acid

substrate: hippuric acid


substrate_name: 4-hydroxyhippuric acid

substrate: 4-hydroxyhippuric acid


substrate_name: isocaproylglycine

smiles: CC(C)CCC(=O)NCC(=O)O

substrate: isocaproylglycine


substrate_name: 3-chlorohippuric acid

substrate: 3-chlorohippuric acid


substrate_name: phenylmercaptoacetylglycine

substrate: phenylmercaptoacetylglycine


substrate_name: 2-aminohippuric acid

substrate: 2-aminohippuric acid


substrate_name: 3-methylhippuric acid

substrate: 3-methylhippuric acid


substrate_name: 4-methylhippuric acid

substrate: 4-methylhippuric acid


substrate_name: cinnamoylglycine

substrate: cinnamoylglycine


substrate_name: nicotinuric acid

substrate: nicotinuric acid


substrate_name: 2-methylhippuric acid

substrate: 2-methylhippuric acid


substrate_name: 4-chlorohippuric acid

substrate: 4-chlorohippuric acid


substrate_name: 4-methoxyhippuric acid

substrate: 4-methoxyhippuric acid


substrate_name: CBZ-glycine

substrate: CBZ-glycine


substrate_name: 4-nitrohippuric acid

substrate: 4-nitrohippuric acid


substrate_name: phenylthioacetylglycine

substrate: phenylthioacetylglycine


substrate_name: phenylhydantoic acid

substrate: phenylhydantoic acid


substrate_name: 2-hydroxyhippuric acid

substrate: 2-hydroxyhippuric acid


substrate_name: N-dansyl-Tyr-Val-D-Ala

substrate: N-dansyl-Tyr-Val-D-Ala


substrate_name: hydrocinnamoylglycine

substrate: hydrocinnamoylglycine


substrate_name: 4-aminohippuric acid

substrate: 4-aminohippuric acid


substrate_name: 2-iodohippuric acid

substrate: 2-iodohippuric acid


substrate_name: CBZ-D-alanine

substrate: CBZ-D-alanine


substrate_name: 2,6-difluorohippuric acid

substrate: 2,6-difluorohippuric acid


substrate_name: benzoyl-D-alanine

substrate: benzoyl-D-alanine


substrate_name: N-acetylglycine

smiles: CC(=O)NCC(=O)O

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6
Raw SKiD Env: Temp=-----, pH=-----

substrate: N-acetylglycine


enzyme_display_name: tyrosinase

organism: Streptomyces antibioticus

enzyme: tyrosinase


organism: Neurospora crassa

substrate_name: D-Tyr

substrate: D-Tyr


substrate_name: tyramine

substrate: tyramine


substrate_name: 4-hydroxyphenyl acetic acid

substrate: 4-hydroxyphenyl acetic acid


substrate_name: L-Dopa

substrate: L-Dopa


organism: Triticum aestivum


enzyme_display_name: UniProt B2ZB02

organism: Priestia megaterium

enzyme: UniProt B2ZB02


substrate_name: L-tyrosine

substrate: L-tyrosine


enzyme_display_name: UniProt C0LU17

organism: Juglans regia

enzyme: UniProt C0LU17


enzyme_display_name: UniProt C7FF04

organism: Agaricus bisporus

substrate_name: deoxyarbutin

enzyme: UniProt C7FF04

substrate: deoxyarbutin


substrate_name: beta-arbutin

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7

substrate: beta-arbutin


enzyme_display_name: trimethylamine monooxygenase

substrate_name: Methimazole

enzyme: trimethylamine monooxygenase

substrate: Methimazole


enzyme_display_name: homogentisate 1,2-dioxygenase

enzyme: homogentisate 1,2-dioxygenase


substrate_name: homogentisate

substrate: homogentisate


organism: Carthamus tinctorius

smiles: O=O


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: O2; Arachidonate

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

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: arachidonate 12-lipoxygenase

substrate: O2; Arachidonate


enzyme_display_name: indoleamine 2,3-dioxygenase

proof_lines:
pH 6.5, 25°C, recombinant enzyme IDO1
recombinant enzyme
37°C, pH 6.5

enzyme: indoleamine 2,3-dioxygenase


proof_lines: pH and temperature not specified in the publication


substrate_name: 5,8,11,14,17-eicosapentaenoic acid

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

substrate: 5,8,11,14,17-eicosapentaenoic acid


substrate_name: 8,11,14-eicosatrienoic acid

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

substrate: 8,11,14-eicosatrienoic acid


substrate_name: L-tryptophan

assay_conditions_summary: pH 8

proof_lines: H76A mutant enzyme, pH 8.0, normal atmospheric conditions

substrate: L-tryptophan


proof_lines: Y42F mutant enzyme, pH 8.0, normal atmospheric conditions


substrate_name: arachidonic acid

assay_conditions_summary: pH 7.5; 288.15 K; buffer 25 mM Hepes

proof_lines:
at 15°C, pH 7.5
at 40°C, pH 7.5

substrate: arachidonic acid


assay_conditions_summary: pH 7.5; 298.15 K; buffer 25 mM Hepes

proof_lines: with arachidonic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid

proof_lines: with linoleic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid


substrate_name: Benzydamine

assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.1 M tricine

proof_lines: in in 0.1 M tricine buffer, pH 7.4, at 37°C

substrate: Benzydamine


substrate_name: sulindac sulfide

assay_conditions_summary: pH 9; 310.15 K; buffer 0.1 M tricine

proof_lines: in in 0.1 M tricine buffer, pH 9.0, at 37°C

substrate: sulindac sulfide


substrate_name: D-tryptophan

substrate: D-tryptophan


proof_lines: recombinant wild-type enzyme, pH 7.4, 25°C

proof_lines: wild type, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min


enzyme_display_name: 4alpha-methylsterol monooxygenase

enzyme: 4alpha-methylsterol monooxygenase


enzyme_display_name: UniProt E9P162

organism: Streptomyces toxytricini

substrate_name: anthranilamide

enzyme: UniProt E9P162

substrate: anthranilamide


substrate_name: kynurenine

substrate: kynurenine


enzyme_display_name: tryptophan 6-halogenase

organism: Streptomyces albogriseolus

enzyme: tryptophan 6-halogenase


substrate_name: bromide

substrate: bromide


substrate_name: chloride

substrate: chloride


enzyme_display_name: sphingolipid C4-monooxygenase

organism: Zea mays

substrate_name: NADPH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

enzyme: sphingolipid C4-monooxygenase

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

substrate: NADH


substrate_name: D-erythro-sphinganine

smiles: CCCCCCCCCCCCCCCC(C(CO)N)O

substrate: D-erythro-sphinganine


enzyme_display_name: pseudobaptigenin synthase

organism: Cicer arietinum

substrate_name: Pratensein

enzyme: pseudobaptigenin synthase

substrate: Pratensein


substrate_name: Calycosin

substrate: Calycosin


assay_conditions_summary: pH 7.5; 285.15 K; cofactor NADPH

proof_lines: pH 7.5, 12°C, 5-hydroxypseudobaptigenin synthesis

proof_lines: pH 7.5, 12°C, pseudobaptigenin synthesis


enzyme_display_name: tryptophan 5-halogenase

organism: Xenorhabdus szentirmaii

proof_lines: with chloride as cosubstrate, at pH 7.4 and 37°C

enzyme: tryptophan 5-halogenase


enzyme_display_name: (S)-cheilanthifoline synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

enzyme: (S)-cheilanthifoline synthase

substrate: (S)-scoulerine


enzyme_display_name: sterol 22-desaturase

organism: Nakaseomyces glabratus

verification_status: verified

assay_conditions_summary: pH 6.8; cofactor NADPH

column_label: Abstract reports enzyme kinetic studies revealed a Km for ergosta-5,7-dienol of 12.5 microM.

raw_value_unit_evidence: Km raw_value=12.5 microM raw_unit=microM

row_label: Candida glabrata sterol delta22-desaturase / ergosta-5,7-dienol

table_label: PubMed XML abstract PMID 10390230

enzyme: sterol 22-desaturase

status: verified


organism: uncultured bacterium


enzyme_display_name: UniProt P18548

organism: Streptomyces clavuligerus

substrate_name: Penicillin N

enzyme: UniProt P18548

substrate: Penicillin N


substrate_name: penicillin G

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

substrate: penicillin G


substrate_name: ampicillin

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

substrate: ampicillin


enzyme_display_name: 1,2-dehydroreticuline synthase

organism: Papaver rhoeas

substrate_name: (S)-reticuline

assay_conditions_summary: pH 7.8; cofactor NADPH

proof_lines: pH 7.8, temperature not specified in the publication

enzyme: 1,2-dehydroreticuline synthase

substrate: (S)-reticuline


verification_status: corrected

column_label: Table 2, Kinetics of selected substrates with SttH wild type; row=kynurenine (4); metric columns=Km [uM], kcat [min^-1], kcat/Km [min^-1 mM^-1].

normalized_value_unit_evidence: Normalized values from the primary table: Km 0.241 mM; kcat 0.51/60 = 0.0085 s^-1; kcat/Km 2.1/60 = 0.035 s^-1 mM^-1.

row_label: kynurenine (4)

table_label: Table 2

status: corrected


column_label: Table 2, Kinetics of selected substrates with SttH wild type; row=anthranilamide (5); metric columns=Km [uM], kcat [min^-1], kcat/Km [min^-1 mM^-1].

row_label: anthranilamide (5)


enzyme_display_name: all-trans-retinol 3,4-desaturase

organism: Danio rerio

substrate_name: all-trans-retinal

sequence_source: multiple

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

source_databases_merged: brenda uniprot

enzyme: all-trans-retinol 3,4-desaturase

substrate: all-trans-retinal


substrate_name: all-trans-retinoic acid

substrate: all-trans-retinoic acid


substrate_name: all-trans-retinol

substrate: all-trans-retinol


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Actinomyces sp.

enzyme: deacetoxycephalosporin-C synthase


enzyme_display_name: (S)-canadine synthase

organism: Thalictrum tuberosum

substrate_name: (S)-tetrahydrocolumbamine

proof_lines: canadine synthase in complex with a cytochrome P-450 reductase

enzyme: (S)-canadine synthase

substrate: (S)-tetrahydrocolumbamine


substrate_name: [reduced NADPH-hemoprotein reductase]

assay_conditions_summary: cofactor NADPH

substrate: [reduced NADPH-hemoprotein reductase]


enzyme_display_name: salutaridine synthase

organism: Sus scrofa

substrate_name: (R)-reticuline

enzyme: salutaridine synthase

substrate: (R)-reticuline


organism: Hapsidospora chrysogena

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M306I to reconstruct the assayed variant sequence.

proof_lines: 30°C, double mutant with truncation at residue 310 and M306I


sequence_variant_note: Mutation signature M306I/N305L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: 30°C, triple mutant with truncation at residue 310, M306I and N305L


sequence_variant_note: Mutation signature N305L/M306I could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 30°C, recombinant mutant DELTA310/N305L/M306I


kcat_over_km_origin: calculated

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

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R308L to reconstruct the assayed variant sequence.

proof_lines: mutant R308L, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R308I to reconstruct the assayed variant sequence.

proof_lines: mutant R308I, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: Noroxomaritidine synthase

organism: Narcissus aff. pseudonarcissus MK-2014

source_db: uniprot

assay_conditions_summary: pH 6.5; buffer 200 mM KPO4 pH 6.5

column_label: Table 5 row 4'-O-Methylnorbelladine, column Km (uM) = 1.13 +/- 0.54.

normalized_value_unit_evidence: Required Km: 1.13 uM = 0.00113 mM. Kcat and kcat/Km are present in the table but not required for this UniProt row.

raw_value_unit_evidence: Table 5 4'-O-Methylnorbelladine row: Km 1.13 +/- 0.54 uM; kcat 15.0 +/- 2.03 1/min; kcat/Km 13 1/uM*min; modifications monitored: C-C phenol coupling.

table_label: Table 5. Substrate specificity tests for CYP96T1.

enzyme: Noroxomaritidine synthase

source: uniprot


substrate_name: (S)-coclaurine

column_label: Table 5 row (S)-Coclaurine, column Km (uM) = 637 +/- 156.

normalized_value_unit_evidence: Required Km: 637 uM = 0.637 mM. Kcat and kcat/Km are present in the table but not required for this UniProt row.

raw_value_unit_evidence: Table 5 (S)-Coclaurine row: Km 637 +/- 156 uM; kcat 1.34 +/- 0.15 1/min; kcat/Km 2.11 x 10^-3 1/uM*min; modifications monitored: intramolecular phenol coupling and intermolecular coupling.

row_label: (S)-Coclaurine

substrate: (S)-coclaurine


enzyme_display_name: sn-1 linoleoyl-lipid 6-desaturase

organism: Limnospira platensis

substrate_name: linoleic acid

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

enzyme: sn-1 linoleoyl-lipid 6-desaturase

substrate: linoleic acid


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


organism: Homo sapiens

proof_lines: pH 7.4, temperature not specified in the publication


enzyme_display_name: biflaviolin synthase

organism: Streptomyces coelicolor

substrate_name: flaviolin

proof_lines: wild type isoform CYP158A2, at pH 8.2 and 37°C

enzyme: biflaviolin synthase

substrate: flaviolin


proof_lines: wild type isoform CYP158A1, at pH 8.2 and 37°C


enzyme_display_name: UniProt Q9FCA6

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

proof_lines: kcat is 1.4 min(-1) with flaviolin as substrate (at pH 7.5 and 37 degrees Celsius). kcat is 0.02 min(-1) with 2-hydroxy-1,4-naphthoquinone as substrate (at pH 7.5 and 25 degrees Celsius).

source_databases_merged: skid uniprot

enzyme: UniProt Q9FCA6


enzyme_display_name: UniProt Q9KZF5

proof_lines: kcat is 0.9 min(-1) with flaviolin as substrate (at pH 8.2 and 37 degrees Celsius).

enzyme: UniProt Q9KZF5


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R307L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N305L with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


enzyme_display_name: tryptophan 6-halogenase

organism: Streptomyces toxytricini

substrate_name: kynurenine

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

enzyme: tryptophan 6-halogenase

substrate: kynurenine


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: anthranilamide

substrate: anthranilamide


enzyme_display_name: Tryptophan 6-halogenase SttH

proof_lines: kcat is 1.53 min(-1) with L-tryptophan as substrate (PubMed:21424165). kcat is 0.65 min(-1) with tryptophan as substrate (PubMed:26840773). kcat is 0.51 min(-1) with kynurenine as substrate (PubMed:26840773). kcat is 1.21 min(-1) with anthr

enzyme: Tryptophan 6-halogenase SttH


enzyme_display_name: 2-hydroxy fatty acid dioxygenase

organism: Saccharomyces cerevisiae

substrate_name: (2R)-2-hydroxypalmitic acid

smiles: CCCCCCCCCCCCCCC(C(=O)O)O

enzyme: 2-hydroxy fatty acid dioxygenase

substrate: (2R)-2-hydroxypalmitic acid


enzyme_display_name: tetracycline 7-halogenase

organism: Kitasatospora aureofaciens

proof_lines: kcat is 0.51 min(-1) for tetracycline (TC) as substrate.

enzyme: tetracycline 7-halogenase


organism: Papaver somniferum

proof_lines: pH 7.8, temperature not specified in the publication

proof_lines: Cyp82Y2 module, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: 7-chloro-L-tryptophan 6-halogenase

organism: Kutzneria sp. 744

assay_conditions_summary: pH 7; cofactor NADH

column_label: Prose states the KtzR kcat ratio for 7-Cl-L-Trp/L-Trp is 1.4 min^-1/0.08 min^-1 and the Km value for 7-Cl-L-Trp is 114 uM versus 808 uM for L-Trp.

normalized_value_unit_evidence: kcat normalized=0.0013 s^-1; Km normalized=0.808 mM; kcat/Km normalized=0.0016089108910891088 s^-1 mM^-1

raw_value_unit_evidence: kcat raw=0.08 min^-1; Km raw=808 uM; kcat/Km raw=computed from same prose kcat and Km

row_label: KtzR with L-Trp as halogenation substrate

table_label: PMC full text Results prose, KtzR kinetic characterization

enzyme: 7-chloro-L-tryptophan 6-halogenase


normalized_value_unit_evidence: kcat normalized=0.023 s^-1; Km normalized=0.114 mM; kcat/Km normalized=0.20175438596491227 s^-1 mM^-1

raw_value_unit_evidence: kcat raw=1.4 min^-1; Km raw=114 uM; kcat/Km raw=computed from same prose kcat and Km

row_label: KtzR with 7-Cl-L-Trp as halogenation substrate


enzyme_display_name: tryptophan 5-halogenase

organism: Streptomyces rugosporus

proof_lines:
pH 7.2, 30°C
Raw SKiD Env: Temp=30°C, pH=7.2
kcat is 3.56 min(-1).

source_databases_merged: brenda skid uniprot

enzyme: tryptophan 5-halogenase


enzyme_display_name: camalexin synthase

organism: Arabidopsis thaliana

proof_lines: pH and temperature not specified in the publication

enzyme: camalexin synthase


proof_lines: kcat is 1.64 min(-1) for (R)-reticuline.


enzyme_display_name: (S)-cheilanthifoline synthase

organism: Argemone mexicana

substrate_name: (S)-scoulerine

enzyme: (S)-cheilanthifoline synthase

substrate: (S)-scoulerine


column_label: Abstract reports recombinant CYP719A21 displayed strict substrate specificity and high affinity (Km=4.63+/-0.71 microM) for (S)-tetrahydrocolumbamine.

raw_value_unit_evidence: Km raw_value=4.63+/-0.71 microM raw_unit=microM

row_label: recombinant CYP719A21 / (S)-tetrahydrocolumbamine

table_label: PubMed XML abstract PMID 24316226


enzyme_display_name: Pluviatolide synthase

organism: Podophyllum peltatum

substrate_name: (-)-matairesinol

proof_lines: kcat is 7.8 min(-1) with (-)-matairesinol as substrate.

enzyme: Pluviatolide synthase

substrate: (-)-matairesinol


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Streptomyces clavuligerus

substrate_name: O2; Penicillin N; 2-Oxoglutarate

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

enzyme: deacetoxycephalosporin-C synthase

substrate: O2; Penicillin N; 2-Oxoglutarate


assay_conditions_summary: pH 6


enzyme_display_name: Trifunctional (S)-stylopine synthase/(S)-nandinine synthase/(S)-canadine synthase

substrate_name: Unknown

proof_lines: kcat is 13.8 min(-1) for (S)-cheilanthifoline.

substrate: Unknown


enzyme_display_name: (S)-canadine synthase CYP719A21

enzyme: (S)-canadine synthase CYP719A21


organism: Cephalosporium acremonium

substrate_name: O2; 2-Oxoglutarate; Penicillin G

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

substrate: O2; 2-Oxoglutarate; Penicillin G


assay_conditions_summary: pH 7.2; 303.15 K; buffer potassium phosphate

proof_lines: wild type enzyme, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y454F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y454F, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E46Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E46Q, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F49A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F49A, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


enzyme_display_name: (S)-stylopine synthase

substrate_name: (S)-cheilanthifoline

enzyme: (S)-stylopine synthase

substrate: (S)-cheilanthifoline


enzyme_display_name: Cheilanthifoline synthase

enzyme: Cheilanthifoline synthase


organism: Sinopodophyllum hexandrum

proof_lines: kcat is 14.9 min(-1) with (-)-matairesinol as substrate.


enzyme_display_name: noroxomaritidine synthase

source_db: oed

column_label: Table 5; row 4′ -O-Methyl-N-methylnorbelladine; column Km (uM) cell 3.28 +/- 2.27; column kcat (1/min) cell 2.44 +/- 0.54; column kcat/Km (1/uM*min) cell 0.742; column Modifications monitored cell C-C phenol coupling.

raw_value_unit_evidence: Table 5 row 4′ -O-Methyl-N-methylnorbelladine: Km (µM) 3.28 +/- 2.27; kcat (1/min) 2.44 +/- 0.54; kcat/Km (1/µM*min) 0.742; Modifications monitored C-C phenol coupling.

row_label: 4′ -O-Methyl-N-methylnorbelladine

table_label: Table 5 | Substrate specificity tests for CYP96T1.

enzyme: noroxomaritidine synthase

source: oed


column_label: Table 5; row 4′ -O-Methylnorbelladine; column Km (uM) cell 1.13 +/- 0.54; column kcat (1/min) cell 15.0 +/- 2.03; column kcat/Km (1/uM*min) cell 13; column Modifications monitored cell C-C phenol coupling.

normalized_value_unit_evidence: Km 1.13 uM = 1.13/1000 = 0.00113 mM. kcat 15.0 1/min = 15.0/60 = 0.25 s^-1. kcat/Km recorded here is this same Table 5 row's kcat divided by its Km, 0.25 / 0.00113 = 221.23893805309734 s^-1*mM^-1; the table's own efficiency column prints 13 1/uM*min, which equals 216.66666666666666 s^-1*mM^-1 at the rounded precision the table prints.

raw_value_unit_evidence: Table 5 row 4′ -O-Methylnorbelladine: Km (µM) 1.13 +/- 0.54; kcat (1/min) 15.0 +/- 2.03; kcat/Km (1/µM*min) 13; Modifications monitored C-C phenol coupling.

row_label: 4′ -O-Methylnorbelladine


substrate_name: (R)-coclaurine

column_label: Table 5; row (R)-Coclaurine; column Km (uM) cell 659 +/- 104; column kcat (1/min) cell 2.07 +/- 0.14; column kcat/Km (1/uM*min) cell 3.15 × 10−3; column Modifications monitored cell Intramolecular phenol coupling and Intermolecular coupling.

normalized_value_unit_evidence: Km 659 uM = 659/1000 = 0.659 mM. kcat 2.07 1/min = 2.07/60 = 0.0345 s^-1. kcat/Km recorded here is this same Table 5 row's kcat divided by its Km, 0.0345 / 0.659 = 0.05235204855842185 s^-1*mM^-1; the table's own efficiency column prints 3.15 × 10−3 1/uM*min, which equals 0.0525 s^-1*mM^-1 at the rounded precision the table prints.

raw_value_unit_evidence: Table 5 row (R)-Coclaurine: Km (µM) 659 +/- 104; kcat (1/min) 2.07 +/- 0.14; kcat/Km (1/µM*min) 3.15 × 10−3; Modifications monitored Intramolecular phenol coupling and Intermolecular coupling.

row_label: (R)-Coclaurine

substrate: (R)-coclaurine


substrate_name: (S)-Coclaurine

column_label: Table 5; row (S)-Coclaurine; column Km (uM) cell 637 +/- 156; column kcat (1/min) cell 1.34 +/- 0.15; column kcat/Km (1/uM*min) cell 2.11 × 10−3; column Modifications monitored cell Intramolecular phenol coupling and Intermolecular coupling.

raw_value_unit_evidence: Table 5 row (S)-Coclaurine: Km (µM) 637 +/- 156; kcat (1/min) 1.34 +/- 0.15; kcat/Km (1/µM*min) 2.11 × 10−3; Modifications monitored Intramolecular phenol coupling and Intermolecular coupling.

substrate: (S)-Coclaurine


substrate_name: Ampicillin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258A to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258A mutant

substrate: Ampicillin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258F to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258F mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258H to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258H mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258K to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258K mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258L to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258L mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258Q to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258Q mutant


substrate_name: Penicillin G

substrate: Penicillin G


proof_lines:
deacetoxycephalosporin-C synthase
R258 mutants
2-oxoacid cosubstrate selectivity


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

assay_conditions_summary: pH 7; 295.15 K; cofactor NADH


organism: Pseudomonas syringae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H116Q to reconstruct the assayed variant sequence.

smiles: O=C(O)CCC(=O)C(=O)O


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H168Q 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 H169Q 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 H268Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H284Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H305Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H309Q with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H335Q to reconstruct the assayed variant sequence.


organism: Pseudomonas savastanoi pv. phaseolicola


substrate_name: L-arginine

substrate: L-arginine


substrate_name: 2-Hydroxymyristate; O2

smiles: CCCCCCCCCCCCC(C(=O)O)O

substrate: 2-Hydroxymyristate; O2


organism: Oryctolagus cuniculus

substrate_name: O2; H+; 7alpha-Hydroxycholest-4-en-3-one; NADPH


enzyme_display_name: methylsterol monooxygenase

organism: Rattus norvegicus

substrate_name: H+; NADH; O2; 5alpha-Cholest-7-ene-3-one-4alpha-carbaldehyde

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

enzyme: methylsterol monooxygenase


enzyme_display_name: all-trans-retinol 3,4-desaturase

organism: Homo sapiens

substrate_name: all-trans-retinoic acid from cellular retinoic acid-binding protein-2

enzyme: all-trans-retinol 3,4-desaturase


substrate_name: all-trans-retinaldehyde from cellular retinol-binding protein-1


enzyme_display_name: salutaridine synthase

substrate_name: [reduced NADPH-hemoprotein reductase]

enzyme: salutaridine synthase

substrate: [reduced NADPH-hemoprotein reductase]


enzyme_display_name: (S)-canadine synthase

organism: Coptis japonica

enzyme: (S)-canadine synthase


enzyme_display_name: Methylsterol monooxygenase 1

enzyme: Methylsterol monooxygenase 1


enzyme_display_name: Cytochrome P450 710A1

substrate_name: beta-sisterol

enzyme: Cytochrome P450 710A1

substrate: beta-sisterol


enzyme_display_name: sterol 22-desaturase

organism: Saccharomyces cerevisiae

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

enzyme: sterol 22-desaturase


enzyme_display_name: Cytochrome P450 710A11

organism: Solanum lycopersicum

enzyme: Cytochrome P450 710A11


enzyme_display_name: Noroxomaritidine synthase

organism: Narcissus aff. pseudonarcissus MK-2014

proof_lines: kcat is 15.0 min(-1) with 4'-O-methylnorbelladine as substrate. kcat is 2.44 min(-1) with 4'-O-methyl-N-methylnorbelladine as substrate. kcat is 1.34 min(-1) with (S)-coclaurine as substrate. kcat is 2.07 min(-1) with (R)-coclaurine as subs

enzyme: Noroxomaritidine synthase


enzyme_display_name: tryptophan 5-halogenase

substrate_name: L-tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E46D with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E46D, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C

enzyme: tryptophan 5-halogenase

substrate: L-tryptophan


organism: Hapsidospora chrysogena


substrate_name: Penicillin N

substrate: Penicillin N


enzyme_display_name: 2-hydroxy-palmitic acid dioxygenase MPO1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

smiles: CCCCCCCCCCCCCCC(C(=O)[O-])O


enzyme_display_name: UniProt P05979

organism: Ovis aries

enzyme: UniProt P05979


enzyme_display_name: UniProt P23219

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

enzyme: UniProt P23219


substrate_name: cis-5,8,11,14,17-eicosapentaenoic acid

substrate: cis-5,8,11,14,17-eicosapentaenoic acid


substrate_name: alpha-linolenic acid

smiles: CCC=CCC=CCC=CCCCCCCCC(=O)O

substrate: alpha-linolenic acid


substrate_name: cis-5,8,11,14-eicosatetraenoic acid

substrate: cis-5,8,11,14-eicosatetraenoic acid


substrate_name: linoleic acid

substrate: linoleic acid


substrate_name: cis-11,14-eicosadienoic acid

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

substrate: cis-11,14-eicosadienoic acid


substrate_name: cis-7,10,13,16-docosatetraenoic acid

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

substrate: cis-7,10,13,16-docosatetraenoic acid


substrate_name: gamma-linolenic acid

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

substrate: gamma-linolenic acid


enzyme_display_name: UniProt P35354

enzyme: UniProt P35354


substrate_name: cis-8,11,14-eicosatrienoic acid

substrate: cis-8,11,14-eicosatrienoic acid


enzyme_display_name: UniProt Q05769

organism: Mus musculus

substrate_name: arachidonate

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

enzyme: UniProt Q05769

substrate: arachidonate


column_label: PubMed abstract metric sentence gives Km for CYP61 sterol delta22-desaturation as 20.4 microM, normalized to 0.0204 mM

normalized_value_unit_evidence: PubMed abstract Km normalized_value=0.0204 normalized_unit=mM

raw_value_unit_evidence: PubMed abstract: The enzyme kinetics associated with its endogenous role in sterol Delta22-desaturation revealed a Km of 20.4 microM and a Vmax of 2.9nmol/min/nmol CYP61

row_label: CYP61 sterol delta22-desaturation Km sentence

table_label: PubMed abstract


enzyme_display_name: Trifunctional (S)-stylopine synthase 2/(S)-nandinine synthase/(S)-canadine synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

column_label: PMID 17250743 substrate-affinity section, CYP719A3 / (S)-scoulerine row/segment, Km = 0.54 +/- 0.03 uM.

raw_value_unit_evidence: CYP719A3 Km for (S)-scoulerine was 0.54 +/- 0.03 uM.

row_label: CYP719A3 / (S)-scoulerine

table_label: Substrate-affinity section for CYP719A3 toward (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: (S)-stylopine synthase 1

substrate_name: (R,S)-scoulerine

enzyme: (S)-stylopine synthase 1

substrate: (R,S)-scoulerine


organism: Arthrobacter sp.


substrate_name: beta-sitosterol

substrate: beta-sitosterol


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Amycolatopsis lactamdurans

substrate_name: oxoglutarate

assay_conditions_summary: pH 7

column_label: Captured primary-paper prose: The apparent Km for 2-oxoglutarate was 3 uM.

raw_value_unit_evidence: Km raw_value=3 raw_unit=uM for 2-oxoglutarate.

row_label: 2-oxoglutarate varied from 1 to 50 uM

table_label: Primary-paper Results prose: Kinetics of the DAOC synthase, journal pages 3169-3171

enzyme: deacetoxycephalosporin-C synthase

substrate: oxoglutarate


column_label: Captured primary-paper prose: For penicillin N, the apparent Km was 52 uM.

raw_value_unit_evidence: Km raw_value=52 raw_unit=uM for penicillin N.

row_label: Penicillin N varied from 0.01 to 0.15 mM


enzyme_display_name: sn-1 linoleoyl-lipid 6-desaturase

organism: Limnospira platensis

substrate_name: linoleate

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

enzyme: sn-1 linoleoyl-lipid 6-desaturase

substrate: linoleate


enzyme_display_name: beta-carotene 15,15'-monooxygenase

substrate_name: beta-carotene

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

proof_lines: recombinant His6-tagged enzyme, pH and temperature not specified in the publication

enzyme: beta-carotene 15,15'-monooxygenase

substrate: beta-carotene


enzyme_display_name: UniProt G2LET6

organism: Chloracidobacterium thermophilum

substrate_name: hercynine

enzyme: UniProt G2LET6

substrate: hercynine


substrate_name: gamma-L-glutamyl-L-cysteine

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

substrate: gamma-L-glutamyl-L-cysteine


enzyme_display_name: kynurenine 7,8-hydroxylase

organism: Unknown

substrate_name: Unknown

source_db: unknown

source_license: see source

enzyme: kynurenine 7,8-hydroxylase

substrate: Unknown

source: unknown


assay_conditions_summary: cofactor NADH


enzyme_display_name: all-trans-retinol 3,4-desaturase

substrate_name: all-trans-retinol

enzyme: all-trans-retinol 3,4-desaturase

substrate: all-trans-retinol


enzyme_display_name: Corytuberine synthase

substrate_name: (R,S)-reticuline

enzyme: Corytuberine synthase

substrate: (R,S)-reticuline


enzyme_display_name: gamma-glutamyl hercynylcysteine S-oxide synthase

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

proof_lines: mutant D52L, pH not specified in the publication, temperature not specified in the publication


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

enzyme: gamma-glutamyl hercynylcysteine S-oxide synthase


proof_lines: mutant A420Y, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication


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


organism: Erwinia tasmaniensis

substrate_name: histamine

substrate: histamine


substrate_name: L-histidinamide

substrate: L-histidinamide


substrate_name: D-histidine

substrate: D-histidine


substrate_name: L-cysteine

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

substrate: L-cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K108F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K108L to reconstruct the assayed variant sequence.


proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme


enzyme_display_name: Bifunctional protein STORR

organism: Papaver somniferum

enzyme: Bifunctional protein STORR


enzyme_display_name: lytic cellulose monooxygenase (C1-hydroxylating)

organism: Thermothelomyces thermophilus

substrate_name: cellulose

substrate: cellulose


organism: Talaromyces amestolkiae

smiles: OO

enzyme: lytic cellulose monooxygenase (C1-hydroxylating)


proof_lines: variant lacking the C-terminal linker-like region, pH 6, 23°C

proof_lines: variant with an additional C-terminal carbohydrate binding domain, pH 6, 23°C


enzyme_display_name: Hercynine oxygenase

organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

enzyme: Hercynine oxygenase


enzyme_display_name: UniProt G7CFI3

organism: Mycolicibacterium thermoresistibile

proof_lines: kcat is 0.87 sec(-1) for the oxidative sulfurization of hercynine with gamma-L-glutamyl-L-cysteine as sulfur donor. kcat is 0.25 sec(-1) for the oxidative sulfurization of hercynine with N-glutaryl-cysteine as sulfur donor.

enzyme: UniProt G7CFI3


enzyme_display_name: UniProt Q9UBK8

organism: Homo sapiens

substrate_name: 3-acetylpyridine adenine dinucleotide phosphate

enzyme: UniProt Q9UBK8


substrate_name: menadione

substrate: menadione


substrate_name: doxorubicin

substrate: doxorubicin


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 8

proof_lines: pH 8.0, 26°C, recombinant enzyme mutant Y377F

proof_lines: pH 6.0, 26°C, recombinant enzyme mutant Y377F


organism: Trichoderma reesei


organism: Thermothielavioides terrestris


substrate_name: gamma-L-glutamyl-cysteine

substrate: gamma-L-glutamyl-cysteine


organism: Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)


enzyme_display_name: hercynylcysteine S-oxide synthase

organism: Neurospora crassa

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

enzyme: hercynylcysteine S-oxide synthase


column_label: Table 1 row D-Histidine (9) reports kcat = 7.8 x 10^-1 s^-1 and KM = 6.7 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: kcat normalized_value=0.78 normalized_unit=s^-1; Km normalized_value=0.67 normalized_unit=mM; kcat_over_km normalized_value=1.164179104477612 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=7.8 x 10^-1 raw_unit=s^-1; Km raw_value=6.7 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.67 mM

row_label: Sulphur acceptor / D-Histidine (9)

table_label: Table 1. Michaelis-Menten parameters of OvoA catalyzed sulphurization of imidazole derivatives


column_label: Table 1 row Histamine (7) reports kcat = 3.6 x 10^-1 s^-1 and KM = 2.3 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: kcat normalized_value=0.36 normalized_unit=s^-1; Km normalized_value=0.23 normalized_unit=mM; kcat_over_km normalized_value=1.5652173913043477 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=3.6 x 10^-1 raw_unit=s^-1; Km raw_value=2.3 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.23 mM

row_label: Sulphur acceptor / Histamine (7)


column_label: Table 1 row L-Histidinamide (6) reports kcat = 5.7 x 10^-1 s^-1 and KM = 3.1 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: kcat normalized_value=0.57 normalized_unit=s^-1; Km normalized_value=0.31 normalized_unit=mM; kcat_over_km normalized_value=1.8387096774193548 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=5.7 x 10^-1 raw_unit=s^-1; Km raw_value=3.1 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.31 mM

row_label: Sulphur acceptor / L-Histidinamide (6)


substrate_name: L-histidine

column_label: Table 1 row L-Histidine (5) reports KM = 3.4 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: Km normalized_value=0.34 normalized_unit=mM; kcat_over_km normalized_value=9.999999999999998 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=3.4 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.34 mM

row_label: Sulphur acceptor / L-Histidine (5)

substrate: L-histidine


substrate_name: L-Cysteine

column_label: Table 1 row L-Cysteine reports KM = 3.5 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: Km normalized_value=0.35 normalized_unit=mM; kcat_over_km normalized_value=9.428571428571429 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=3.5 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.35 mM

row_label: Sulphur donor / L-Cysteine

substrate: L-Cysteine


enzyme_display_name: tryptophan 5-halogenase

organism: Streptomyces rugosporus

substrate_name: L-tryptophan

enzyme: tryptophan 5-halogenase

substrate: L-tryptophan


enzyme_display_name: superoxide dismutase

organism: Psidium guajava

substrate_name: riboflavin

enzyme: superoxide dismutase

substrate: riboflavin


substrate_name: Nitro blue tetrazolium

substrate: Nitro blue tetrazolium


enzyme_display_name: Transferred entry: 1.21.3.10

enzyme: Transferred entry: 1.21.3.10


enzyme_display_name: tryptophan 6-halogenase

organism: Streptomyces toxytricini

enzyme: tryptophan 6-halogenase


enzyme_display_name: mercury(II) reductase

organism: Azotobacter chroococcum

substrate_name: Hg

smiles: [Hg]

enzyme: mercury(II) reductase

substrate: Hg


enzyme_display_name: diferric-transferrin reductase

organism: Mycobacterium avium subsp. paratuberculosis

substrate_name: ferric ammonium citrate

enzyme: diferric-transferrin reductase

substrate: ferric ammonium citrate


organism: Yersinia enterolytica


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus

substrate_name: NADH

substrate: NADH


organism: Penicillium sp.


enzyme_display_name: Mercuric reductase

organism: Lysinibacillus sphaericus

enzyme: Mercuric reductase


enzyme_display_name: Mycocyclosin synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: cYY (at pH7.2 and 30 degrees Celsius)

enzyme: Mycocyclosin synthase

substrate: cYY (at pH7.2 and 30 degrees Celsius)


enzyme_display_name: Trifunctional (S)-stylopine synthase 2/(S)-nandinine synthase/(S)-canadine synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: Sarpagan bridge enzyme 1

organism: Rauvolfia serpentina

substrate_name: geissoschizine

column_label: Article results prose states Rs_12057 and Gs_207-0.13 exhibited Michaelis-Menten kinetics with apparent KM values of 22.5 uM and 35.3 uM, respectively, for geissoschizine.

raw_value_unit_evidence: apparent KM value of 22.5 uM for Rs_12057 with geissoschizine

row_label: Rs_12057 / RsSBE with geissoschizine

table_label: Results prose, Supplementary Figure 8

enzyme: Sarpagan bridge enzyme 1

substrate: geissoschizine


organism: Benthodytes marianensis

substrate_name: superoxide

substrate: superoxide


enzyme_display_name: Superoxide dismutase [Mn/Fe]

organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: superoxide (at pH 9.5, with the Fe-SOD form)

column_label: Abstract states the Michaelis constant for the Fe-superoxide dismutase was Km = 0.54 mmol/l at pH 9.5.

raw_value_unit_evidence: Km raw_value=0.54 raw_unit=mmol/l

row_label: Propionibacterium shermanii Fe-superoxide dismutase with superoxide

table_label: PubMed/PMC abstract PMID 7575431

enzyme: Superoxide dismutase [Mn/Fe]


organism: Metallosphaera sedula

assay_conditions_summary: pH 6.7; 310.15 K; cofactor NADPH

column_label: PMC Results prose states Hg2+ Km values of 400 and 150 uM at 37 and 70 C, respectively; Table 1 M. sedula row lists Hg Km 400a/150b and specific activity 1.9a/3.1b.

raw_value_unit_evidence: Km raw_value=150 uM raw_unit=uM for Hg2+ at 70 C; table also lists 400 uM at 37 C.

row_label: M. sedula MerA / Hg2+ / 70 C

table_label: PMC Table 1 MerA comparison and Results prose


enzyme_display_name: Sarpagan bridge enzyme

organism: Gelsemium sempervirens

raw_value_unit_evidence: apparent KM value of 35.3 uM for Gs_207-0.13 with geissoschizine

row_label: Gs_207-0.13 / GsSBE with geissoschizine

enzyme: Sarpagan bridge enzyme


enzyme_display_name: gamma-glutamyl hercynylcysteine S-oxide synthase

organism: Mycolicibacterium thermoresistibile

substrate_name: hercynine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y377F with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

substrate: hercynine


enzyme: gamma-glutamyl hercynylcysteine S-oxide synthase


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


enzyme_display_name: ferroxidase

organism: Caretta caretta

substrate_name: p-phenylenediamine

enzyme: ferroxidase

substrate: p-phenylenediamine


enzyme_display_name: iron-cytochrome-c reductase

organism: Acidithiobacillus ferrooxidans

substrate_name: ferrocytochrome c

enzyme: iron-cytochrome-c reductase

substrate: ferrocytochrome c


organism: Acidomyces acidophilus

substrate_name: Fe(II)

proof_lines: recombinant wild-type enzyme, pH 5.0, 25°C

substrate: Fe(II)


enzyme_display_name: manganese oxidase

organism: Bacillus sp. PL-12

proof_lines: at pH 7.8, temperature not specified in the publication

enzyme: manganese oxidase


organism: Shewanella oneidensis

proof_lines:
isozyme MtrC, at pH 8.0 and 30°C
isozyme OmcA, at pH 8.0 and 30°C


organism: Desulfovibrio sp. A2


organism: Bacillus sp.


enzyme_display_name: Ceruloplasmin

organism: Homo sapiens

substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

proof_lines: kcat is 22.5 min(-1) and 30.3 min(-1) with Cu(+) and Fe(2+) as substrates, respectively.

enzyme: Ceruloplasmin

substrate: glutathione


substrate_name: tert-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: tert-butyl hydroperoxide


enzyme_display_name: Multicopper oxidase CueO

organism: Escherichia coli (strain K12)

substrate_name: enterobactin (at pH 5.0, in the presence of 1 mM Cu(2+))

assay_conditions_summary: pH 5

proof_lines: kcat is 914 min(-1) with Cu(+) as substrate (at pH 5.0, in the absence of added Cu(2+)) (PubMed:15516598). kcat is 651 min(-1) with Cu(+) as substrate (at pH 5.0, in the presence of 1 mM Cu(2+)) (PubMed:15516598). kcat is 57 min(-1) with Cu

enzyme: Multicopper oxidase CueO


substrate_name: ABTS (at pH 5.0, in the presence of 1 mM Cu(2+))


substrate_name: 2,6-DMP (at pH 5.0, in the presence of 1 mM Cu(2+))


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature E185A/D409A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'E185A/D409A'; column 'KM (µM)' = 3994±387; column 'kcat (min-1)' = 13.9±0.4; column 'single-turnover reduction by FeII (s-1), fast phase' = 0.41 ± 0.01; column 'single-turnover reduction by FeII (s-1), slow phase' = 0.02 ± 0.07; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 13.9 min-1; min^-1 to s^-1 is a division by 60, so 13.9 / 60 = 0.23166666666666666 s^(-1); the export carries 0.232 s^(-1). Km: printed Table 2 cell 3994 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 3994 / 1000 = 3.994 mM; the export carries 3.994 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.058003672174929057 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.23166666666666666 / 3.994 of this row's own two printed cells, typed derived_same_measurement; the export carries 0.05808713069604406 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'E185A/D409A': KM = 3994 µM; kcat = 13.9 min-1; Table 2 prints no kcat/KM cell for this row.

table_label: Table 2: Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII (Biochemistry 2006, 45(42):12741-12749)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature E185A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'E185A'; column 'KM (µM)' = 35.6±2.8; column 'kcat (min-1)' = 24.3±0.6; column 'single-turnover reduction by FeII (s-1), fast phase' = 2.47 ± 0.04; column 'single-turnover reduction by FeII (s-1), slow phase' = 0.36 ± 0.01; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 24.3 min-1; min^-1 to s^-1 is a division by 60, so 24.3 / 60 = 0.405 s^(-1); the export carries 0.48 s^(-1). Km: printed Table 2 cell 35.6 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 35.6 / 1000 = 0.0356 mM; the export carries 0.0356 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 11.376404494382024 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.405 / 0.0356 of this row's own two printed cells, typed derived_same_measurement; the export carries 13.48314606741573 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'E185A': KM = 35.6 µM; kcat = 24.3 min-1; Table 2 prints no kcat/KM cell for this row.

row_label: Table 2, Fet3p species row 'E185A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature D409A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'D409A'; column 'KM (µM)' = 18.8±1.6; column 'kcat (min-1)' = 48.2±1.2; column 'single-turnover reduction by FeII (s-1), fast phase' = 62.03 ± 0.60; column 'single-turnover reduction by FeII (s-1), slow phase' = 1.31 ± 0.07; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 48.2 min-1; min^-1 to s^-1 is a division by 60, so 48.2 / 60 = 0.8033333333333333 s^(-1); the export carries 6.08 s^(-1). Km: printed Table 2 cell 18.8 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 18.8 / 1000 = 0.0188 mM; the export carries 0.0188 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 42.730496453900706 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.8033333333333333 / 0.0188 of this row's own two printed cells, typed derived_same_measurement; the export carries 323.40425531914894 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'D409A': KM = 18.8 µM; kcat = 48.2 min-1; Table 2 prints no kcat/KM cell for this row.

row_label: Table 2, Fet3p species row 'D409A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature D283A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'D283A'; column 'KM (µM)' = 19.3±1.5; column 'kcat (min-1)' = 75.7±1.9; column 'single-turnover reduction by FeII (s-1), fast phase' = 681.9 ± 23.7; column 'single-turnover reduction by FeII (s-1), slow phase' = 2.46 ± 0.28; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 75.7 min-1; min^-1 to s^-1 is a division by 60, so 75.7 / 60 = 1.2616666666666667 s^(-1); the export carries 1.26 s^(-1). Km: printed Table 2 cell 19.3 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 19.3 / 1000 = 0.0193 mM; the export carries 0.0193 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 65.37132987910189 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.2616666666666667 / 0.0193 of this row's own two printed cells, typed derived_same_measurement; the export carries 65.28497409326424 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'D283A': KM = 19.3 µM; kcat = 75.7 min-1; Table 2 prints no kcat/KM cell for this row.

row_label: Table 2, Fet3p species row 'D283A'


substrate_name: hydroquinone

column_label: Table 3 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ), Fet3p species row 'E185A/D409A'; column 'KM (mM)' = 30.5±2.1; column 'kcat (min-1)' = 132.8±3.9; column 'single-turnover reduction by HQ (s-1), fast phase' = 2.127 ± 0.085; column 'single-turnover reduction by HQ (s-1), slow phase' = 0.256 ± 0.020; Table 3 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 132.8 min-1; min^-1 to s^-1 is a division by 60, so 132.8 / 60 = 2.2133333333333334 s^(-1); the export carries 2.3 s^(-1). Km: printed Table 3 cell 30.5 mM in the 'KM (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 30.5 mM; the export carries 0.03 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.07256830601092897 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.2133333333333334 / 30.5 of this row's own two printed cells, typed derived_same_measurement; the export carries 76.66666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Fet3p species row 'E185A/D409A': KM = 30.5 mM; kcat = 132.8 min-1; Table 3 prints no kcat/KM cell for this row.

table_label: Table 3: Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ (Biochemistry 2006, 45(42):12741-12749)

substrate: hydroquinone


column_label: Table 3 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ), Fet3p species row 'D409A'; column 'KM (mM)' = 30.3±2.4; column 'kcat (min-1)' = 139.7±4.7; column 'single-turnover reduction by HQ (s-1), fast phase' = 1.124 ± 0.103; column 'single-turnover reduction by HQ (s-1), slow phase' = 0.105 ± 0.003; Table 3 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 139.7 min-1; min^-1 to s^-1 is a division by 60, so 139.7 / 60 = 2.328333333333333 s^(-1); the export carries 2.33 s^(-1). Km: printed Table 3 cell 30.3 mM in the 'KM (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 30.3 mM; the export carries 0.03 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.07684268426842683 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.328333333333333 / 30.3 of this row's own two printed cells, typed derived_same_measurement; the export carries 77.66666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Fet3p species row 'D409A': KM = 30.3 mM; kcat = 139.7 min-1; Table 3 prints no kcat/KM cell for this row.

row_label: Table 3, Fet3p species row 'D409A'


column_label: Table 3 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ), Fet3p species row 'D283A'; column 'KM (mM)' = 19.3±1.1; column 'kcat (min-1)' = 169.5±3.5; column 'single-turnover reduction by HQ (s-1), fast phase' = 0.072 ± 0.018; column 'single-turnover reduction by HQ (s-1), slow phase' = 0.001 ± 0.101; Table 3 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 169.5 min-1; min^-1 to s^-1 is a division by 60, so 169.5 / 60 = 2.825 s^(-1); the export carries 2.81 s^(-1). Km: printed Table 3 cell 19.3 mM in the 'KM (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 19.3 mM; the export carries 0.019 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.14637305699481865 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.825 / 19.3 of this row's own two printed cells, typed derived_same_measurement; the export carries 147.89473684210526 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Fet3p species row 'D283A': KM = 19.3 mM; kcat = 169.5 min-1; Table 3 prints no kcat/KM cell for this row.

row_label: Table 3, Fet3p species row 'D283A'


substrate_name: Cu(+) (at pH 5.0, in the absence of added Cu(2+))


substrate_name: Fe(2+) (at pH 5.0, in the presence of 1 mM Cu(2+))


column_label: Table 1; hCp row; Cu1+ KM (uM) column = 36.8 +/- 5.1.

raw_value_unit_evidence: Table 1 hCp row reports Cu1+ KM = 36.8 +/- 5.1 uM.

row_label: hCp row; Cu1+ KM column

table_label: PMID 14623105, Table 1: Kinetic constants for the cuprous oxidase and ferroxidase reactions of Fet3p and hCp


column_label: Table 1; hCp row; Fe2+ KM (uM) column = 8.3 +/- 1.5.

raw_value_unit_evidence: Table 1 hCp row reports Fe2+ KM = 8.3 +/- 1.5 uM.

row_label: hCp row; Fe2+ KM column


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E185A/Y354A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E185A with inferred residue-numbering offset -31 to reconstruct the assayed variant sequence.

proof_lines:
mutant E185A, pH 6.0
mutant E185A
mutant E185A, pH 6.5, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D278A with inferred residue-numbering offset -31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E185D with inferred residue-numbering offset -31 to reconstruct the assayed variant sequence.

proof_lines:
mutant E185D, pH 6.0
mutant E185D, pH 6.5, 4°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y354A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines:
mutant Y354A, pH 6.0
mutant Y354A, pH 6.5, 4°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y354F with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines:
mutant Y354F, pH 6.0
mutant Y354F, pH 6.5, 4°C


proof_lines:
mutant E185D, pH 6.0
mutant E185D, pH 6.5, 25°C


proof_lines:
mutant Y354F, pH 6.0
mutant Y354F, pH 6.5, 25°C


proof_lines:
mutant Y354A, pH 6.0
mutant Y354A, pH 6.5, 25°C


enzyme_display_name: Hephaestin

proof_lines: kcat is 18 min(-1) for the oxidation of Fe(2+) (at pH 5.0).

enzyme: Hephaestin


organism: Bacillus pumilus

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


enzyme_display_name: Iron transport multicopper oxidase FET3

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

column_label: Table 1; Fet3p row; Cu1+ KM (uM) column = 37.9 +/- 3.6.

raw_value_unit_evidence: Table 1 Fet3p row reports Cu1+ KM = 37.9 +/- 3.6 uM.

row_label: Fet3p row; Cu1+ KM column

enzyme: Iron transport multicopper oxidase FET3


column_label: Table 1; Fet3p row; Fe2+ KM (uM) column = 5.4 +/- 0.8.

raw_value_unit_evidence: Table 1 Fet3p row reports Fe2+ KM = 5.4 +/- 0.8 uM.

row_label: Fet3p row; Fe2+ KM column


organism: Aquifex aeolicus


organism: Campylobacter jejuni


organism: Escherichia coli


organism: Rana catesbeiana


enzyme_display_name: cuproxidase

enzyme: cuproxidase


proof_lines: kcat is 79.2 min(-1) and 63.9 min(-1) with Cu(+) and Fe(2+) as substrates, respectively.


substrate_name: 2,3-DHB (at pH 5.0, in the presence of 1 mM Cu(2+))


substrate_name: Unknown


enzyme_display_name: mercury(II) reductase

organism: Lysinibacillus sphaericus


substrate_name: NADPH

substrate: NADPH


organism: Rhodobacter capsulatus


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


organism: Salmonella typhimurium


substrate_name: ferric enterobactin (at pH 6.5, in the presence of 0.5 mM Cu(2+))


assay_conditions_summary: pH 6; 298.15 K; buffer pH 6

column_label: PDF page 5, Results kinetic-analysis prose immediately before Figure 6: Fe(II) oxidation fit gives Km [Fe(II)] 4.8 +/- 0.3 uM and kcat [Fe(II) turnover] 9.5 min^-1; Figure 6 caption states Fe(II) oxidation was followed by Fe(III) appearance at 315 nm.

raw_value_unit_evidence: PDF page 5 Results text reports Km [Fe(II)] = 4.8 +/- 0.3 uM and kcat [Fe(II) turnover] = 9.5 min^-1.

row_label: Fet3p Fe(II) oxidation limiting-substrate fit

table_label: Results kinetic-analysis prose and Figure 6 caption


smiles: O=O

column_label: PDF page 5, Results kinetic-analysis prose immediately before Figure 6: O2 fit gives Km (O2) 1.3 +/- 0.2 uM and kcat [O2 turnover] 2.3 min^-1; Figure 6 caption states O2 consumption was determined by O2 electrode.

raw_value_unit_evidence: PDF page 5 Results text reports Km (O2) = 1.3 +/- 0.2 uM and kcat [O2 turnover] = 2.3 min^-1.

row_label: Fet3p O2 consumption limiting-substrate fit


substrate_name: Cu+

column_label: Table 1; Fet3p row; Cu1+ KM (uM) column = 37.9 +/- 3.6; Cu1+ kcat (min^-1) column = 79.2 +/- 2.7; no separate kcat/KM column is printed.

raw_value_unit_evidence: Table 1 Fet3p row reports Cu1+ KM = 37.9 +/- 3.6 uM and Cu1+ kcat = 79.2 +/- 2.7 min^-1.

row_label: Fet3p row; Cu1+ KM and Cu1+ kcat columns

substrate: Cu+


enzyme_display_name: DNA-binding protein HupB

organism: Mycobacterium leprae (strain TN)

column_label: Primary article prose/abstract segment; M. leprae ML-LBP/MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Abstract paragraph reports MDP1 Km values: M. leprae 0.129 mM.

table_label: Abstract/results prose: MDP1 ferroxidase Km values

enzyme: DNA-binding protein HupB


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: Primary article prose/abstract segment; M. tuberculosis MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Abstract paragraph reports MDP1 Km values: M. tuberculosis 0.252 mM.


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

column_label: Primary article prose/abstract segment; M. smegmatis MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Results text for M. smegmatis MDP1-deficient strain section reports Km value 0.136 mM.

row_label: M. smegmatis MDP1 ferroxidase activity


organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)

column_label: Primary article prose/abstract segment; M. bovis BCG MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Abstract paragraph reports MDP1 Km values: M. bovis BCG 0.292 mM.

row_label: M. bovis BCG MDP1 ferroxidase activity


assay_conditions_summary: pH 5; 313.15 K; buffer 100 mM Mes

column_label: Public ITQB PDF text, Table 1, wild-type Fe(II) row, + Cu(II) columns: Km 7 uM, kcat 38 min^-1, kcat/Km 5.4 min^-1 uM^-1. Local text refs: itqb_public_pdf_pmid_17451433_text.txt lines 467-486.

normalized_value_unit_evidence: Km 7 uM normalizes to 0.007 mM and kcat 38 min^-1 normalizes to 0.633 s^-1, matching the export values. The paper's explicit kcat/Km cell 5.4 min^-1 uM^-1 normalizes to 90.0 s^-1*mM^-1, while the export carries 90.42857142857143 s^-1*mM^-1.

raw_value_unit_evidence: Table 1 wild-type Fe(II) row reports + Cu(II) Km 7 +/- 2 uM, kcat 38 +/- 0.6 min^-1, and kcat/Km 5.4 min^-1 uM^-1.

row_label: Wild type / Fe(II)

table_label: Table 1. Kinetic parameters for oxidation of the metal ions Cu(I), Fe(II) and laccase substrates


substrate_name: prochlorperazine

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

substrate: prochlorperazine


organism: Desulfovibrio sp. A2


organism: Homo sapiens


substrate_name: perphenazine

substrate: perphenazine


substrate_name: promazine

substrate: promazine


substrate_name: alimemazine

substrate: alimemazine


substrate_name: thioridazine

substrate: thioridazine


substrate_name: p-Aminophenol

substrate: p-Aminophenol


substrate_name: periciazine

substrate: periciazine


substrate_name: diethazine

substrate: diethazine


substrate_name: Promethazine

substrate: Promethazine


substrate_name: L-epinephrine

substrate: L-epinephrine


substrate_name: 2-sulfonic acid-p-phenylenediamine

substrate: 2-sulfonic acid-p-phenylenediamine


substrate_name: Trifluoperazine

substrate: Trifluoperazine


substrate_name: L-norepinephrine

substrate: L-norepinephrine


substrate_name: o-aminophenol

substrate: o-aminophenol


substrate_name: o-phenylenediamine

substrate: o-phenylenediamine


substrate_name: N,N-dimethyl-m-phenylenediamine

substrate: N,N-dimethyl-m-phenylenediamine


substrate_name: chlorpromazine

substrate: chlorpromazine


substrate_name: fluphenazine

substrate: fluphenazine


substrate_name: ascorbate

substrate: ascorbate


substrate_name: p-anisidine

substrate: p-anisidine


substrate_name: 5-hydroxyindol-3-ylacetic acid

substrate: 5-hydroxyindol-3-ylacetic acid


substrate_name: triflupromazine

substrate: triflupromazine


substrate_name: N-acetyl-p-phenylenediamine

substrate: N-acetyl-p-phenylenediamine


substrate_name: m-phenylenediamine

substrate: m-phenylenediamine


substrate_name: N-phenyl-p-phenylenediamine

substrate: N-phenyl-p-phenylenediamine


substrate_name: pyrogallol

substrate: pyrogallol


substrate_name: quinone

substrate: quinone


substrate_name: durenediamine

substrate: durenediamine


substrate_name: N,N-Dimethyl-p-phenylenediamine

substrate: N,N-Dimethyl-p-phenylenediamine


substrate_name: catechol

substrate: catechol


substrate_name: N,N-diethyl-p-phenylenediamine

substrate: N,N-diethyl-p-phenylenediamine


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


enzyme_display_name: UniProt P22985

organism: Rattus norvegicus

substrate_name: NAD+

enzyme: UniProt P22985

substrate: NAD+


proof_lines: mutant enzyme C558A, anaerobic conditions

enzyme: mercury(II) reductase


proof_lines: mutant enzyme C559A, anaerobic conditions


proof_lines:
wild-type enzyme, aerobic conditions
wild-type enzyme, anaerobic conditions


organism: Candida albicans

proof_lines: recombinant E184A/D408A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication


proof_lines: recombinant E184A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication


proof_lines: recombinant wild-type CaFet34, pH not specified in the publication, temperature not specified in the publication


organism: Rhodococcus erythropolis

substrate_name: Cu+

proof_lines: pH 5.5, 30°C, mutant containing a deleted methionine-rich C-terminal tail

substrate: Cu+


organism: Saccharomyces cerevisiae

substrate_name: p-phenylenediamine

substrate: p-phenylenediamine


substrate_name: o-phenylenediamine

substrate: o-phenylenediamine


substrate_name: L-epinephrine

substrate: L-epinephrine


organism: uncultured Pseudomonadota bacterium

proof_lines: isoform ATII-LCL-NH mutant D415A/D416A, at 25°C, pH not specified in the publication


proof_lines: isoform ATII-LCL-NH, at 25°C, pH not specified in the publication


proof_lines: isoform ATII-LCL-NH mutant D414A/D415A/D416A/D417A, at 25°C, pH not specified in the publication


organism: Acidithiobacillus ferrooxidans

smiles: Cl[Hg]Cl


substrate_name: Hg

substrate: Hg


enzyme_display_name: UniProt P04036

organism: Escherichia coli

enzyme: UniProt P04036


enzyme_display_name: UniProt Q3M723

organism: Trichormus variabilis

substrate_name: NADH

enzyme: UniProt Q3M723

substrate: NADH


enzyme_display_name: UniProt Q9K1F1

organism: Neisseria meningitidis

enzyme: UniProt Q9K1F1


enzyme_display_name: UniProt Q5HG24

organism: Staphylococcus aureus

substrate_name: NADPH

enzyme: UniProt Q5HG24

substrate: NADPH


enzyme_display_name: UniProt A0A0A1EQY0

organism: [Candida] boidinii

substrate_name: formate

enzyme: UniProt A0A0A1EQY0

substrate: formate


enzyme_display_name: UniProt P33160

organism: Pseudomonas sp. 101

enzyme: UniProt P33160


substrate_name: NADP+

substrate: NADP+


enzyme_display_name: formate dehydrogenase

organism: Thermothelomyces thermophilus

smiles: O=C=O

enzyme: formate dehydrogenase


organism: Thermochaetoides thermophila

smiles: O=CO


enzyme_display_name: UniProt G8NVB5

organism: Granulicella mallensis

enzyme: UniProt G8NVB5


enzyme_display_name: formate dehydrogenase (NADP(+))

organism: Burkholderia stabilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q223E with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

enzyme: formate dehydrogenase (NADP(+))


enzyme_display_name: ferroxidase

organism: Anser sp.

enzyme: ferroxidase


substrate_name: o-Dianisidine

substrate: o-Dianisidine


enzyme_display_name: superoxide dismutase

organism: Bos taurus

enzyme: superoxide dismutase


proof_lines: pH 7, presence of Cu(II), temperature not specified in the publication

proof_lines: pH 5, presence of Cu(II), temperature not specified in the publication

proof_lines: pH 5, temperature not specified in the publication


organism: Arabidopsis thaliana

substrate_name: Fe(II)

proof_lines: wild type enzyme, at pH 5.8, temperature not specified in the publication

substrate: Fe(II)


proof_lines: mutant enzyme D370A, at pH 5.8, temperature not specified in the publication


proof_lines: pH 5.0, 23°C, mutant enzyme M358S/M361S/M362S/M364S/M366S


proof_lines: xanthine oxidoreductase with ferroxidase activity


organism: Gallus sp.


organism: Homo sapiens

proof_lines: pH 5.0, temperature not specified in the publication


substrate_name: hypoxia-inducible factor-L-proline

proof_lines: N-terminal oxygen degradation domain DALTLLAP402AAGDTIISLDYG mutant F413Y in absence of NaCl, pH 7.0, 37°C

proof_lines: N-terminal oxygen degradation domain DALTLLAP402AAGDTIISLDYG mutant F413Y in presence of 100 mM NaCl, pH 7.0, 37°C

substrate: hypoxia-inducible factor-L-proline


proof_lines: C-terminal oxygen degradation domain DLDLEALAP564YIPADDDFQL mutant M561A/M568A in absence of NaCl, pH 7.0, 37°C

proof_lines: C-terminal oxygen degradation domain DLDLEALAP564YIPADDDFQL mutant M561A/M568A in presence of 100 mM NaCl, pH 7.0, 37°C


enzyme_display_name: UniProt O54050

organism: Rhodobacter capsulatus

substrate_name: xanthine

enzyme: UniProt O54050

substrate: xanthine


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonate

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonate


enzyme_display_name: arachidonate 15-lipoxygenase

enzyme: arachidonate 15-lipoxygenase


enzyme_display_name: DNA oxidative demethylase

substrate_name: 3-methylcytosine in 3'-tailed DNA

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

enzyme: DNA oxidative demethylase

substrate: 3-methylcytosine in 3'-tailed DNA


proof_lines: in the presence of RAD51C, at pH 8.0 and 37°C


organism: Klebsiella pneumoniae


proof_lines:
wild-type, pH 8,23°C
wild-type enzyme


proof_lines: pH 7.5, 25°C, mutant Y34F with fluorinated Tyr-residues


proof_lines: pH 7.5, 25°C, wild-type with fluorinated Tyr-residues


enzyme_display_name: cuproxidase

organism: Escherichia coli

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

enzyme: cuproxidase


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


organism: Kitasatospora aureofaciens

substrate_name: CTP

proof_lines:
immobilized enzyme
presence of effector dATP

substrate: CTP


substrate_name: UTP

substrate: UTP


substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines:
immobilized enzyme
in presence of effector dGTP

substrate: ATP


substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


substrate_name: GTP

substrate: GTP


substrate_name: CDP

substrate: CDP


enzyme_display_name: xanthine oxidase

organism: Arthrobacter sp.

enzyme: xanthine oxidase


enzyme_display_name: ribonucleoside-diphosphate reductase

organism: Tequatrovirus T4

substrate_name: GDP

proof_lines: in the presence of 0.4 mM dTTP as effector

enzyme: ribonucleoside-diphosphate reductase

substrate: GDP


proof_lines: in the presence of 0.002 mM dATP as effector

proof_lines: in the presence of 0.5 mM ATP as effector

proof_lines: in the presence of 0.02 mM dTTP as effector


proof_lines: in the presence of 0.007 mM dGTP as effector


substrate_name: UDP

proof_lines: in the presence of 0.3 mM ATP as effector

substrate: UDP


substrate_name: Unknown

proof_lines:
in the presence of 0.15 mM dGTP
with 0.001 mM dATP as positive effector
in the presence of 0.55 mM dTTP

substrate: Unknown


organism: Blastobotrys adeninivorans

substrate_name: hypoxanthine

substrate: hypoxanthine


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 316.15 K; cofactor NAD+

substrate: NAD+


substrate_name: purine

substrate: purine


organism: Locusta sp.


organism: Thermus sp.

proof_lines:
at 37°C
at 70°C


assay_conditions_summary: 343.15 K; cofactor ATP


proof_lines: pH 8.5, 25°C, recombinant wild-type enzyme


enzyme_display_name: pteridine oxidase

organism: Ricinus communis

enzyme: pteridine oxidase


organism: Acinetobacter calcoaceticus


organism: Oshimavirus P7426

proof_lines: pH and temperature not specified in the publication, mutant G68S/R69P


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


substrate_name: Reduced glutaredoxin; CDP

substrate: Reduced glutaredoxin; CDP


substrate_name: CDP; Reduced glutaredoxin

substrate: CDP; Reduced glutaredoxin


enzyme_display_name: ribonucleoside-triphosphate reductase

organism: Lactococcus lactis subsp. cremoris

substrate_name: CTP; Reduced thioredoxin

enzyme: ribonucleoside-triphosphate reductase

substrate: CTP; Reduced thioredoxin


organism: Cellulosimicrobium cellulans

substrate_name: xanthine

substrate: xanthine


enzyme_display_name: 6-hydroxynicotinate dehydrogenase

organism: Neobacillus niacini

enzyme: 6-hydroxynicotinate dehydrogenase


organism: Drosophila melanogaster


organism: Anabaena sp.

substrate_name: CTP; 1,4-Dithiothreitol

substrate: CTP; 1,4-Dithiothreitol


organism: Sinomonas cyclohexanicum

proof_lines: at pH 7.2, temperature not specified in the publication


organism: Lens culinaris

substrate_name: H2O; Xanthine; O2

substrate: H2O; Xanthine; O2


enzyme_display_name: juglone 3-hydroxylase

organism: Pseudomonas putida

proof_lines:
enzyme 1
enzyme 2

enzyme: juglone 3-hydroxylase


organism: Euglena gracilis

substrate_name: Reduced thioredoxin; CTP

substrate: Reduced thioredoxin; CTP


organism: Lactobacillus leichmannii

substrate_name: ATP; Reduced thioredoxin

substrate: ATP; Reduced thioredoxin


substrate_name: CTP

proof_lines:
in presence of dATP
in presence of dTTP

substrate: CTP


substrate_name: ATP

substrate: ATP


organism: Rhodobacter capsulatus

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


enzyme_display_name: Vitamin B12-dependent ribonucleoside-diphosphate reductase

organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: CDP (at 80 degrees Celsius)

substrate: CDP (at 80 degrees Celsius)


organism: Cellulosimicrobium funkei


enzyme_display_name: UniProt P80457

organism: Bos taurus

enzyme: UniProt P80457


enzyme_display_name: Xanthine dehydrogenase/oxidase

substrate_name: NAD

assay_conditions_summary: cofactor NAD+

enzyme: Xanthine dehydrogenase/oxidase

substrate: NAD


enzyme_display_name: Ribonucleoside-diphosphate reductase small chain 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: Ribonucleoside-diphosphate reductase small chain 2


enzyme_display_name: Ribonucleoside-diphosphate reductase large chain 1


substrate_name: Oxidized thioredoxin

substrate: Oxidized thioredoxin


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: ADP (at 55 degrees Celsius)

assay_conditions_summary: 328.15 K; cofactor ADP

enzyme: Vitamin B12-dependent ribonucleoside-diphosphate reductase

substrate: ADP (at 55 degrees Celsius)


enzyme_display_name: phenylacetyl-CoA dehydrogenase

organism: Thauera aromatica

substrate_name: phenylacetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: pH 7.5, 30°C, duroquinone as electron acceptor

proof_lines: pH 7.5, 30°C, 2,6-dichlorophenolindophenol as electron acceptor

enzyme: phenylacetyl-CoA dehydrogenase

substrate: phenylacetyl-CoA


substrate_name: pyridine 3-aldehyde

substrate: pyridine 3-aldehyde


substrate_name: succinate semialdehyde

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

substrate: succinate semialdehyde


substrate_name: glyceraldehyde 3-phosphate

smiles: C(C(C=O)O)OP(=O)(O)O

substrate: glyceraldehyde 3-phosphate


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


enzyme_display_name: Caffeine dehydrogenase subunit alpha

organism: Pseudomonas sp. (strain CBB1)

substrate_name: caffeine (at 35 degrees Celsius and pH 7)

proof_lines: kcat is 10 min(-1) with caffeine as substrate.

enzyme: Caffeine dehydrogenase subunit alpha


enzyme_display_name: Caffeine dehydrogenase subunit gamma

enzyme: Caffeine dehydrogenase subunit gamma

substrate: caffeine (at 35 degrees Celsius and pH 7)


enzyme_display_name: Caffeine dehydrogenase subunit beta

enzyme: Caffeine dehydrogenase subunit beta


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
cosubstrate cytochrome c
cosubstrate indophenol
cofactor 2,6-dichlorophenolindophenol

substrate: NADPH


substrate_name: hypoxanthine

substrate: hypoxanthine


substrate_name: xanthine

assay_conditions_summary: pH 8.2; 296.65 K; cofactor NADH

proof_lines:
(+ O2)
cofactor 2,6-dichlorophenolindophenol
pH 8.2, 23.5°C

substrate: xanthine


substrate_name: aldehyde

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

substrate: aldehyde


enzyme_display_name: ethylbenzene hydroxylase

organism: Azoarcus sp.

enzyme: ethylbenzene hydroxylase


substrate_name: ferricenium

substrate: ferricenium


organism: Struthio camelus

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: xanthine oxidase


substrate_name: nitrite

substrate: nitrite


organism: Homo sapiens


organism: Mus musculus

substrate_name: all-trans-Retinal

substrate: all-trans-Retinal


organism: Pyrococcus furiosus

substrate_name: CDP

substrate: CDP


enzyme_display_name: ribonucleoside-diphosphate reductase

organism: Escherichia coli


substrate_name: dCDP

substrate: dCDP


organism: Rattus norvegicus

proof_lines: recombinant wild-type enzyme in recombinant Pichia pastoris membranes, pH 7.4, 37°C


proof_lines: native enzyme in membranes, pH 7.4, 37°C


proof_lines: pH 7.4, 37°C, recombinant mutant Y139F enzyme

proof_lines: pH 7.4, 37°C, liver microsomes from rats homozygous for Y139F


proof_lines: pH 7.4, 37°C, recombinant enzyme mutants Y139F, and L128Q


proof_lines: pH 7.4, 37°C, recombinant mutant Y139S enzyme


proof_lines: pH 7.4, 37°C, recombinant mutant L128Q enzyme


proof_lines: pH 7.4, 37°C, recombinant mutant Y139C enzyme


proof_lines: pH 7.4, 37°C, recombinant mutant L120Q enzyme


proof_lines: above, pH 7.4, 37°C, recombinant enzyme mutants Y139F, L120Q, Y139C, Y139F, and Y139S


substrate_name: dTTP

substrate: dTTP


substrate_name: ATP

substrate: ATP


substrate_name: UDP

substrate: UDP


substrate_name: GDP

substrate: GDP


proof_lines:
wild-typpe enzyme, pH 7.4, 37°C
wild-type, pH 8.6, 30°C


proof_lines:
substrate and inhibitor compound
25°C, pH 7.4, oxidized form of enzyme
25°C, pH 7.4, reduced form of enzyme


enzyme_display_name: UniProt P28861

substrate_name: Fe(III)-EDTA

enzyme: UniProt P28861

substrate: Fe(III)-EDTA


enzyme_display_name: UniProt Q8EY89

organism: Leptospira interrogans

enzyme: UniProt Q8EY89


enzyme_display_name: UniProt C6KT68

organism: Plasmodium falciparum

enzyme: UniProt C6KT68


organism: Mesocricetus auratus

proof_lines:
vs. GDP
vs. ADP
vs. UDP


proof_lines:
vs. ADP
vs. CDP
vs. UDP


substrate_name: ADP

proof_lines:
vs. GDP
vs. CDP
vs. UDP

substrate: ADP


proof_lines:
vs. GDP
vs. CDP
vs. ADP


enzyme: xanthine oxidase


substrate_name: NADH

substrate: NADH


assay_conditions_summary: pH 8.5; cofactor NADH

proof_lines:
with xanthine as cosubstrate
cosubstrate xanthine, pH 8.5
cosubstrate xanthine, pH 10.0


proof_lines:
pterin as cosubstrate
hypoxanthine as cosubstrate
with xanthine as cosubstrate


substrate_name: methylene blue

substrate: methylene blue


substrate_name: thionine

substrate: thionine


organism: Cricetulus griseus

proof_lines:
in the presence of 1.5 mM ATP
in the presence of 3.6 mM dCTP

enzyme: ribonucleoside-diphosphate reductase


proof_lines:
optimum dGTP concentration
in the presence of 0.2 mM GTP


substrate_name: glyceryl trinitrate

substrate: glyceryl trinitrate


substrate_name: isosorbide dinitrate

substrate: isosorbide dinitrate


substrate_name: xanthine

proof_lines: pH not specified in the publication, temperature not specified in the publication, mutant E802Q

substrate: xanthine


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


enzyme_display_name: UniProt O69054

organism: Pseudomonas stutzeri

substrate_name: phosphonate

enzyme: UniProt O69054

substrate: phosphonate


enzyme_display_name: UniProt G4XDR8

organism: Ralstonia sp.

substrate_name: NAD+

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.2
Raw SKiD Env: Temp=40°C, pH=7.2

enzyme: UniProt G4XDR8

substrate: NAD+


proof_lines:
Raw SKiD Env: Temp=40°C, pH=7.2
Raw SKiD Env: Temp=30°C, pH=7.2


substrate_name: phosphite

substrate: phosphite


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.3


enzyme_display_name: phosphite dehydrogenase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E175A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

smiles: O=[PH](O)O

enzyme: phosphite dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M53A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M53N to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt Q6VAL8

organism: Pseudorhizobium banfieldiae

substrate_name: arsenite

enzyme: UniProt Q6VAL8

substrate: arsenite


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: dATP

substrate: dATP


substrate_name: glutaredoxin 1

substrate: glutaredoxin 1


substrate_name: CDP

substrate: CDP


enzyme_display_name: gibberellin 2beta-dioxygenase

organism: Lathyrus oleraceus

substrate_name: gibberellin 1

enzyme: gibberellin 2beta-dioxygenase

substrate: gibberellin 1


substrate_name: gibberellin 9

substrate: gibberellin 9


organism: Klebsiella pneumoniae

substrate_name: 3,4-dihydroxybenzoic acid

substrate: 3,4-dihydroxybenzoic acid


enzyme_display_name: mercury(II) reductase

enzyme: mercury(II) reductase


organism: Herpes simplex virus


substrate_name: ADP

substrate: ADP


enzyme_display_name: coenzyme F420 hydrogenase

organism: Methanococcus voltae

substrate_name: coenzyme F420

enzyme: coenzyme F420 hydrogenase

substrate: coenzyme F420


substrate_name: methyl viologen

substrate: methyl viologen


organism: Methanothermobacter wolfeii

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Mus musculus

substrate_name: NADPH

enzyme: nitric-oxide synthase (NADPH)

substrate: NADPH


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


enzyme_display_name: 3-ketosteroid 9alpha-monooxygenase

organism: Mycobacterium tuberculosis

proof_lines: in 0.1 M potassium phosphate, pH 7.0, at 25°C

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

enzyme: 3-ketosteroid 9alpha-monooxygenase


enzyme_display_name: chlorite O2-lyase

organism: Nitrospira defluvii

substrate_name: Chlorite

smiles: [O-]Cl=O

enzyme: chlorite O2-lyase

substrate: Chlorite


organism: Oryctolagus cuniculus

proof_lines: in the presence of 5'-adenylimidodiphosphate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: nitric-oxide synthase (flavodoxin)

organism: Nocardia sp.

enzyme: nitric-oxide synthase (flavodoxin)


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Populus trichocarpa

substrate_name: trans-cinnamate

proof_lines: isoforms C4H1/C4H2/p-coumaroyl ester 3-hydroxylase C3H3 complex, pH 7.0, 20°C

proof_lines: isoform C4H1/p-coumaroyl ester 3-hydroxylase C3H3 complex, pH 7.0, 20°C

proof_lines: isoform C4H2/p-coumaroyl ester 3-hydroxylase C3H3 complex, pH 7.0, 20°C

enzyme: trans-cinnamate 4-monooxygenase

substrate: trans-cinnamate


proof_lines: isoforms C4H1/C4H2 complex, pH 7.0, 20°C


enzyme_display_name: catechol 1,2-dioxygenase

organism: Pseudomonas putida

enzyme: catechol 1,2-dioxygenase


enzyme_display_name: 6-hydroxynicotinate 3-monooxygenase

enzyme: 6-hydroxynicotinate 3-monooxygenase


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: homogentisate 1,2-dioxygenase

substrate_name: homogentisate

proof_lines: pH not specified in the publication, 25°C, wild-type enzyme

enzyme: homogentisate 1,2-dioxygenase

substrate: homogentisate


proof_lines: pH not specified in the publication, 25°C, mutant Y346F


organism: Rattus norvegicus

substrate_name: dithiothreitol

smiles: C(C(C(CS)O)O)S

proof_lines: in the presence of 0.0017 mM R,S-warfarin

substrate: dithiothreitol


substrate_name: vitamin K 2,3-epoxide

substrate: vitamin K 2,3-epoxide


organism: Pseudomonas sp. ZZ-5

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADH


mutation_type: deletion


substrate_name: styrene 1',2'-oxide

substrate: styrene 1',2'-oxide


substrate_name: allylbenzene 2',3'-oxide

substrate: allylbenzene 2',3'-oxide


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonic acid

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

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonic acid


substrate_name: 5,8,11,14,17-eicosapentaenoic acid

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

substrate: 5,8,11,14,17-eicosapentaenoic acid


enzyme_display_name: sterol 14alpha-demethylase

organism: Saccharomyces cerevisiae

substrate_name: lanosterol

proof_lines: fusion protein CYP51 (F1) consisting of the ORF of modified CYP51, a linker region containing the amino acid sequence S-T, and DELTA41 P450 reductase

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


proof_lines: fusion protein CYP51 (F2) consisting of the ORF of modified CYP51, a linker region containing the amino acid sequence S-T-E-Q-S-A-K-K-V-R-K-K-A, and DELTA55 P450 reductase


enzyme_display_name: ferroxidase

substrate_name: hydroquinone

proof_lines:
wild-type, pH 6.0
wild-type
wild-type, pH 6.5, 25°C

enzyme: ferroxidase

substrate: hydroquinone


substrate_name: p-phenylenediamine

assay_conditions_summary: pH 6

substrate: p-phenylenediamine


enzyme_display_name: UniProt P10868

substrate_name: S-adenosyl-L-methionine

enzyme: UniProt P10868

substrate: S-adenosyl-L-methionine


substrate_name: Guanidinoacetate

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

substrate: Guanidinoacetate


enzyme_display_name: UniProt Q93088

organism: Homo sapiens

substrate_name: S-methyl-L-methionine

smiles: C[S+](C)CCC(C(=O)O)N

enzyme: UniProt Q93088

substrate: S-methyl-L-methionine


organism: Sorghum sp.


smiles: O=O


enzyme_display_name: superoxide dismutase

organism: Solanum lycopersicum

substrate_name: riboflavin

enzyme: superoxide dismutase

substrate: riboflavin


substrate_name: Nitro blue tetrazolium

substrate: Nitro blue tetrazolium


organism: Sus scrofa

substrate_name: o-Dianisidine

substrate: o-Dianisidine


enzyme_display_name: gibberellin 3beta-dioxygenase

organism: Triticum aestivum

substrate_name: gibberellin a9

enzyme: gibberellin 3beta-dioxygenase

substrate: gibberellin a9


substrate_name: gibberellin a20

substrate: gibberellin a20


enzyme_display_name: biflaviolin synthase

organism: Streptomyces coelicolor

substrate_name: flaviolin

proof_lines: mutant K90I of isoform CYP158A1, at pH 8.2 and 37°C

enzyme: biflaviolin synthase

substrate: flaviolin


proof_lines: mutant I87K of isoform CYP158A2, at pH 8.2 and 37°C


enzyme_display_name: ectoine hydroxylase

organism: Stutzerimonas stutzeri

substrate_name: ectoine

enzyme: ectoine hydroxylase

substrate: ectoine


enzyme_display_name: mercury(II) reductase

organism: Acidithiobacillus ferrooxidans

enzyme: mercury(II) reductase


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


organism: Tupaia chinensis

proof_lines: pH 7.4, temperature not specified in the publication


substrate_name: arachidonate

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

substrate: arachidonate


enzyme_display_name: carnitine monooxygenase

organism: Acinetobacter baumannii

substrate_name: Unknown

proof_lines: pH 7.6, temperature not specified in the publication

enzyme: carnitine monooxygenase

substrate: Unknown


enzyme_display_name: UniProt P50135

enzyme: UniProt P50135


organism: Arabidopsis thaliana

proof_lines: in 100 mM Tris-HCl pH 7.9 containing 4 mM ascorbate, 4 mM DTT, 4 mM 2-oxoglutarate, 0.5 mM FeSO4, 2 mg/ml bovine serum albumin and 1 mg/ml catalase


organism: Acinetobacter sp. Y64

substrate_name: catechol

substrate: catechol


enzyme_display_name: sterol 22-desaturase

substrate_name: beta-sitosterol

proof_lines: isoform CYP710A1, pH and temperature not specified in the publication

proof_lines: isoform CYP710A2, pH and temperature not specified in the publication

enzyme: sterol 22-desaturase

substrate: beta-sitosterol


organism: Zea mays


substrate_name: obtusifoliol

substrate: obtusifoliol


enzyme_display_name: UniProt B2HHT4

organism: Mycobacterium marinum

substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

enzyme: UniProt B2HHT4

substrate: octanoic acid


substrate_name: Decanoic acid

smiles: CCCCCCCCCC(=O)O

substrate: Decanoic acid


substrate_name: 3-hydroxyoctanoic acid

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

substrate: 3-hydroxyoctanoic acid


substrate_name: 3-hydroxydecanoic acid

smiles: CCCCCCCC(CC(=O)O)O

substrate: 3-hydroxydecanoic acid


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: homogentisate

substrate: homogentisate


enzyme_display_name: indole-3-pyruvate monooxygenase

proof_lines: pH 8.5, 35°C, recombinant His-tagged enzyme

enzyme: indole-3-pyruvate monooxygenase


enzyme_display_name: fatty-acid O-methyltransferase

enzyme: fatty-acid O-methyltransferase


organism: Zymomonas mobilis

substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


substrate_name: phosphatidyl-N-methylethanolamine

substrate: phosphatidyl-N-methylethanolamine


substrate_name: phosphatidylethanolamine

smiles: CC(=O)OCC(COP(=O)(O)OCCN)OC(=O)C

substrate: phosphatidylethanolamine


substrate_name: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: catechol O-methyltransferase

organism: Unknown

enzyme: catechol O-methyltransferase


organism: Mycolicibacterium phlei


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase

enzyme: 9-cis-epoxycarotenoid dioxygenase


substrate_name: dodecanoic acid

smiles: CCCCCCCCCCCC(=O)O

substrate: dodecanoic acid


substrate_name: 3-hydroxydodecanoic acid

smiles: CCCCCCCCCC(CC(=O)O)O

substrate: 3-hydroxydodecanoic acid


organism: Pseudomonas sp.

substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


substrate_name: Trimethylsulfonium

substrate: Trimethylsulfonium


organism: Ricinus communis


enzyme_display_name: UniProt P82610

organism: Candida albicans

substrate_name: L-homocysteine

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

proof_lines: kcat is 25 min(-1) for homocysteine. kcat is 29 min(-1) for 5-methyl-tetrahydrofolate-triglutamate.

enzyme: UniProt P82610

substrate: L-homocysteine


enzyme_display_name: phenylethanolamine N-methyltransferase

organism: Oryctolagus cuniculus

substrate_name: m-octopamine

enzyme: phenylethanolamine N-methyltransferase

substrate: m-octopamine


enzyme_display_name: UniProt P11086

organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P11086


enzyme_display_name: glycine N-methyltransferase

organism: Rattus norvegicus

enzyme: glycine N-methyltransferase


substrate_name: Gly

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

substrate: Gly


organism: Catharanthus roseus


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

substrate_name: 5-methyltetrahydrofolate-triglutamate (at 37 degrees Celsius)


substrate_name: glycine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R175K with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

substrate: glycine


enzyme_display_name: polysaccharide O-methyltransferase

enzyme: polysaccharide O-methyltransferase


substrate_name: Glycine; S-Adenosyl-L-methionine

substrate: Glycine; S-Adenosyl-L-methionine


organism: Sus scrofa

substrate_name: S-Adenosyl-L-methionine; Glycine

substrate: S-Adenosyl-L-methionine; Glycine


organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: thiol S-methyltransferase

enzyme: thiol S-methyltransferase


organism: Arabidopsis thaliana


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: S-adenosyl-L-methionine (in presence of phosphatidylethanolamine (PE) as substrate)


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


column_label: Table 1 WT row, columns kcat min^-1, AdoMet Km uM, and AdoMet kcat/Km M^-1 s^-1: 174.5 +/- 23.2; 108 +/- 18; 26935 +/- 5738.

normalized_value_unit_evidence: kcat 2.908333333333333 s^(-1); AdoMet Km 0.108 mM; independently printed AdoMet kcat/Km 26.935 s^(-1)*mM^(-1).

raw_value_unit_evidence: WT row: kcat 174.5 +/- 23.2 min^-1; AdoMet Km 108 +/- 18 uM; independently printed AdoMet kcat/Km 26935 +/- 5738 M^-1 s^-1.

row_label: WT

table_label: Table 1. Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21A in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.59; column 'Km (uM)' under the AdoMet spanner = 539; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 18.3; the same data line prints the glycine spanner pair as 'Km (mM)' = 26.6 and 'kcat/Km (M-1 s-1)' = 0.37.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21A in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.59; printed Km (uM) cell 539; printed kcat/Km (M-1 s-1) cell 18.3.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21F in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 25.2; column 'Km (uM)' under the AdoMet spanner = 174; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 2409; the same data line prints the glycine spanner pair as 'Km (mM)' = 1.7 and 'kcat/Km (M-1 s-1)' = 248.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21F in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 25.2; printed Km (uM) cell 174; printed kcat/Km (M-1 s-1) cell 2409.