substrate_name: Benzylacetone

column_label: Table II Benzylacetone row, Km column 520 uM and kcat column 0.021 s^-1; Table II has no separate kcat/Km column, so the current ratio is the exact same-row quotient.

raw_value_unit_evidence: Table II Benzylacetone row: Km 520 uM; kcat 0.021 s^-1; FMT 91%.

row_label: Benzylacetone

substrate: Benzylacetone


enzyme_display_name: phenylacetone monooxygenase

organism: Mycobacterium tuberculosis

substrate_name: Ethionamide

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADPH

column_label: Table II Ethionamide row, Km column 340 uM and kcat column 0.027 s^-1; Table II has no separate kcat/Km column, so the current ratio is the exact same-row quotient.

raw_value_unit_evidence: Table II Ethionamide row: Km 340 uM; kcat 0.027 s^-1; FMT 88%.

row_label: Ethionamide

table_label: Table II. Steady-state kinetic parameters of EtaA

data_origin: experimental

enzyme: phenylacetone monooxygenase

substrate: Ethionamide

status: verified

source: oed


substrate_name: Phenylacetone

verification_status: unverified

substrate: Phenylacetone

status: unverified


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Rattus norvegicus

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F1395A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

enzyme: nitric-oxide synthase (NADPH)

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F1395S with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F1395W with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


column_label: Table 1; row WT; NADH columns; columns NADH Km, kcat, kcat/Km.

raw_value_unit_evidence: Table 1 WT NADH cells: Km 5890 +/- 270 uM; kcat 44.1 +/- 2.7 s^-1; printed kcat/Km 0.0075 uM^-1 s^-1.

row_label: WT; NADH columns

table_label: Table 1


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

substrate: NADPH


verification_status: corrected

column_label: Table 1 row WT, NADPH Km and kcat cells; the exact same-row quotient preserves the central values.

raw_value_unit_evidence: Table 1 WT NADPH cells: Km 28.2 +/- 4.5 uM; kcat 161.6 +/- 7.2 s^-1; printed rounded kcat/Km 5.7 uM^-1 s^-1.

row_label: WT; NADPH columns

status: corrected


enzyme_display_name: 7-methylxanthine demethylase

organism: Pseudomonas putida

substrate_name: Caffeine

source_db: brenda

kcat_over_km_display: Not reported

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

proof_lines: pH and temperature not specified in the publication

enzyme: 7-methylxanthine demethylase

substrate: Caffeine

source: brenda


kcat_display: Not reported

smiles: O=O


enzyme_display_name: 6-hydroxynicotinate 3-monooxygenase

organism: Bordetella bronchiseptica

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H302A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines:
H302A
Bordetella bronchiseptica NicC
6-Hydroxynicotinate 3-monooxygenase

enzyme: 6-hydroxynicotinate 3-monooxygenase


proof_lines:
wild-type NicC
NADH oxidation
Bordetella bronchiseptica


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y215F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines:
Y215F
Bordetella bronchiseptica NicC
6-Hydroxynicotinate 3-monooxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y225F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines:
Y225F
Bordetella bronchiseptica NicC
6-Hydroxynicotinate 3-monooxygenase


proof_lines: theobromine demethylase, pH and temperature not specified in the publication


enzyme_display_name: FAD-dependent urate hydroxylase

organism: Klebsiella pneumoniae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R204Q with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

enzyme: FAD-dependent urate hydroxylase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y216F to reconstruct the assayed variant sequence.


substrate_name: Urate

substrate: Urate


column_label: Table 1 row 4-HBA; columns kcat, KSM, kcat/KSM; footnote states pH 7.5 and 25 C.

table_label: Table 1. Comparison of reactions catalyzed by wild-type NicC with 6-HNA and analogues


column_label: Table 1 row 5-Cl-6-HNA; columns kcat, KSM, kcat/KSM; footnote states pH 7.5 and 25 C.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:A0A0H3LKL4 and applied mutation signature C202A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer pH 7; cofactor NADH

column_label: Table 2. Comparison of the Apparent Steady-State Kinetic Constants Derived from NADH Oxidation Rates of NicC Active Site Variants; row C202A; columns kcat (s^-1), K_M^6HNA (uM), and kcat/K_M^6HNA (M^-1 s^-1); C202A: kcat 0.26 +/- 0.02 s^-1; K_M^6HNA (uM) 200 +/- 37 uM; efficiency evidence (1.3 +/- 0.3) x 10^3. Km is converted from uM to mM by division by 1000. The independently printed efficiency is (1.3 +/- 0.3) x 10^3 M^-1*s^-1, normalized to 1.3 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:A0A0H3LKL4 and applied mutation signature H211A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 2. Comparison of the Apparent Steady-State Kinetic Constants Derived from NADH Oxidation Rates of NicC Active Site Variants; row H211A; columns kcat (s^-1), K_M^6HNA (uM), and kcat/K_M^6HNA (M^-1 s^-1); H211A: kcat 5.9 +/- 0.2 s^-1; K_M^6HNA (uM) 193 +/- 39 uM; efficiency evidence (3.1 +/- 0.8) x 10^4. Km is converted from uM to mM by division by 1000. The independently printed efficiency is (3.1 +/- 0.8) x 10^4 M^-1*s^-1, normalized to 31 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:A0A0H3LKL4 and applied mutation signature H302A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 2. Comparison of the Apparent Steady-State Kinetic Constants Derived from NADH Oxidation Rates of NicC Active Site Variants; row H302A; columns kcat (s^-1), K_M^6HNA (uM), and kcat/K_M^6HNA (M^-1 s^-1); H302A: kcat 0.90 +/- 0.02 s^-1; K_M^6HNA (uM) 20 +/- 7 uM; efficiency evidence (4.5 +/- 1.6) x 10^4. Km is converted from uM to mM by division by 1000. The independently printed efficiency is (4.5 +/- 1.6) x 10^4 M^-1*s^-1, normalized to 45 s^-1*mM^-1.


column_label: Table 2 WT row; columns kcat, K6HNA_M, kcat/K6HNA_M; footnote states pH 7.5 and 25 C.

row_label: WT

table_label: Table 2. Apparent steady-state kinetic constants from NADH oxidation rates of NicC active site variants


sequence_variant_note: Resolved canonical sequence from uniprot_accession:A0A0H3LKL4 and applied mutation signature Y215F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer pH 7; cofactor NAD+

column_label: Table 2. Comparison of the Apparent Steady-State Kinetic Constants Derived from NADH Oxidation Rates of NicC Active Site Variants; row Y215F; columns kcat (s^-1), K_M^6HNA (uM), and kcat/K_M^6HNA (M^-1 s^-1); Y215F: kcat 12 +/- 9 s^-1; K_M^6HNA (uM) 1600 +/- 1500 uM; efficiency evidence (7.5 +/- 9.0) x 10^3. Km is converted from uM to mM by division by 1000. The independently printed efficiency is (7.5 +/- 9.0) x 10^3 M^-1*s^-1, normalized to 7.5 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:A0A0H3LKL4 and applied mutation signature Y225F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 2. Comparison of the Apparent Steady-State Kinetic Constants Derived from NADH Oxidation Rates of NicC Active Site Variants; row Y225F; columns kcat (s^-1), K_M^6HNA (uM), and kcat/K_M^6HNA (M^-1 s^-1); Y225F: kcat 5.24 +/- 0.03 s^-1; K_M^6HNA (uM) 51 +/- 8 uM; efficiency evidence (1.0 +/- 0.2) x 10^5. Km is converted from uM to mM by division by 1000. The independently printed efficiency is (1.0 +/- 0.2) x 10^5 M^-1*s^-1, normalized to 100 s^-1*mM^-1.


column_label: Table 2. Comparison of the Apparent Steady-State Kinetic Constants Derived from NADH Oxidation Rates of NicC Active Site Variants; row C202A; columns kcat (s^-1), K_M^NADH (uM), and same-row derivation from kcat and K_M^NADH; C202A: kcat 0.26 +/- 0.02 s^-1; K_M^NADH (uM) 6.3 +/- 2.3 uM; efficiency evidence 0.26 s^-1 / 0.0063 mM. Km is converted from uM to mM by division by 1000. Table 2 has no kcat/K_M^NADH column; the package derives 41.26984126984127 s^-1*mM^-1 transparently from the same row's exact kcat 0.26 s^-1 and K_M^NADH 0.0063 mM cells.


column_label: Table 2. Comparison of the Apparent Steady-State Kinetic Constants Derived from NADH Oxidation Rates of NicC Active Site Variants; row H211A; columns kcat (s^-1), K_M^NADH (uM), and same-row derivation from kcat and K_M^NADH; H211A: kcat 5.9 +/- 0.2 s^-1; K_M^NADH (uM) 25 +/- 6 uM; efficiency evidence 5.9 s^-1 / 0.025 mM. Km is converted from uM to mM by division by 1000. Table 2 has no kcat/K_M^NADH column; the package derives 236 s^-1*mM^-1 transparently from the same row's exact kcat 5.9 s^-1 and K_M^NADH 0.025 mM cells.


proof_lines: pH 7.5, 30°C, kinetic parameters for two-subunit N-demethylase component (Ndm), in the presence of saturating amounts of Ccr (reductase component with cytochrome c reductase activity) and 50 mM Fe2+


assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.5) at 30°C


enzyme_display_name: trimethylamine monooxygenase

organism: Calanus finmarchicus

substrate_name: N,N,N-trimethylamine

smiles: CN(C)C

assay_conditions_summary: pH 7.7; 287.15 K; buffer potassium diphosphate

proof_lines: in potassium diphosphate buffer (pH 7.7), at 14°C

enzyme: trimethylamine monooxygenase

substrate: N,N,N-trimethylamine


assay_conditions_summary: pH 7.7; 287.15 K; buffer potassium diphosphate; cofactor NADPH


organism: Homo sapiens


assay_conditions_summary: pH 8.4; 310.15 K; buffer 0.1 M potassium phosphate

proof_lines: isozyme FMO3, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C


enzyme_display_name: Trimethylamine monooxygenase

organism: Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM)

substrate_name: methimazole

source_db: uniprot

proof_lines: kcat is 0.53 sec(-1) with TMA as substrate. kcat is 0.22 sec(-1) with methimazole as substrate. kcat is 0.15 sec(-1) with indole as substrate. kcat is 0.17 sec(-1) with DMA as substrate.

enzyme: Trimethylamine monooxygenase

substrate: methimazole

source: uniprot


substrate_name: indole

substrate: indole


substrate_name: DMA

substrate: DMA


organism: Pelagibacter sp. (strain HTCC7211)

column_label: Official PNAS supplement Table S3 page 7 row Pelagibacter ubique HTCC7211, substrate DMA, Km column gives 306.1 +/- 51.3 microM, not 181.4 microM.

row_label: Pelagibacter ubique HTCC7211 / DMA

table_label: Table S3. Steady-state kinetic assays on purified Tmm from recombinant E. coli


assay_conditions_summary: pH 7

column_label: PDF Table 1 row Tmm7211 / Methimazole; apparent KM column reports 116.2 uM, normalized to 0.1162 mM for the exported Km-only record.

normalized_value_unit_evidence: Km normalized_value=0.1162 normalized_unit=mM from 116.2 uM.

raw_value_unit_evidence: KM raw_value=116.2 raw_unit=uM for methimazole.

row_label: Methimazole

table_label: Table 1. Kinetic parameters for Tmm7211 and RnTmm


assay_conditions_summary: cofactor NADPH

column_label: PDF Table 3 row Wild type; columns apparent KM 12.8 uM (normalized 0.0128 mM) and kcat 4.5 min^-1 (export-normalized  s^-1); kcat/Km from same-row values  s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value= normalized_unit=s^-1 from 4.5 min^-1; Km normalized_value=0.0128 normalized_unit=mM from 12.8 uM; kcat/Km normalized_value= normalized_unit=s^-1*mM^-1 from same-row export values

raw_value_unit_evidence: KM raw_value=12.8 raw_unit=uM for NADPH; kcat raw_value=4.5 raw_unit=min^-1

row_label: Wild type

table_label: Table 3. Kinetic parameters for Tmm7211 and its mutants toward NADPH


enzyme_display_name: 1-hydroxy-2-naphthoate hydroxylase

organism: Unknown

substrate_name: Unknown

source_db: unknown

km_display: Not reported

source_license: see source

enzyme: 1-hydroxy-2-naphthoate hydroxylase

substrate: Unknown

source: unknown


enzyme_display_name: Flavin-containing monooxygenase 1

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

proof_lines: kcat is 55 min(-1) for the NAPDPH-dependent oxygenation of hypotaurine (at pH 8.5 and 37 degrees Celsius).

enzyme: Flavin-containing monooxygenase 1


organism: Mus musculus


substrate_name: DMSO

smiles: CS(=O)C

proof_lines: kcat is 22.4 min(-1) with TMA as substrate. kcat is 17.9 min(-1) with DMA as substrate. kcat is 4.5 min(-1) with DMS as substrate. kcat is 5.2 min(-1) with methimazole as substrate.

substrate: DMSO


organism: Candidatus Pelagibacter communis

assay_conditions_summary: pH 7.6; buffer 80 mM PIPES

proof_lines: recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C


organism: Candidatus Pelagibacter sp. HTCC7211

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature R226A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Arg226Ala'; column 'apparent K_M (uM)' = 101.8; column 'k_cat (min^-1)' = 0.9. Table 3 has only these two value columns for every enzyme form it lists and carries no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table 3 cell 101.8 uM; one uM is one thousandth of a mM, so 101.8 / 1000 = 0.1018 mM, which is the paper value in catalog units. kcat: printed Table 3 cell 0.9 min-1; one min^-1 is one sixtieth of a s^-1, so 0.9 / 60 = 0.015 s^(-1). kcat/Km: Table 3 has no catalytic-efficiency column, so the paper value 0.14734774066797643 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.015 / 0.1018 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Arg226Ala': the apparent K_M (uM) cell reads 101.8 uM and the k_cat (min^-1) cell reads 0.9 min-1. Table 3 has only these two value columns and carries no catalytic-efficiency column, so it prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'Arg226Ala' (catalog mutation signature R226A)

table_label: Table 3: Kinetic parameters for Tmm7211 and its mutants toward NADPH (Frontiers in Microbiology 2021, 12:735793)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature S203A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Ser203Ala'; column 'apparent K_M (uM)' = 134.8; column 'k_cat (min^-1)' = 1.0. Table 3 has only these two value columns for every enzyme form it lists and carries no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table 3 cell 134.8 uM; one uM is one thousandth of a mM, so 134.8 / 1000 = 0.1348 mM, which is the paper value in catalog units. kcat: printed Table 3 cell 1.0 min-1; one min^-1 is one sixtieth of a s^-1, so 1.0 / 60 = 0.016666666666666666 s^(-1), carried here at full precision rather than rounded to three significant figures. kcat/Km: Table 3 has no catalytic-efficiency column, so the paper value 0.12363996043521265 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.016666666666666666 / 0.1348 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Ser203Ala': the apparent K_M (uM) cell reads 134.8 uM and the k_cat (min^-1) cell reads 1.0 min-1. Table 3 has only these two value columns and carries no catalytic-efficiency column, so it prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'Ser203Ala' (catalog mutation signature S203A)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature N288A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NADPH

column_label: PDF Table 3 row Asn288Ala; columns apparent KM 61.1 uM (normalized 0.0611 mM) and kcat 1.3 min^-1 (normalized 0.0216666666666667 s^-1)

normalized_value_unit_evidence: kcat normalized_value=0.0216666666666667 normalized_unit=s^-1 from 1.3 min^-1; Km normalized_value=0.0611 normalized_unit=mM from 61.1 uM; kcat/Km normalized_value=0.354609929078014 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: KM raw_value=61.1 raw_unit=uM for NADPH; kcat raw_value=1.3 raw_unit=min^-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature N72A to reconstruct the assayed variant sequence.

column_label: PDF Table 3 row Asn72Ala; columns apparent KM 34.1 uM (normalized 0.0341 mM) and kcat 1.9 min^-1 (normalized 0.0316666666666667 s^-1)

normalized_value_unit_evidence: kcat normalized_value=0.0316666666666667 normalized_unit=s^-1 from 1.9 min^-1; Km normalized_value=0.0341 normalized_unit=mM from 34.1 uM; kcat/Km normalized_value=0.928641251221896 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: KM raw_value=34.1 raw_unit=uM for NADPH; kcat raw_value=1.9 raw_unit=min^-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature D314A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Asp314Ala'; column 'apparent K_M (uM)' = 32.0; column 'k_cat (min^-1)' = 2.1. Table 3 has only these two value columns for every enzyme form it lists and carries no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table 3 cell 32.0 uM; one uM is one thousandth of a mM, so 32.0 / 1000 = 0.032 mM, which is the paper value in catalog units. kcat: printed Table 3 cell 2.1 min-1; one min^-1 is one sixtieth of a s^-1, so 2.1 / 60 = 0.035 s^(-1). kcat/Km: Table 3 has no catalytic-efficiency column, so the paper value 1.09375 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.035 / 0.032 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Asp314Ala': the apparent K_M (uM) cell reads 32.0 uM and the k_cat (min^-1) cell reads 2.1 min-1. Table 3 has only these two value columns and carries no catalytic-efficiency column, so it prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'Asp314Ala' (catalog mutation signature D314A)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature H227A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'His227Ala'; column 'apparent K_M (uM)' = 41.2; column 'k_cat (min^-1)' = 2.5. Table 3 has only these two value columns for every enzyme form it lists and carries no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table 3 cell 41.2 uM; one uM is one thousandth of a mM, so 41.2 / 1000 = 0.0412 mM, which is the paper value in catalog units. kcat: printed Table 3 cell 2.5 min-1; one min^-1 is one sixtieth of a s^-1, so 2.5 / 60 = 0.041666666666666664 s^(-1), carried here at full precision rather than rounded to three significant figures. kcat/Km: Table 3 has no catalytic-efficiency column, so the paper value 1.0113268608414239 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.041666666666666664 / 0.0412 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'His227Ala': the apparent K_M (uM) cell reads 41.2 uM and the k_cat (min^-1) cell reads 2.5 min-1. Table 3 has only these two value columns and carries no catalytic-efficiency column, so it prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'His227Ala' (catalog mutation signature H227A)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature R409A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Arg409Ala'; column 'apparent K_M (uM)' = 44.9; column 'k_cat (min^-1)' = 2.7. Table 3 has only these two value columns for every enzyme form it lists and carries no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table 3 cell 44.9 uM; one uM is one thousandth of a mM, so 44.9 / 1000 = 0.0449 mM, which is the paper value in catalog units. kcat: printed Table 3 cell 2.7 min-1; one min^-1 is one sixtieth of a s^-1, so 2.7 / 60 = 0.045 s^(-1). kcat/Km: Table 3 has no catalytic-efficiency column, so the paper value 1.0022271714922049 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.045 / 0.0449 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Arg409Ala': the apparent K_M (uM) cell reads 44.9 uM and the k_cat (min^-1) cell reads 2.7 min-1. Table 3 has only these two value columns and carries no catalytic-efficiency column, so it prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'Arg409Ala' (catalog mutation signature R409A)


substrate_name: Dimethyl sulfide

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

smiles: CSC

column_label: PDF Table 1 row Tmm7211 / DMS; columns apparent KM 250.5 uM, kcat 4.5 min^-1, kcat/KM 18 min^-1 mM^-1; normalized values do not exactly equal all exported top-level values

normalized_value_unit_evidence: kcat normalized_value=0.075 normalized_unit=s^-1 from 4.5 min^-1; Km normalized_value=0.2505 normalized_unit=mM from 250.5 uM; kcat/Km normalized_value=0.3 normalized_unit=s^-1*mM^-1 from printed table value

raw_value_unit_evidence: kcat raw_value=4.5 raw_unit=min^-1; KM raw_value=250.5 raw_unit=uM; printed kcat/KM=18 min^-1 mM^-1

row_label: DMS

source_databases_merged: brenda oed

substrate: Dimethyl sulfide


column_label: PDF Table 3 row Wild type; columns apparent KM 12.8 uM (normalized 0.0128 mM) and kcat 4.5 min^-1 (export-normalized 0.075 s^-1); kcat/Km from same-row values 5.859375 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.075 normalized_unit=s^-1 from 4.5 min^-1; Km normalized_value=0.0128 normalized_unit=mM from 12.8 uM; kcat/Km normalized_value=5.859375 normalized_unit=s^-1*mM^-1 from same-row export values


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A6H1Q4Q3 and applied mutation signature D314E to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Asp314Glu'; column 'apparent K_M (uM)' = 9.7; column 'k_cat (min^-1)' = 5.2. Table 3 has only these two value columns for every enzyme form it lists and carries no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table 3 cell 9.7 uM; one uM is one thousandth of a mM, so 9.7 / 1000 = 0.0097 mM, which is the paper value in catalog units. kcat: printed Table 3 cell 5.2 min-1; one min^-1 is one sixtieth of a s^-1, so 5.2 / 60 = 0.08666666666666667 s^(-1), carried here at full precision rather than rounded to three significant figures. kcat/Km: Table 3 has no catalytic-efficiency column, so the paper value 8.934707903780069 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.08666666666666667 / 0.0097 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3 (Kinetic parameters for Tmm7211 and its mutants toward NADPH), enzyme row 'Asp314Glu': the apparent K_M (uM) cell reads 9.7 uM and the k_cat (min^-1) cell reads 5.2 min-1. Table 3 has only these two value columns and carries no catalytic-efficiency column, so it prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'Asp314Glu' (catalog mutation signature D314E)


substrate_name: Methimazole

column_label: PDF Table 1 row Tmm7211 / Methimazole; columns apparent KM 116.2 uM, kcat 5.2 min^-1, kcat/KM 44.8 min^-1 mM^-1; normalized values do not exactly equal all exported top-level values

normalized_value_unit_evidence: kcat normalized_value=0.0866666666666667 normalized_unit=s^-1 from 5.2 min^-1; Km normalized_value=0.1162 normalized_unit=mM from 116.2 uM; kcat/Km normalized_value=0.746666666666667 normalized_unit=s^-1*mM^-1 from printed table value

raw_value_unit_evidence: kcat raw_value=5.2 raw_unit=min^-1; KM raw_value=116.2 raw_unit=uM; printed kcat/KM=44.8 min^-1 mM^-1

substrate: Methimazole


substrate_name: N,N-dimethylamine

smiles: CNC

column_label: PDF Table 1 row Tmm7211 / DMA; columns apparent KM 181.4 uM, kcat 17.9 min^-1, kcat/KM 98.7 min^-1 mM^-1; normalized values do not exactly equal all exported top-level values

normalized_value_unit_evidence: kcat normalized_value=0.298333333333333 normalized_unit=s^-1 from 17.9 min^-1; Km normalized_value=0.1814 normalized_unit=mM from 181.4 uM; kcat/Km normalized_value=1.645 normalized_unit=s^-1*mM^-1 from printed table value

raw_value_unit_evidence: kcat raw_value=17.9 raw_unit=min^-1; KM raw_value=181.4 raw_unit=uM; printed kcat/KM=98.7 min^-1 mM^-1

row_label: DMA

substrate: N,N-dimethylamine


column_label: PDF Table 1 row Tmm7211 / TMA; columns apparent KM 139 uM, kcat 22.4 min^-1, kcat/KM 161.2 min^-1 mM^-1; normalized values do not exactly equal all exported top-level values

normalized_value_unit_evidence: kcat normalized_value=0.373333333333333 normalized_unit=s^-1 from 22.4 min^-1; Km normalized_value=0.139 normalized_unit=mM from 139 uM; kcat/Km normalized_value=2.68666666666667 normalized_unit=s^-1*mM^-1 from printed table value

raw_value_unit_evidence: kcat raw_value=22.4 raw_unit=min^-1; KM raw_value=139 raw_unit=uM; printed kcat/KM=161.2 min^-1 mM^-1

row_label: TMA


organism: Oryctolagus cuniculus

proof_lines: isoform FMO3, at pH 8.4, temperature not specified in the publication


enzyme_display_name: senecionine N-oxygenase

organism: Tyria jacobaeae

sequence_source: multiple

column_label: Abstract reports the reaction is strictly NADPH-dependent with Km 1.3 microM.

raw_value_unit_evidence: Km raw_value=1.3 microM raw_unit=microM

row_label: Tyria jacobaeae senecionine N-oxygenase / NADPH

table_label: PubMed XML abstract PMID 9182998

source_databases_merged: brenda uniprot

enzyme: senecionine N-oxygenase


substrate_name: senecionine

substrate: senecionine


substrate_name: monocrotaline

column_label: Abstract reports Km values of senecionine, monocrotaline and heliotrine as 1.3 microM, 12.5 microM and 290 microM respectively.

raw_value_unit_evidence: Km raw_value=12.5 microM raw_unit=microM

row_label: Tyria jacobaeae senecionine N-oxygenase / monocrotaline

substrate: monocrotaline


substrate_name: heliotrine

substrate: heliotrine


enzyme_display_name: taxoid 14beta-hydroxylase

organism: Taxus cuspidata

proof_lines: in Tris-HCl pH 7.5, temperature not specified in the publication

enzyme: taxoid 14beta-hydroxylase


substrate_name: TMA

substrate: TMA


organism: Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2)

column_label: PMC HTML Table 1 row DMA, Km column gives 89.7 +/- 13.2 microM.

table_label: Table 1. Steady-state kinetic assays on purified Tmm of M. silvestris from recombinant E. coli


column_label: PMC HTML Table 1 row DMSO, Km column gives 3,575 +/- 151 microM.

row_label: DMSO


substrate_name: cysteamine

smiles: C(CS)N

column_label: PMC HTML Table 1 row Cysteamine, Km column gives 3,139 +/- 534 microM.

row_label: Cysteamine

substrate: cysteamine


column_label: PMC HTML Table 1 row Methimazole, Km column gives 28.2 +/- 5.1 microM.


substrate_name: dimethylaniline

column_label: PMC HTML Table 1 row Dimethylaniline, Km column gives 35.7 +/- 2.5 microM.

row_label: Dimethylaniline

substrate: dimethylaniline


enzyme_display_name: Flavin-containing monooxygenase 3

substrate_name: trimethylamine (at pH 8.5)

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

assay_conditions_summary: pH 8.5; cofactor NADPH

column_label: Table 2; row Trimethylamine; FMO3 Enzyme Reference; KM column; raw 20.9 +/- 4.8 uM.

raw_value_unit_evidence: Table 2 Reference Trimethylamine KM cell: 20.9 +/- 4.8 uM

row_label: Trimethylamine / Reference FMO3 enzyme

table_label: PMID 17050781 Table 2, FMO3 structural variants

enzyme: Flavin-containing monooxygenase 3

substrate: trimethylamine (at pH 8.5)


substrate_name: benzydamine (at pH 7.4 and 37 degrees Celsius)


substrate_name: ethylenethiourea (at pH 8.5)

column_label: Table 2; row Ethylenethiourea; FMO3 Enzyme Reference; KM column; raw 55.7 +/- 12.1 uM.

raw_value_unit_evidence: Table 2 Reference Ethylenethiourea KM cell: 55.7 +/- 12.1 uM

row_label: Ethylenethiourea / Reference FMO3 enzyme

substrate: ethylenethiourea (at pH 8.5)


substrate_name: methimazole (at pH 8.5)

column_label: Table 2; row Methimazole; FMO3 Enzyme Reference; KM column; raw 71.8 +/- 8.1 uM.

raw_value_unit_evidence: Table 2 Reference Methimazole KM cell: 71.8 +/- 8.1 uM

row_label: Methimazole / Reference FMO3 enzyme

substrate: methimazole (at pH 8.5)


substrate_name: sulindac (at pH 8.5)

column_label: Table 2; row Sulindac; FMO3 Enzyme Reference; KM column; raw 150.1 +/- 39.8 uM.

raw_value_unit_evidence: Table 2 Reference Sulindac KM cell: 150.1 +/- 39.8 uM

row_label: Sulindac / Reference FMO3 enzyme

substrate: sulindac (at pH 8.5)


substrate_name: methyl p-tolyl sulfide (at pH 7.4 and 37 degrees Celsius)


substrate_name: trimethylamine

substrate: trimethylamine


organism: Pelagibacter ubique (strain HTCC1002)


organism: Roseovarius sp. (strain 217)


organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)


enzyme_display_name: monocyclic monoterpene ketone monooxygenase

organism: Rhodococcus erythropolis

sequence: MQTIPSTTETAADFDAVIXGAGFXGLYALHR

wild_type_sequence: MQTIPSTTETAADFDAVIXGAGFXGLYALHR

assay_conditions_summary: pH 9.5; 303.15 K; buffer glycine/NaOH

column_label: Table 4; row (1R,4S)-Menthone; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 4: (1R,4S)-Menthone; kcat 3.6 s^-1; Km 0.12 mM; kcat/Km 30 s^-1 mM^-1.

table_label: Table 4


column_label: Table 4; row (1S,4R)-1-Hydroxy-2-oxolimonene; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 4: (1S,4R)-1-Hydroxy-2-oxolimonene; kcat 3.9 s^-1; Km 0.13 mM; kcat/Km 30 s^-1 mM^-1.

enzyme: monocyclic monoterpene ketone monooxygenase


column_label: Table 4; row (4R)-Dihydrocarvone*; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1); footnote *Diastereomeric mixture.

raw_value_unit_evidence: Table 4: (4R)-Dihydrocarvone*; kcat 3.9 s^-1; Km 0.13 mM; kcat/Km 30 s^-1 mM^-1; *Diastereomeric mixture.


organism: Pseudomonas putida

column_label: Table 3 columns KM^6-HNA (uM), kcat (s^-1), and kcat/KM^6-HNA (M^-1 s^-1) for row P. putida.

normalized_value_unit_evidence: KM^6-HNA 0.097 mM; kcat 2.2 s^-1; kcat/KM^6-HNA 22 s^-1 mM^-1 table rounded, consistent with csv ratio 22.6804124.

row_label: P. putida

table_label: Table 3


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

column_label: Table 3; row P. putida; columns kcat (s^-1) and Km NADH (uM); same-row quotient; raw kcat 2.2 +/- 0.1; raw Km 3 +/- 2.

raw_value_unit_evidence: kcat 2.2 +/- 0.1 s^-1; Km NADH 3 +/- 2 uM; same-row kcat/Km derived as 2.2 / 0.003.

row_label: P. putida / NADH

table_label: Table 3: Comparison of the Apparent Steady-State Kinetic Constants of P. putida and B. bronchiseptica RB50 NicC

substrate: NADH


organism: Bordetella bronchiseptica

column_label: Table 3 columns KM^6-HNA (uM), kcat (s^-1), and kcat/KM^6-HNA (M^-1 s^-1) for row B. bronchiseptica RB50.

normalized_value_unit_evidence: KM^6-HNA 0.085 mM; kcat 4.2 s^-1; kcat/KM^6-HNA 50 s^-1 mM^-1 table rounded, consistent with csv ratio 49.4117647.

row_label: B. bronchiseptica RB50


column_label: Table 3; row B. bronchiseptica RB50; columns kcat (s^-1) and Km NADH (uM); same-row quotient; raw kcat 4.2 +/- 0.1; raw Km 6 +/- 2.

raw_value_unit_evidence: kcat 4.2 +/- 0.1 s^-1; Km NADH 6 +/- 2 uM; same-row kcat/Km derived as 4.2 / 0.006.

row_label: B. bronchiseptica RB50 / NADH


organism: Pseudomonas fluorescens

substrate_name: 6-hydroxynicotinic acid (at 30 degrees Celsius and pH 7.0)


organism: Escherichia coli

assay_conditions_summary: pH 7.4; 295.15 K; cofactor NADPH


substrate_name: NADPH

substrate: NADPH


substrate_name: DMA

proof_lines:
trimethylamine monooxygenase
Tmm
Pelagibacter ubique

substrate: DMA


substrate_name: DMSO

substrate: DMSO


organism: Xanthomonas campestris

proof_lines:
Xanthomonas campestris
FAD-dependent protein
urate


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


substrate_name: Urate

assay_conditions_summary: pH 8; 298.15 K; cofactor FAD

substrate: Urate


organism: Stenotrophomonas geniculata

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


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


organism: Ochrobactrum sp.

proof_lines: pH 8.0, 25°C, recombinant His-tagged enzyme


enzyme_display_name: 4-nitrophenol 4-monooxygenase

organism: Burkholderia sp.

proof_lines: pH and temperature not specified in the publication

enzyme: 4-nitrophenol 4-monooxygenase


enzyme_display_name: Indole-3-pyruvate monooxygenase YUCCA6

organism: Arabidopsis thaliana

substrate_name: Unknown

proof_lines: kcat is 0.31 sec(-1) for NADPH with phenyl pyruvate as substrate.

enzyme: Indole-3-pyruvate monooxygenase YUCCA6

substrate: Unknown


organism: Pseudomonas sp.

substrate_name: p-Nitrophenol; H+; NADPH; O2

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

substrate: p-Nitrophenol; H+; NADPH; O2


assay_conditions_summary: pH 7; buffer 20 mM phosphate; cofactor NADPH

column_label: Section Biochemical properties of PnpA states H6-PnpA Km values for NADPH and PNP were 137.4 +/- 12.3 and 12.0 +/- 1.6 uM, respectively.

row_label: H6-PnpA / PNP (para-nitrophenol)

table_label: Results prose: Biochemical properties of PnpA


row_label: H6-PnpA / NADPH


enzyme_display_name: UniProt E9QYP0

organism: Aspergillus fumigatus

substrate_name: L-ornithine

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt E9QYP0

substrate: L-ornithine

source: skid


substrate_name: phenyl pyruvate

substrate: phenyl pyruvate


substrate_name: tryptamine

substrate: tryptamine


substrate_name: N,N,N-trimethylamine

substrate: N,N,N-trimethylamine


organism: Pseudomonas putida (strain DSM 28022 / S16)

substrate_name: HSP

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

assay_conditions_summary: cofactor NADH

substrate: HSP


enzyme_display_name: 5-methyl-1-naphthoate 3-hydroxylase

organism: Streptomyces sahachiroi

enzyme: 5-methyl-1-naphthoate 3-hydroxylase


substrate_name: dimethyl sulfide

substrate: dimethyl sulfide


enzyme_display_name: phenylacetone monooxygenase

organism: Thermobifida fusca

substrate_name: cyclohexanone

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A442P/L443V with inferred residue-numbering offset -34 to reconstruct the assayed variant sequence.

enzyme: phenylacetone monooxygenase

substrate: cyclohexanone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S441G/A442P/L443T/S444Q to reconstruct the assayed variant sequence.


enzyme_display_name: 2,6-dihydroxypyridine 3-monooxygenase

organism: Paenarthrobacter nicotinovorans

assay_conditions_summary: pH 8; cofactor NADH

enzyme: 2,6-dihydroxypyridine 3-monooxygenase


enzyme_display_name: 7-methylxanthine demethylase

enzyme: 7-methylxanthine demethylase


enzyme_display_name: Para-nitrophenol 4-monooxygenase

organism: Pseudomonas sp. (strain WBC-3)

substrate_name: NADP

enzyme: Para-nitrophenol 4-monooxygenase

substrate: NADP


assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M22L/L380I to reconstruct the assayed variant sequence.


organism: Burkholderia sp

substrate_name: 4-nitrophenol (4NP)

proof_lines: kcat is 0.014 sec(-1) with 4-nitrophenol (4NP) as substrate.

substrate: 4-nitrophenol (4NP)


enzyme_display_name: protoasukamycin 4-monooxygenase

organism: Streptomyces nodosus

substrate_name: NADH

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: in presence of 0.01 mM FAD, recombinant enzyme, pH 7.0, 30°C

proof_lines: kcat is 0.183 min(-1) with protoasukamycin as substrate. kcat is 0.113 sec(-1) with NADH as substrate. kcat is 0.324 sec(-1) with NADPH as substrate.

enzyme: protoasukamycin 4-monooxygenase


substrate_name: protoasukamycin

substrate: protoasukamycin


substrate_name: NADPH

assay_conditions_summary: pH 9; cofactor NADPH


assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM potassium phosphate

column_label: Table 2 row Trimethyluric acid; columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: Direct Table 2 cells normalized independently: kcat=7.4816666666666665 s^-1; Km=0.0102 mM; printed kcat/Km=735.0000000000001 s^-1 mM^-1. The printed kcat/Km cell, not a recomputed quotient, is the correction authority.

raw_value_unit_evidence: Table 2 row Trimethyluric acid reports kcat 448.9 +/- 21.7 min^-1; Km 10.2 +/- 2.2 uM; kcat/Km 44.1 +/- 2.1 min^-1 uM^-1.

row_label: Trimethyluric acid

table_label: Table 2. Kinetic parameters and substrate specificities of purified TmuM-His6


column_label: Table 2 row 1,3-Dimethyluric acid; columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: Direct Table 2 cells normalized independently: kcat=3.0833333333333335 s^-1; Km=0.1265 mM; printed kcat/Km=25.0 s^-1 mM^-1. The printed kcat/Km cell, not a recomputed quotient, is the correction authority.

raw_value_unit_evidence: Table 2 row 1,3-Dimethyluric acid reports kcat 185.0 +/- 16.4 min^-1; Km 126.5 +/- 29.3 uM; kcat/Km 1.5 +/- 0.1 min^-1 uM^-1.

row_label: 1,3-Dimethyluric acid


column_label: Table 2 row 1-Methyluric acid; columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: Direct Table 2 cells normalized independently: kcat=0.485 s^-1; Km=0.0012 mM; printed kcat/Km=408.33333333333337 s^-1 mM^-1. The printed kcat/Km cell, not a recomputed quotient, is the correction authority.

raw_value_unit_evidence: Table 2 row 1-Methyluric acid reports kcat 29.1 +/- 2.4 min^-1; Km 1.2 +/- 0.5 uM; kcat/Km 24.5 +/- 2.0 min^-1 uM^-1.

row_label: 1-Methyluric acid


column_label: Table 2 row 3,7-Dimethyluric acid; columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: Direct Table 2 cells normalized independently: kcat=1.97 s^-1; Km=0.0013 mM; printed kcat/Km=1490.0000000000002 s^-1 mM^-1. The printed kcat/Km cell, not a recomputed quotient, is the correction authority.

raw_value_unit_evidence: Table 2 row 3,7-Dimethyluric acid reports kcat 118.2 +/- 8.4 min^-1; Km 1.3 +/- 0.6 uM; kcat/Km 89.4 +/- 6.3 min^-1 uM^-1.

row_label: 3,7-Dimethyluric acid


assay_conditions_summary: cofactor NADPH


substrate_name: oxygen

substrate: oxygen


substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M22L/L380I to reconstruct the assayed variant sequence.


enzyme_display_name: NO-associated protein 1, chloroplastic/mitochondrial

substrate_name: arginine

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

substrate: arginine


enzyme_display_name: toluene 2-monooxygenase

organism: Burkholderia cepacia

substrate_name: methyl p-tolyl sulfide

proof_lines: wild-type, whole cell assay, recombinant protein, pH not specified in the publication, temperature not specified in the publication

enzyme: toluene 2-monooxygenase

substrate: methyl p-tolyl sulfide


substrate_name: thioanisole

substrate: thioanisole


enzyme_display_name: phenol 2-monooxygenase (NADH)

organism: Rhodococcus erythropolis

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH

enzyme: phenol 2-monooxygenase (NADH)


organism: Stutzerimonas stutzeri

substrate_name: phenol

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

substrate: phenol


substrate_name: N-methyl-5-hydroxynicotinic acid

mutation_signature: calculation from stopped-flow data calculation from stopped-flow data

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

substrate: N-methyl-5-hydroxynicotinic acid


proof_lines: kcat is 552 min(-1) with 5-hydroxynicotinic acid as substrate (at pH 8.0 and 25 degrees Celsius) (PubMed:9207074). kcat is 0.27 sec(-1) with N-methyl-5-hydroxynicotinic acid as substrate (at pH 7.0 and 4 degrees Celsius) (PubMed:9374863).


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


substrate_name: 5-hydroxynicotinic acid

substrate: 5-hydroxynicotinic acid


organism: Streptomyces cremeus

substrate_name: L-aspartate

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

proof_lines: kcat is 1.14 sec(-1) with L-aspartate as substrate. kcat is 1.19 sec(-1) with NADPH as substrate.

substrate: L-aspartate


substrate: NADPH


organism: Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)

substrate_name: MHPC (at pH 8.0 and 25 degrees Celsius)

assay_conditions_summary: pH 8; buffer 50 mM potassium phosphate; cofactor NADH

column_label: PMID 17270714 Table 3, M. loti enzyme, Km (uM), MHPC row = 25.4 +/- 3.6; assay method states pH 8.0 and 25 deg C.

raw_value_unit_evidence: Results prose reports Km and kcat for MHPC were 25.4 +/- 3.6 uM and 709 min^-1; Table 3 row MHPC lists Km 25.4 +/- 3.6 uM.

row_label: M. loti enzyme / MHPC

table_label: Results prose and Table 3 comparison of properties of Mesorhizobium and Pseudomonas MHPCOs

substrate: MHPC (at pH 8.0 and 25 degrees Celsius)


substrate_name: FAD (at pH 8.0 and 25 degrees Celsius)

assay_conditions_summary: pH 8; cofactor FAD

proof_lines: kcat is 643 min(-1) with 5-hydroxynicotinic acid as substrate (at pH 8.0 and 25 degrees Celsius) (PubMed:17270714). kcat is 709 min(-1) with MHPC as substrate (at pH 8.0 and 25 degrees Celsius) (PubMed:17270714). kcat is 1300 sec(-1) with 5

substrate: FAD (at pH 8.0 and 25 degrees Celsius)


organism: Mesorhizobium loti

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y270A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y270F with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


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

source_databases_merged: brenda skid uniprot


enzyme_display_name: F-actin monooxygenase

organism: Homo sapiens

substrate_name: Unknown

enzyme: F-actin monooxygenase

substrate: Unknown


organism: Arabidopsis thaliana

substrate_name: GTP (at 37 degrees Celsius)

enzyme: NO-associated protein 1, chloroplastic/mitochondrial

substrate: GTP (at 37 degrees Celsius)


enzyme_display_name: butane monooxygenase (soluble)

organism: Thauera butanivorans

enzyme: butane monooxygenase (soluble)


proof_lines:
pH 8.0, 25°C
Raw SKiD Env: Temp=25°C, pH=8

source_databases_merged: brenda skid


proof_lines:
5-hydroxynicotinic acid
5-pyridoxic acid
Tyr270


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y270A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y270F with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


proof_lines: about a 6,000-fold preference toward NADPH over NADH


enzyme_display_name: magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase

organism: Rubrivivax gelatinosus

substrate_name: magnesium-protoporphyrin IX 13-monomethyl ester


enzyme_display_name: UniProt P05177

substrate_name: fenthion

enzyme: UniProt P05177

substrate: fenthion


enzyme_display_name: FAD-dependent urate hydroxylase

organism: Klebsiella pneumoniae

substrate_name: Urate

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

assay_conditions_summary: pH 8; 298.15 K; buffer 0.1 M potassium phosphate; cofactor FAD

proof_lines: mutant enzyme R204Q, in 0.1 M potassium phosphate buffer (pH 8.0), at 25°C

enzyme: FAD-dependent urate hydroxylase

substrate: Urate


substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; buffer 0.1 M potassium phosphate; cofactor NADH


proof_lines: mutant enzyme Y216F, in 0.1 M potassium phosphate buffer (pH 8.0), at 25°C


proof_lines: wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0), at 25°C


enzyme_display_name: 4-hydroxyphenylacetate 3-monooxygenase

organism: Pseudomonas putida

substrate_name: FAD

enzyme: 4-hydroxyphenylacetate 3-monooxygenase

substrate: FAD


substrate_name: phenylacetic acid

substrate: phenylacetic acid


enzyme_display_name: UniProt Q6Q272

organism: Acinetobacter baumannii

enzyme: UniProt Q6Q272

substrate: NADH


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Rattus norvegicus

substrate_name: tetrahydrobiopterin

enzyme: nitric-oxide synthase (NADPH)

substrate: tetrahydrobiopterin


substrate_name: L-arginine

proof_lines:
22°C, wild type
pH 7.6, 10°C, wild type

substrate: L-arginine


enzyme_display_name: trimethylamine monooxygenase

substrate_name: sulindac sulfide

mutation_signature: truncated recombinant enzyme

assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: truncated recombinant enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C

enzyme: trimethylamine monooxygenase

substrate: sulindac sulfide


proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C


substrate_name: Methimazole

substrate: Methimazole


substrate_name: Benzydamine

substrate: Benzydamine


enzyme_display_name: putrescine N-hydroxylase

organism: Streptomyces sviceus

substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: with cadaverine as cosubstrate, at pH 8.0 and 25°C

enzyme: putrescine N-hydroxylase


substrate_name: putrescine

smiles: C(CCN)CN

proof_lines: with NADH as cosubstrate, at pH 8.0 and 25°C

substrate: putrescine


substrate_name: cadaverine

smiles: C(CCN)CCCCN

proof_lines: with NADPH as cosubstrate, at pH 8.0 and 25°C

substrate: cadaverine


substrate_name: nitroblue tetrazolium

substrate: nitroblue tetrazolium


proof_lines:
NADPH
NADPH, diaphorase activity
with Ca2+, 0.01 mM


proof_lines: irreversible inactivation of neuronal isoform after preincubation

proof_lines: neuronal isoform in presence of 0.004 mM tetrahydrobiopterin


substrate_name: nitric oxide

mutation_type: deletion

proof_lines: DELTAG810 mutant enzyme, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25°C

proof_lines: DELTAG810 mutant enzyme, in the presence of 10 units/ml catalase and superoxide dismutase, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25°C

substrate: nitric oxide


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADPH


proof_lines: wild type enzyme, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25°C

proof_lines: wild type enzyme, in the presence of 10 units/ml catalase and superoxide dismutase, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25°C


enzyme_display_name: styrene monooxygenase

organism: Herbaspirillum huttiense

substrate_name: Styrene

enzyme: styrene monooxygenase

substrate: Styrene


proof_lines: Km values measured using the C1-C2 complex.

source_databases_merged: skid uniprot


enzyme_display_name: Alkanesulfonate monooxygenase

organism: Escherichia coli (strain K12)

substrate_name: decanesulfonate

enzyme: Alkanesulfonate monooxygenase

substrate: decanesulfonate


enzyme_display_name: UniProt A0A140NG21

organism: Escherichia coli

substrate_name: umbelliferone

enzyme: UniProt A0A140NG21

substrate: umbelliferone


substrate_name: 4-coumaric acid

substrate: 4-coumaric acid


organism: Pseudomonas sp.


enzyme_display_name: Styrene monooxygenase StyA

organism: Pseudomonas sp

substrate_name: Unknown

enzyme: Styrene monooxygenase StyA

substrate: Unknown


enzyme_display_name: Anthranilate 3-monooxygenase oxygenase component

organism: Geobacillus thermodenitrificans (strain NG80-2)


enzyme: Anthranilate 3-monooxygenase oxygenase component


assay_conditions_summary: pH 9.1; cofactor NADPH

column_label: JBC full-table HTML Table IV row 1,3-Dioxo-2-isoindolineethanesulfonic acid (33-500 microM) column K m (microM) reports 114, converted to 0.114 mM.

raw_value_unit_evidence: Km raw_value=114 raw_unit=microM

table_label: Table IV. Kinetic parameters of alkanesulfonate monooxygenase


column_label: JBC full-table HTML Table IV row 2-(4-Pyridyl)ethanesulfonic acid (33-500 microM) column K m (microM) reports 139, converted to 0.139 mM.

raw_value_unit_evidence: Km raw_value=139 raw_unit=microM


substrate_name: N-phenyltaurine

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

raw_value_unit_evidence: Km raw_value=237 raw_unit=microM

row_label: N-Phenyltaurine (50-500 microM)

substrate: N-phenyltaurine


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

raw_value_unit_evidence: Km raw_value=110 raw_unit=microM


substrate_name: MOPS

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

raw_value_unit_evidence: Km raw_value=617 raw_unit=microM

row_label: MOPS (70-1000 microM)

substrate: MOPS


substrate_name: butanesulfonate

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

raw_value_unit_evidence: Km raw_value=870 raw_unit=microM

row_label: Butanesulfonic acid (250-1000 microM)

substrate: butanesulfonate


substrate_name: PIPES

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

raw_value_unit_evidence: Km raw_value=1110 raw_unit=microM

row_label: PIPES (333-3000 microM)

substrate: PIPES


enzyme_display_name: FMN reductase (NADH)

organism: Aminobacter aminovorans

substrate_name: Nitrilotriacetic acid; O2; H+; NADH

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

enzyme: FMN reductase (NADH)

substrate: Nitrilotriacetic acid; O2; H+; NADH


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

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


substrate_name: naringenin

substrate: naringenin


substrate_name: resveratrol

substrate: resveratrol


enzyme_display_name: alkanesulfonate monooxygenase

substrate_name: octanesulfonate

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

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

enzyme: alkanesulfonate monooxygenase

substrate: octanesulfonate


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


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


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


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


substrate_name: NADH

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

substrate: NADH


enzyme_display_name: Nitrilotriacetate monooxygenase component A

substrate_name: nitriloacetate

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

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

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

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

row_label: Mg(2+)-NTA substrate

table_label: PubMed abstract / official PMC abstract prose

substrate: nitriloacetate


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

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

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

row_label: NTA-Mo substrate/cofactor Km sentence

table_label: PubMed abstract

enzyme: Nitrilotriacetate monooxygenase component A


substrate_name: decanesulfonic acid

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

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

substrate: decanesulfonic acid


substrate_name: octanesulfonic acid

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

substrate: octanesulfonic acid


substrate_name: hexanesulfonic acid

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

substrate: hexanesulfonic acid


substrate_name: 4-phenyl-1-butanesulfonic acid

substrate: 4-phenyl-1-butanesulfonic acid


substrate_name: 2-(4-pyridyl)ethanesulfonic acid

substrate: 2-(4-pyridyl)ethanesulfonic acid


substrate_name: pentanesulfonic acid

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

substrate: pentanesulfonic acid


substrate_name: N-phenyltaurine

substrate: N-phenyltaurine


substrate_name: MOPS

substrate: MOPS


substrate_name: butanesulfonic acid

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

substrate: butanesulfonic acid


substrate_name: PIPES

substrate: PIPES


substrate_name: FMN

assay_conditions_summary: cofactor FMN

substrate: FMN


substrate_name: riboflavin

substrate: riboflavin


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


assay_conditions_summary: cofactor NADH


substrate_name: naringenin

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

substrate: naringenin


substrate_name: 4-coumaric acid

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

substrate: 4-coumaric acid


substrate_name: umbelliferone

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

substrate: umbelliferone


substrate_name: resveratrol

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

substrate: resveratrol


enzyme_display_name: UniProt A7U483

organism: Danio rerio

substrate_name: progesterone

enzyme: UniProt A7U483

substrate: progesterone


substrate_name: pregnenolone

substrate: pregnenolone


enzyme_display_name: UniProt B3DH80

enzyme: UniProt B3DH80


substrate_name: methyl 4-hydroxybenzoate

substrate: methyl 4-hydroxybenzoate


substrate_name: phenol

substrate: phenol


substrate_name: DL-4-hydroxymandelic acid

substrate: DL-4-hydroxymandelic acid


substrate_name: octanesulfonate

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

substrate: octanesulfonate


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


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


enzyme_display_name: DNA oxidative demethylase

assay_conditions_summary: 310.15 K; cofactor ATP

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

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

enzyme: DNA oxidative demethylase


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


enzyme_display_name: UniProt Q9LAG2

organism: Parageobacillus thermoglucosidasius

enzyme: UniProt Q9LAG2


enzyme_display_name: UniProt Q9LBX2

organism: Paenibacillus sp.

substrate_name: benzothiophene

enzyme: UniProt Q9LBX2

substrate: benzothiophene


enzyme_display_name: UniProt P22680

organism: Homo sapiens

enzyme: UniProt P22680


enzyme_display_name: UniProt C4B644

organism: Pseudonocardia autotrophica

substrate_name: vitamin D3

enzyme: UniProt C4B644

substrate: vitamin D3


enzyme_display_name: UniProt Q9Y6A2

substrate_name: cholesterol 3-sulfate

enzyme: UniProt Q9Y6A2

substrate: cholesterol 3-sulfate


enzyme_display_name: 3-carboxyethylcatechol 2,3-dioxygenase

substrate_name: catechol

enzyme: 3-carboxyethylcatechol 2,3-dioxygenase

substrate: catechol


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: mitomycin C

proof_lines: full-length enzyme, absence of calmodulin

enzyme: nitric-oxide synthase (NADPH)

substrate: mitomycin C


substrate_name: adriamycin

substrate: adriamycin


substrate_name: menadione

substrate: menadione


enzyme_display_name: gentisate 1,2-dioxygenase

enzyme: gentisate 1,2-dioxygenase


enzyme_display_name: taurine dioxygenase

substrate_name: N-methyltaurine

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

proof_lines:
deuterated substrate
commercially available substrate

enzyme: taurine dioxygenase

substrate: N-methyltaurine


smiles: O=O

proof_lines: commercially available substrate 2-methyltaurine


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonate

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

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonate


enzyme_display_name: arachidonate 15-lipoxygenase

enzyme: arachidonate 15-lipoxygenase


enzyme_display_name: Hexahomomethionine N-hydroxylase

organism: Arabidopsis thaliana

substrate_name: pentahomomethionine

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

enzyme: Hexahomomethionine N-hydroxylase

substrate: pentahomomethionine


substrate_name: hexahomomethionine

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

substrate: hexahomomethionine


substrate_name: L-arginine

substrate: L-arginine


substrate_name: Unknown

ki_unit: mM

proof_lines:
wild type nNOS
wild type eNOS

substrate: Unknown


enzyme_display_name: UniProt O34453

organism: Bacillus subtilis

substrate_name: tetrahydrobiopterin

enzyme: UniProt O34453

substrate: tetrahydrobiopterin


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


enzyme_display_name: Cytochrome P450 71D178

organism: Origanum vulgare

substrate_name: gamma-terpinene

enzyme: Cytochrome P450 71D178

substrate: gamma-terpinene


enzyme_display_name: indoleamine 2,3-dioxygenase

substrate_name: L-tryptophan

enzyme: indoleamine 2,3-dioxygenase

substrate: L-tryptophan


enzyme_display_name: phenylacetaldehyde oxime monooxygenase

organism: Prunus mume

assay_conditions_summary: pH 7.6; cofactor NADPH

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

enzyme: phenylacetaldehyde oxime monooxygenase


substrate_name: phenylacetonitrile

substrate: phenylacetonitrile


substrate_name: (E)-phenylacetaldehyde oxime

substrate: (E)-phenylacetaldehyde oxime


enzyme_display_name: Cytochrome P450 71D180

organism: Thymus vulgaris

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

enzyme: Cytochrome P450 71D180


enzyme_display_name: aromatic aldoxime N-monooxygenase

substrate_name: (E)-p-hydroxyphenylacetaldehyde oxime

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

enzyme: aromatic aldoxime N-monooxygenase

substrate: (E)-p-hydroxyphenylacetaldehyde oxime


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

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


enzyme_display_name: Cytochrome P450 2U1

substrate_name: arachidonic acid

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

enzyme: Cytochrome P450 2U1

substrate: arachidonic acid


enzyme_display_name: flavonoid 3'-monooxygenase

organism: Citrus sinensis

substrate_name: naringenin

enzyme: flavonoid 3'-monooxygenase

substrate: naringenin


enzyme_display_name: Tabersonine 3-oxygenase

organism: Catharanthus roseus

substrate_name: tabersonine

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

enzyme: Tabersonine 3-oxygenase

substrate: tabersonine


substrate_name: Phenylacetaldoxime; NADPH; O2

assay_conditions_summary: cofactor NADP+

substrate: Phenylacetaldoxime; NADPH; O2


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


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

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

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

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


enzyme_display_name: tabersonine 3-oxygenase

substrate_name: Tabersonine; O2; NADPH

enzyme: tabersonine 3-oxygenase

substrate: Tabersonine; O2; NADPH


enzyme_display_name: Cytochrome P450 2C9

enzyme: Cytochrome P450 2C9


enzyme_display_name: UniProt Q00456

organism: Pseudomonas mendocina

substrate_name: Benzene

enzyme: UniProt Q00456

substrate: Benzene


substrate_name: Toluene

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

substrate: Toluene


substrate_name: anisole

substrate: anisole


substrate_name: chlorobenzene

substrate: chlorobenzene


substrate_name: nitrobenzene

substrate: nitrobenzene


substrate_name: methyl phenyl sulfide

substrate: methyl phenyl sulfide


enzyme_display_name: UniProt Q00459

enzyme: UniProt Q00459


enzyme_display_name: nitric-oxide synthase (flavodoxin)

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

enzyme: nitric-oxide synthase (flavodoxin)


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


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


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Helianthus tuberosus

substrate_name: NADPH

enzyme: trans-cinnamate 4-monooxygenase

substrate: NADPH


substrate_name: (E)-phenylacetaldehyde oxime


substrate_name: (E)-p-hydroxyphenylacetaldehyde oxime


substrate_name: tolbutamide

substrate: tolbutamide


substrate_name: diclofenac

substrate: diclofenac


substrate_name: losartan

substrate: losartan


enzyme_display_name: syn-pimaradiene 3-monooxygenase

organism: Oryza sativa subsp. japonica

substrate_name: ent-sandaracopimaradiene

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

enzyme: syn-pimaradiene 3-monooxygenase

substrate: ent-sandaracopimaradiene


substrate_name: ent-kaurene

substrate: ent-kaurene


enzyme_display_name: dimethylamine monooxygenase

organism: Cyberlindnera jadinii

substrate_name: diethylmethylamine

smiles: CCN(C)CC

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

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

enzyme: dimethylamine monooxygenase

substrate: diethylmethylamine


substrate_name: trimethylamine

smiles: CN(C)C

substrate: trimethylamine


substrate_name: dimethylethylamine

smiles: CCN(C)C

substrate: dimethylethylamine


substrate_name: triethylamine

smiles: CCN(CC)CC

substrate: triethylamine


substrate_name: Diethylamine

smiles: CCNCC

substrate: Diethylamine


substrate_name: dibutylamine

smiles: CCCCNCCCC

substrate: dibutylamine


substrate_name: NADH

substrate: NADH


substrate_name: methylbutylamine

smiles: CCCCNC

substrate: methylbutylamine


substrate_name: Dimethylamine

smiles: CNC

substrate: Dimethylamine


substrate_name: methyloctylamine

smiles: CCCCCCCCNC

substrate: methyloctylamine


substrate_name: Methylpropylamine

smiles: CCCNC

substrate: Methylpropylamine


substrate_name: methylethylamine

smiles: CCNC

substrate: methylethylamine


organism: Aminobacter aminovorans

assay_conditions_summary: pH 6.8; 301.15 K; cofactor NADH


substrate_name: NADPH

assay_conditions_summary: pH 6.8; 301.15 K; cofactor NADPH

substrate: NADPH


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


proof_lines: pH and temperature not specified in the publication


substrate_name: methyl-n-propylamine

substrate: methyl-n-propylamine


substrate_name: N-Methylethanolamine

smiles: CNCCO

substrate: N-Methylethanolamine


substrate_name: ethyl-n-propylamine

smiles: CCCNCC

substrate: ethyl-n-propylamine


substrate_name: n-butylmethylamine

substrate: n-butylmethylamine


organism: Sorghum bicolor

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

assay_conditions_summary: cofactor NADPH

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


enzyme_display_name: toluene 4-monooxygenase

organism: Burkholderia cepacia

substrate_name: methyl 4-tolyl sulfide

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

enzyme: toluene 4-monooxygenase

substrate: methyl 4-tolyl sulfide


substrate_name: methyl phenyl sulfide

substrate: methyl phenyl sulfide


substrate_name: ethylbutylamine

smiles: CCCCNCC

substrate: ethylbutylamine


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


substrate_name: methylisopropylamine

smiles: CC(C)NC

substrate: methylisopropylamine


substrate_name: dipropylamine

smiles: CCCNCCC

substrate: dipropylamine


substrate_name: Methylethanolamine

substrate: Methylethanolamine


substrate_name: propylbutylamine

smiles: CCCCNCCC

substrate: propylbutylamine


substrate_name: ethylpropylamine

substrate: ethylpropylamine


enzyme_display_name: 5-pyridoxate monooxygenase

organism: Pseudomonas sp.

substrate_name: 5-pyridoxic acid

enzyme: 5-pyridoxate monooxygenase

substrate: 5-pyridoxic acid


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: isoflavone 3'-hydroxylase

organism: Cicer arietinum

substrate_name: formononetin

enzyme: isoflavone 3'-hydroxylase

substrate: formononetin


substrate_name: Biochanin A

substrate: Biochanin A


enzyme_display_name: 4'-methoxyisoflavone 2'-hydroxylase

enzyme: 4'-methoxyisoflavone 2'-hydroxylase


enzyme_display_name: ent-kaurene monooxygenase

organism: Montanoa tomentosa

enzyme: ent-kaurene monooxygenase


organism: Physcomitrium patens

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


enzyme_display_name: 7-deoxyloganate 7-hydroxylase

organism: Lonicera japonica

enzyme: 7-deoxyloganate 7-hydroxylase


organism: Arthrobacter sp.

substrate_name: NADPH

substrate: NADPH


smiles: O=O


enzyme_display_name: Isoflavone 2'-hydroxylase

organism: Medicago truncatula

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

enzyme: Isoflavone 2'-hydroxylase


substrate_name: biochanin A

substrate: biochanin A


enzyme_display_name: Isoflavone 3'-hydroxylase

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

enzyme: Isoflavone 3'-hydroxylase


enzyme_display_name: 2-hydroxyisoflavanone synthase

organism: Glycyrrhiza echinata

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

enzyme: 2-hydroxyisoflavanone synthase


organism: Ectopseudomonas mendocina

substrate_name: Toluene

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

assay_conditions_summary: pH 7.5; cofactor NADH

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

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

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

row_label: DeltaN7 T4moD

table_label: Official ACS Table 4

substrate: Toluene


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

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

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

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

row_label: DeltaN4 T4moD


enzyme_display_name: Heme-dependent oxidative N-demethylase alpha subunit

organism: Ectopseudomonas mendocina (strain ymp)

substrate_name: dimethylamine

substrate: dimethylamine


enzyme_display_name: Indole-3-acetate monooxygenase

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

substrate_name: indole

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

enzyme: Indole-3-acetate monooxygenase

substrate: indole


substrate_name: NADH

substrate: NADH


enzyme_display_name: linalool 8-monooxygenase

organism: Pseudomonas putida

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

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

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

enzyme: linalool 8-monooxygenase


organism: Anthoceros agrestis

substrate_name: trans-cinnamate

substrate: trans-cinnamate


organism: Glycine max

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: pH 7.5, temperature not specified in the publication


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

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


enzyme_display_name: UniProt Q00456

organism: Pseudomonas mendocina

substrate_name: methyl 4-tolyl sulfide

enzyme: UniProt Q00456

substrate: methyl 4-tolyl sulfide


organism: Catharanthus roseus

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

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


substrate_name: O2; H+; NADPH; Liquiritigenin

substrate: O2; H+; NADPH; Liquiritigenin


substrate_name: H+; NADPH; O2; Biochanin A

assay_conditions_summary: pH 8; cofactor NADP+

column_label: Article prose states MtI3H kcat for biochanin A.

row_label: MtI3H / biochanin A

table_label: Kinetic properties prose section

substrate: H+; NADPH; O2; Biochanin A


substrate_name: O2; Formononetin; H+; NADPH

column_label: Article prose states MtI3H Km for formononetin.

raw_value_unit_evidence: Km 49.7 uM

row_label: MtI3H / formononetin

substrate: O2; Formononetin; H+; NADPH


enzyme_display_name: isoflavone 2'-hydroxylase

substrate_name: H+; Formononetin; NADPH; O2

enzyme: isoflavone 2'-hydroxylase

substrate: H+; Formononetin; NADPH; O2


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Helianthus tuberosus

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

assay_conditions_summary: pH 7.4; cofactor NADPH

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


enzyme_display_name: Ent-kaurene oxidase, chloroplastic

organism: Arabidopsis thaliana

substrate_name: ent-kaurene

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

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

row_label: ent-Kaurene (1)

table_label: Table 1

enzyme: Ent-kaurene oxidase, chloroplastic

substrate: ent-kaurene


substrate_name: ent-kaurenol

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

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

row_label: ent-Kaurenol (2)

substrate: ent-kaurenol


substrate_name: ent-kaurenal

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

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

row_label: ent-Kaurenal (3)

substrate: ent-kaurenal


substrate_name: ent-isokaurene

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

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

row_label: ent-Isokaurene (5)

table_label: Table 2

substrate: ent-isokaurene


substrate_name: ent-beyerene

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

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

row_label: ent-Beyerene (9)

substrate: ent-beyerene


substrate_name: Unknown

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

substrate: Unknown


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


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

unit: lgwedgeoneswedgeone

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


organism: Oryza sativa


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

enzyme: trans-cinnamate 4-monooxygenase

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


organism: Petroselinum crispum


substrate_name: Toluene

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

substrate: Toluene


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


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


enzyme_display_name: 7-deoxyloganic acid hydroxylase

substrate_name: 7-deoxyloganic acid

enzyme: 7-deoxyloganic acid hydroxylase

substrate: 7-deoxyloganic acid


substrate_name: NADPH

proof_lines:
CrDL7H
7-deoxyloganic acid
secologanin biosynthesis

substrate: NADPH


substrate_name: Biochanin A

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

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

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

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

row_label: MtI3'H (MtCYP81E9) / Biochanin A

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

substrate: Biochanin A


substrate_name: formononetin

substrate: formononetin


organism: Papaver somniferum


enzyme_display_name: Trans-cinnamate 4-monooxygenase

organism: Sorghum bicolor

substrate_name: trans-cinnamate

enzyme: Trans-cinnamate 4-monooxygenase

substrate: trans-cinnamate


substrate_name: 2-naphthoic acid

substrate: 2-naphthoic acid


substrate_name: chlorotoluron

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

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

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

row_label: Chlorotoluron

table_label: Table 5. CYP73 kinetic constants for various substrates

substrate: chlorotoluron


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

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

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


substrate_name: p-chloro-N-methylaniline

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

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

row_label: p-Chloro-N-methylaniline

substrate: p-chloro-N-methylaniline


enzyme_display_name: benzoate 4-monooxygenase

organism: Cystobasidium minutum

substrate_name: cinnamate

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

enzyme: benzoate 4-monooxygenase

substrate: cinnamate


substrate_name: benzoate

substrate: benzoate


enzyme_display_name: toluene 4-monooxygenase

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

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

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

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

row_label: Native T4moD

enzyme: toluene 4-monooxygenase


organism: Medicago truncatula

assay_conditions_summary: pH 8; cofactor NADPH

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

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

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

row_label: MtI2'H (MtCYP81E7) / formononetin


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

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

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

row_label: MtI2'H (MtCYP81E7) / Biochanin A


organism: Pseudomonas sp.

substrate_name: NADH

substrate: NADH


organism: Rhodotorula graminis


organism: Corydalis vaginans

substrate_name: cis-N-methylcanadine

substrate: cis-N-methylcanadine


enzyme_display_name: (S)-limonene 3-monooxygenase

organism: Mentha x piperita

substrate_name: (-)-limonene

enzyme: (S)-limonene 3-monooxygenase

substrate: (-)-limonene


organism: Cytospora rhizophorae

substrate_name: thioanisole

substrate: thioanisole


enzyme_display_name: Benzoate 4-monooxygenase bphA

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

enzyme: Benzoate 4-monooxygenase bphA


enzyme_display_name: Cytochrome P450 2C9

organism: Homo sapiens

substrate_name: S-mephenytoin

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

raw_value_unit_evidence: Km raw_value=1.25 mM raw_unit=mM

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

table_label: PubMed XML abstract PMID 3079764

enzyme: Cytochrome P450 2C9

substrate: S-mephenytoin


enzyme_display_name: Cytochrome P450 4F2

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

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

enzyme: Cytochrome P450 4F2


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


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


substrate_name: leukotriene B4

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

substrate: leukotriene B4


substrate_name: lipoxin A4

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

substrate: lipoxin A4


enzyme_display_name: Cytochrome P450 4F3

substrate_name: arachidonate

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

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

enzyme: Cytochrome P450 4F3

substrate: arachidonate


organism: Aspergillus niger


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


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


substrate_name: docosanoate

smiles: CCCCCCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: docosanoate


substrate_name: tetracosanoate

smiles: CCCCCCCCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: tetracosanoate


substrate_name: hexacosanoate

smiles: CCCCCCCCCCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexacosanoate


enzyme_display_name: protopine 6-monooxygenase

organism: Eschscholzia californica

enzyme: protopine 6-monooxygenase


organism: Glycine max

proof_lines: enzyme from elicitor-treated soybean cells


substrate_name: H+; Benzoate; O2; NADPH

substrate: H+; Benzoate; O2; NADPH


enzyme_display_name: leukotriene-B4 20-monooxygenase

organism: Rattus norvegicus

substrate_name: H+; NADH; Leukotriene B4; O2

enzyme: leukotriene-B4 20-monooxygenase

substrate: H+; NADH; Leukotriene B4; O2


substrate_name: menaquinone-4 (MK-4)

substrate: menaquinone-4 (MK-4)


enzyme_display_name: Cytochrome P450 4F1

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

enzyme: Cytochrome P450 4F1


organism: Curvularia lunata

substrate_name: Unknown

substrate: Unknown


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


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

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


enzyme_display_name: Cytochrome P450 4F4

enzyme: Cytochrome P450 4F4


substrate_name: H+; O2; NADPH; Protopine

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

substrate: H+; O2; NADPH; Protopine


substrate_name: 20-hydroxy-leukotriene B4

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

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

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

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

substrate: 20-hydroxy-leukotriene B4


substrate_name: lipoxin B4

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

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

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

row_label: Lipoxin B4

substrate: lipoxin B4


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

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

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


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

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


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

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

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


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

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

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


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

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

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

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


substrate_name: alpha-tocopherol

substrate: alpha-tocopherol


substrate_name: gamma-tocopherol

substrate: gamma-tocopherol


enzyme_display_name: (S)-limonene 6-monooxygenase

organism: Mentha spicata

substrate_name: (-)-limonene

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

enzyme: (S)-limonene 6-monooxygenase

substrate: (-)-limonene


organism: Ammi majus

substrate_name: trans-cinnamate

substrate: trans-cinnamate


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

organism: Artemisia annua

substrate_name: artemisinic aldehyde

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

substrate: artemisinic aldehyde


substrate_name: dihydroartemisinic aldehyde

substrate: dihydroartemisinic aldehyde


enzyme_display_name: amorpha-4,11-diene 12 monooxygenase

enzyme: amorpha-4,11-diene 12 monooxygenase


substrate_name: protopine

substrate: protopine


enzyme_display_name: Protopine 6-monooxygenase

substrate_name: allocryptopine

enzyme: Protopine 6-monooxygenase

substrate: allocryptopine


substrate_name: picolinate

substrate: picolinate


substrate_name: nicotinate

substrate: nicotinate


enzyme_display_name: 2-hydroxyisoflavanone synthase

organism: Glycyrrhiza echinata

substrate_name: liquiritigenin

proof_lines:
Glycyrrhiza echinata
2-hydroxyisoflavanone synthase
liquiritigenin

enzyme: 2-hydroxyisoflavanone synthase

substrate: liquiritigenin


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Anthoceros agrestis

substrate_name: NADPH

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

raw_value_unit_evidence: Km raw_value=60 microM raw_unit=microM

row_label: Anthoceros agrestis cinnamic acid 4-hydroxylase / NADPH

table_label: PubMed XML abstract PMID 12721853

enzyme: trans-cinnamate 4-monooxygenase

substrate: NADPH


enzyme_display_name: Trans-cinnamate 4-monooxygenase

organism: Helianthus tuberosus

substrate_name: 2-naphthoic acid

enzyme: Trans-cinnamate 4-monooxygenase

substrate: 2-naphthoic acid


enzyme_display_name: indoleamine 2,3-dioxygenase

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

enzyme: indoleamine 2,3-dioxygenase


organism: Arabidopsis thaliana

assay_conditions_summary: 303.15 K; cofactor NADPH

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


substrate_name: 2-chlorocinnamic acid

substrate: 2-chlorocinnamic acid


substrate_name: 2-fluorocinnamic acid

substrate: 2-fluorocinnamic acid


substrate_name: 3-hydroxycinnamic acid

substrate: 3-hydroxycinnamic acid


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

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


enzyme_display_name: ent-kaurene monooxygenase

proof_lines: pH and temperature not specified in the publication

enzyme: ent-kaurene monooxygenase


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


substrate_name: ent-sandaracopimaradiene

substrate: ent-sandaracopimaradiene


substrate_name: ent-cassadiene

substrate: ent-cassadiene


enzyme_display_name: methyl farnesoate epoxidase

organism: Locusta migratoria

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

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

enzyme: methyl farnesoate epoxidase

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


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Pseudomonas aeruginosa

enzyme: protocatechuate 3,4-dioxygenase


substrate_name: protocatechuate

substrate: protocatechuate


smiles: O=O


enzyme_display_name: catechol 1,2-dioxygenase

enzyme: catechol 1,2-dioxygenase


substrate_name: catechol

substrate: catechol


enzyme_display_name: 6-hydroxynicotinate 3-monooxygenase

organism: Pseudomonas fluorescens

enzyme: 6-hydroxynicotinate 3-monooxygenase


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: catechol 2,3-dioxygenase

organism: Pseudomonas putida

enzyme: catechol 2,3-dioxygenase


enzyme_display_name: UniProt A2TEF2

organism: Leishmania infantum

substrate_name: obtusifoliol

enzyme: UniProt A2TEF2

substrate: obtusifoliol


substrate_name: lanosterol

substrate: lanosterol


enzyme_display_name: benzoate 1,2-dioxygenase

enzyme: benzoate 1,2-dioxygenase


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NADH-cytochrome c reductase component

substrate: NADH-cytochrome c reductase component


enzyme_display_name: phenylacetyl-CoA 1,2-epoxidase

organism: Pseudomonas sp.

enzyme: phenylacetyl-CoA 1,2-epoxidase


substrate_name: epoxyphenylacetyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: epoxyphenylacetyl-CoA


substrate_name: NADPH

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: tryptophan 2-monooxygenase

organism: Pseudomonas savastanoi

substrate_name: L-tryptophan

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

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

enzyme: tryptophan 2-monooxygenase

substrate: L-tryptophan


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


enzyme_display_name: sterol 14alpha-demethylase

enzyme: sterol 14alpha-demethylase


organism: Malassezia globosa


substrate_name: eburicol

substrate: eburicol


enzyme_display_name: angelicin synthase

organism: Kitagawia praeruptora

substrate_name: (+)-columbianetin

enzyme: angelicin synthase

substrate: (+)-columbianetin


organism: Trypanosoma brucei


organism: Naegleria fowleri

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


organism: Aspergillus fumigatus

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


organism: Pastinaca sativa

assay_conditions_summary: pH 7

proof_lines: pH 7.0, isopropyloxy-hydroxylation of substrate


enzyme_display_name: 5-epiaristolochene 1,3-dihydroxylase

organism: Nicotiana tabacum

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

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

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

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

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

enzyme: 5-epiaristolochene 1,3-dihydroxylase


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

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

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

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

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


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

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

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

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

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


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

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