sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R242E to reconstruct the assayed variant sequence.


enzyme_display_name: 2-hydroxybiphenyl 3-monooxygenase

organism: Pseudomonas nitroreducens

substrate_name: NADH

source_db: brenda

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

mutation_type: substitution

assay_conditions_summary: pH 7.5; cofactor NADH

data_origin: experimental

enzyme: 2-hydroxybiphenyl 3-monooxygenase

substrate: NADH

status: unverified

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R242Q to reconstruct the assayed variant sequence.


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W225A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G255F to reconstruct the assayed variant sequence.


mutation_signature: Unknown

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

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


verification_status: corrected

assay_conditions_summary: pH 7.5; buffer 50 mM phosphate; cofactor NADH

column_label: Table 2. Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH.; row WT / NADH; 2-Hydroxybiphenyl/NADH metric block; columns Km (uM), kcat (sec^-1), kcat/Km (sec^-1 uM^-1); cells Km=149 +/- 22 uM, kcat=3.16 sec^-1, kcat/Km=0.02 sec^-1 uM^-1

normalized_value_unit_evidence: Km normalized_value=0.149 normalized_unit=mM; kcat normalized_value=3.16 normalized_unit=s^-1; kcat/Km normalized_value=20 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=149 +/- 22 raw_unit=uM; kcat raw_value=3.16 raw_unit=sec^-1; kcat/Km raw_value=0.02 raw_unit=sec^-1 uM^-1

row_label: WT / NADH

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W225Y to reconstruct the assayed variant sequence.


enzyme_display_name: 2-hydroxycyclohexanone 2-monooxygenase

organism: Acinetobacter sp.

substrate_name: NADPH

kcat_display: Not reported

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.

assay_conditions_summary: cofactor NADPH

enzyme: 2-hydroxycyclohexanone 2-monooxygenase

substrate: NADPH


enzyme_display_name: nitric-oxide synthase

organism: Oncorhynchus mykiss

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

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

assay_conditions_summary: cofactor NADP+

unit: lswedgeone

enzyme: nitric-oxide synthase

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


organism: Rattus norvegicus

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

ki_unit: mM

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


substrate_name: L-Arginine; NADPH; O2

substrate: L-Arginine; NADPH; O2


enzyme_display_name: alkene monooxygenase

organism: Gordonia rubripertincta

substrate_name: Propene

smiles: CC=C

enzyme: alkene monooxygenase

substrate: Propene


substrate_name: trichlorethene

smiles: C(=C(Cl)Cl)Cl

substrate: trichlorethene


enzyme_display_name: phenylacetone monooxygenase

organism: Thermobifida fusca

substrate_name: cyclohexanone

source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67A/P440F to reconstruct the assayed variant sequence.

enzyme: phenylacetone monooxygenase

substrate: cyclohexanone

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67C/P440F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67G/P440F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67Y/P440F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P440F to reconstruct the assayed variant sequence.


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Drosophila melanogaster

proof_lines:
CaM-bound recombinant eNOS
CaM-free recombinant eNOS

enzyme: nitric-oxide synthase (NADPH)


substrate_name: O2; H+; NADH; 4,4-Dimethyl-5alpha-cholest-7-en-3beta-ol

assay_conditions_summary: cofactor NADH


enzyme_display_name: cyclopentanone monooxygenase

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

proof_lines: recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C

enzyme: cyclopentanone monooxygenase


substrate_name: Cyclopentanone

substrate: Cyclopentanone


smiles: CCCCCCC(=O)C


organism: Pseudomonas sp.


organism: Mus musculus

substrate_name: L-arginine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W457A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

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

substrate: L-arginine


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM phosphate; cofactor NADH

table_label: Table 2. Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature G255F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer absorption at 340 nm in 50 mM phosphate; cofactor NADH

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'G255F', 2-Hydroxybiphenyl column group; column 'Km (uM)' = 26.6; column 'kcat (sec-1)' = 0.71; column 'kcat/Km (sec-1 uM-1)' = 0.03. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.71 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.71 s^(-1). Km: printed Table 2 cell 26.6 in a column headed Km (uM); 26.6 / 1000 = 0.0266 mM. kcat/Km: printed Table 2 cell 0.03 in a column headed kcat/Km (sec-1 uM-1), that is 0.03 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.03 x 1000 = 30.0 s^-1 mM^-1. The exported values are kcat 0.71 s^(-1), Km 0.0266 mM and kcat_over_km 26.69172932330827 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'G255F', 2-Hydroxybiphenyl column group: Km = 26.6 uM; kcat = 0.71 sec-1; printed kcat/Km = 0.03 in a column headed (sec-1 uM-1), that is 0.03 s^(-1)*uM^(-1).

row_label: Table 2, row G255F, 2-Hydroxybiphenyl column group

table_label: Table 2: Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH (Biochimica et Biophysica Acta 1854 (2015) 1906-1913). Printed column heads: Variant; 2-Hydroxybiphenyl Km (uM), kcat (sec-1), kcat/Km (sec-1 uM-1); NADH Km (uM), kcat (sec-1), kcat/Km (sec-1 uM-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature W225A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225A', 2-Hydroxybiphenyl column group; column 'Km (uM)' = 29.5; column 'kcat (sec-1)' = 0.46; column 'kcat/Km (sec-1 uM-1)' = 0.02. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.46 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.46 s^(-1). Km: printed Table 2 cell 29.5 in a column headed Km (uM); 29.5 / 1000 = 0.0295 mM. kcat/Km: printed Table 2 cell 0.02 in a column headed kcat/Km (sec-1 uM-1), that is 0.02 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.02 x 1000 = 20.0 s^-1 mM^-1. The exported values are kcat 0.46 s^(-1), Km 0.0295 mM and kcat_over_km 15.593220338983052 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225A', 2-Hydroxybiphenyl column group: Km = 29.5 uM; kcat = 0.46 sec-1; printed kcat/Km = 0.02 in a column headed (sec-1 uM-1), that is 0.02 s^(-1)*uM^(-1).

row_label: Table 2, row W225A, 2-Hydroxybiphenyl column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature W225Y to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225Y', 2-Hydroxybiphenyl column group; column 'Km (uM)' = 22.8; column 'kcat (sec-1)' = 4.51; column 'kcat/Km (sec-1 uM-1)' = 0.2. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.51 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 4.51 s^(-1). Km: printed Table 2 cell 22.8 in a column headed Km (uM); 22.8 / 1000 = 0.0228 mM. kcat/Km: printed Table 2 cell 0.2 in a column headed kcat/Km (sec-1 uM-1), that is 0.2 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.2 x 1000 = 200.0 s^-1 mM^-1. The exported values are kcat 4.51 s^(-1), Km 0.0228 mM and kcat_over_km 197.80701754385964 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225Y', 2-Hydroxybiphenyl column group: Km = 22.8 uM; kcat = 4.51 sec-1; printed kcat/Km = 0.2 in a column headed (sec-1 uM-1), that is 0.2 s^(-1)*uM^(-1).

row_label: Table 2, row W225Y, 2-Hydroxybiphenyl column group


column_label: Table 2. Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH.; row WT / 2-Hydroxybiphenyl; 2-Hydroxybiphenyl/NADH metric block; columns Km (uM), kcat (sec^-1), kcat/Km (sec^-1 uM^-1); cells Km=3.1 +/- 0.3 uM, kcat=2.26 sec^-1, kcat/Km=0.73 sec^-1 uM^-1

normalized_value_unit_evidence: Km normalized_value=0.0031 normalized_unit=mM; kcat normalized_value=2.26 normalized_unit=s^-1; kcat/Km normalized_value=730 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3.1 +/- 0.3 raw_unit=uM; kcat raw_value=2.26 raw_unit=sec^-1; kcat/Km raw_value=0.73 raw_unit=sec^-1 uM^-1

row_label: WT / 2-Hydroxybiphenyl


column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'G255F', NADH column group; column 'Km (uM)' = 531; column 'kcat (sec-1)' = 1.34; column 'kcat/Km (sec-1 uM-1)' = 2.53 x 10^-3. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.34 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 1.34 s^(-1). Km: printed Table 2 cell 531 in a column headed Km (uM); 531 / 1000 = 0.531 mM. kcat/Km: printed Table 2 cell 2.53 x 10^-3 in a column headed kcat/Km (sec-1 uM-1), that is 0.00253 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00253 x 1000 = 2.53 s^-1 mM^-1. The exported values are kcat 1.34 s^(-1), Km 0.531 mM and kcat_over_km 2.5235404896421847 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'G255F', NADH column group: Km = 531 uM; kcat = 1.34 sec-1; printed kcat/Km = 2.53 x 10^-3 in a column headed (sec-1 uM-1), that is 0.00253 s^(-1)*uM^(-1).

row_label: Table 2, row G255F, NADH column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature R242A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'R242A', NADH column group; column 'Km (uM)' = 446; column 'kcat (sec-1)' = 0.14; column 'kcat/Km (sec-1 uM-1)' = 3.14 x 10^-4. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.14 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.14 s^(-1). Km: printed Table 2 cell 446 in a column headed Km (uM); 446 / 1000 = 0.446 mM. kcat/Km: printed Table 2 cell 3.14 x 10^-4 in a column headed kcat/Km (sec-1 uM-1), that is 0.000314 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.000314 x 1000 = 0.314 s^-1 mM^-1. The exported values are kcat 0.14 s^(-1), Km 0.336 mM and kcat_over_km 0.4166666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'R242A', NADH column group: Km = 446 uM; kcat = 0.14 sec-1; printed kcat/Km = 3.14 x 10^-4 in a column headed (sec-1 uM-1), that is 0.000314 s^(-1)*uM^(-1).

row_label: Table 2, row R242A, NADH column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature R242E to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'R242E', NADH column group; column 'Km (uM)' = 427; column 'kcat (sec-1)' = 0.15; column 'kcat/Km (sec-1 uM-1)' = 3.51 x 10^-4. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.15 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.15 s^(-1). Km: printed Table 2 cell 427 in a column headed Km (uM); 427 / 1000 = 0.427 mM. kcat/Km: printed Table 2 cell 3.51 x 10^-4 in a column headed kcat/Km (sec-1 uM-1), that is 0.000351 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.000351 x 1000 = 0.351 s^-1 mM^-1. The exported values are kcat 0.15 s^(-1), Km 0.427 mM and kcat_over_km 0.351288056206089 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'R242E', NADH column group: Km = 427 uM; kcat = 0.15 sec-1; printed kcat/Km = 3.51 x 10^-4 in a column headed (sec-1 uM-1), that is 0.000351 s^(-1)*uM^(-1).

row_label: Table 2, row R242E, NADH column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature R242Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'R242Q', NADH column group; column 'Km (uM)' = 222; column 'kcat (sec-1)' = 0.24; column 'kcat/Km (sec-1 uM-1)' = 1.08 x 10^-3. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.24 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.24 s^(-1). Km: printed Table 2 cell 222 in a column headed Km (uM); 222 / 1000 = 0.222 mM. kcat/Km: printed Table 2 cell 1.08 x 10^-3 in a column headed kcat/Km (sec-1 uM-1), that is 0.00108 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00108 x 1000 = 1.08 s^-1 mM^-1. The exported values are kcat 0.24 s^(-1), Km 0.222 mM and kcat_over_km 1.081081081081081 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'R242Q', NADH column group: Km = 222 uM; kcat = 0.24 sec-1; printed kcat/Km = 1.08 x 10^-3 in a column headed (sec-1 uM-1), that is 0.00108 s^(-1)*uM^(-1).

row_label: Table 2, row R242Q, NADH column group


column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225A', NADH column group; column 'Km (uM)' = 253; column 'kcat (sec-1)' = 3.45; column 'kcat/Km (sec-1 uM-1)' = 0.014. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.45 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 3.45 s^(-1). Km: printed Table 2 cell 253 in a column headed Km (uM); 253 / 1000 = 0.253 mM. kcat/Km: printed Table 2 cell 0.014 in a column headed kcat/Km (sec-1 uM-1), that is 0.014 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.014 x 1000 = 14.0 s^-1 mM^-1. The exported values are kcat 3.45 s^(-1), Km 0.253 mM and kcat_over_km 13.636363636363637 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225A', NADH column group: Km = 253 uM; kcat = 3.45 sec-1; printed kcat/Km = 0.014 in a column headed (sec-1 uM-1), that is 0.014 s^(-1)*uM^(-1).

row_label: Table 2, row W225A, NADH column group


column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225Y', NADH column group; column 'Km (uM)' = 102; column 'kcat (sec-1)' = 5.8; column 'kcat/Km (sec-1 uM-1)' = 0.057. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.8 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 5.8 s^(-1). Km: printed Table 2 cell 102 in a column headed Km (uM); 102 / 1000 = 0.102 mM. kcat/Km: printed Table 2 cell 0.057 in a column headed kcat/Km (sec-1 uM-1), that is 0.057 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.057 x 1000 = 57.0 s^-1 mM^-1. The exported values are kcat 5.8 s^(-1), Km 0.102 mM and kcat_over_km 56.86274509803922 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225Y', NADH column group: Km = 102 uM; kcat = 5.8 sec-1; printed kcat/Km = 0.057 in a column headed (sec-1 uM-1), that is 0.057 s^(-1)*uM^(-1).

row_label: Table 2, row W225Y, NADH column group


smiles: O=O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I67Y/P440F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


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


sequence_variant_note: Mutation signature I67G/P440F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I67A/P440F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I67C/P440F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: phenylacetone

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

proof_lines:
mutant P3
mutant P1
mutant P2

substrate: phenylacetone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R217L with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220Q/K336N to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant H220Q/K336N


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K336H with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K336N with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220Q/K336H to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant H220Q/K336H


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R217A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220T 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.

proof_lines: pH 8.0, 30°C, recombinant wild-type PAMO


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T218A to reconstruct the assayed variant sequence.


sequence_source: multiple

smiles: CCCCCCCCCCC(=O)C

assay_conditions_summary: pH 7.5; cofactor NADPH

source_databases_merged: brenda uniprot


substrate_name: benzylacetone

substrate: benzylacetone


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

proof_lines: pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q


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

proof_lines: pH 8.0, 25°C, recombinant mutant A442P/L443V


organism: Mycobacterium tuberculosis

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

proof_lines: 25°C, pH 8.5, in the presence of 0.006 mM bovine serum albumin


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P253F/G254A/R258M/L443F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C


enzyme_display_name: senecionine N-oxygenase

organism: Arctia caja

substrate_name: senecionine

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

enzyme: senecionine N-oxygenase

substrate: senecionine


substrate_name: monocrotaline

substrate: monocrotaline


substrate_name: heliotrine

substrate: heliotrine


organism: Creatonotos transiens


organism: Comamonas sp. NCIMB 9872

substrate_name: Cyclopentanone; O2; NADPH; H+

substrate: Cyclopentanone; O2; NADPH; H+


substrate_name: H+; NADPH; Ethionamide; O2

substrate: H+; NADPH; Ethionamide; O2


organism: Zonocerus variegatus

assay_conditions_summary: pH 9; 310.15 K; buffer 100 mM glycine/NaOH

proof_lines: in 100 mM glycine/NaOH buffer pH 9.0, at 37°C


substrate_name: phalaenopsine

substrate: phalaenopsine


substrate_name: atropine

substrate: atropine


enzyme_display_name: UniProt A6T923

organism: Klebsiella pneumoniae

substrate_name: NADH

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A6T923

substrate: NADH

source: skid


enzyme_display_name: monocyclic monoterpene ketone monooxygenase

organism: Rhodococcus erythropolis

sequence: MQTIPSTTETAADFDAVIXGAGFXGLYALHR

proof_lines: kcat is 3.9 sec(-1) with (4R)-dihydrocarvone as substrate. kcat is 4.9 sec(-1) with (1R,4S)-1-hydroxy-2-oxolimonene as substrate. kcat is 3.9 sec(-1) with (1S,4R)-1-hydroxy-2-oxolimonene as substrate. kcat is 3.6 sec(-1) with (1R,4S)-mentho


enzyme: monocyclic monoterpene ketone monooxygenase


substrate_name: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q47PU3 and applied mutation signature R258M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: Table 1 carries a substrate-block column, a PAMO construct column and three kinetic columns headed K_M [mM], k_cat [s^-1] and k_cat/K_M [M^-1 s^-1]. The cited cell set is the 2-Octanone block, PAMO row R258M: K_M [mM] = 0.3; k_cat [s^-1] = 0.067; k_cat/K_M [M^-1 s^-1] = 2.3 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.067 in the 2-Octanone block of PAMO row R258M under the column head k_cat [s^-1]; the column is already per second, so no unit conversion applies and the paper value is 0.067 s^(-1). Km: printed Table 1 cell 0.3 under the column head K_M [mM]; the column is already in mM, so no unit conversion applies and the paper value is 0.3 mM. kcat/Km: printed Table 1 cell 2.3 x 10^2 under the column head k_cat/K_M [M^-1 s^-1], that is 230.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 230.0 / 1000 = 0.23 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Octanone block, PAMO row R258M: K_M = 0.3 mM; k_cat = 0.067 s^-1; printed k_cat/K_M = 2.3 x 10^2 M^-1 s^-1.

table_label: Table 1: Steady-state kinetic parameters of PAMO WT and variants R258A, R258M and P253F/G254A/R258M/L443F for the conversion of 2-octanone (Phys. Chem. Chem. Phys., 2018, 20, 2558-2570)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q47PU3 and applied mutation signature R258A to reconstruct the assayed variant sequence.

column_label: Table 1 carries a substrate-block column, a PAMO construct column and three kinetic columns headed K_M [mM], k_cat [s^-1] and k_cat/K_M [M^-1 s^-1]. The cited cell set is the 2-Octanone block, PAMO row R258A: K_M [mM] = 2.1; k_cat [s^-1] = 0.091; k_cat/K_M [M^-1 s^-1] = 43.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.091 in the 2-Octanone block of PAMO row R258A under the column head k_cat [s^-1]; the column is already per second, so no unit conversion applies and the paper value is 0.091 s^(-1). Km: printed Table 1 cell 2.1 under the column head K_M [mM]; the column is already in mM, so no unit conversion applies and the paper value is 2.1 mM. kcat/Km: printed Table 1 cell 43 under the column head k_cat/K_M [M^-1 s^-1], that is 43.0 M^-1 s^-1, a value the paper also restates in prose as the catalytic efficiency of R258A; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 43.0 / 1000 = 0.043 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Octanone block, PAMO row R258A: K_M = 2.1 mM; k_cat = 0.091 s^-1; printed k_cat/K_M = 43 M^-1 s^-1.


column_label: Table 1 (printed page 2563, PDF page 6), wave-12 decoded plain-numeral transcription, substrate block `2-Octanone`, PAMO sub-row `WT^17`: column `KM [mM]` = 3.2; column `kcat [s^-1]` = 0.22; column `kcat/KM [M^-1 s^-1]` = 66.

normalized_value_unit_evidence: kcat: printed cell 0.22 s^-1 -> 0.22 s^(-1); no unit conversion applies because the column is printed in s^-1. Km: printed cell 3.2 mM -> 3.2 mM; no unit conversion applies because the column is printed in mM. kcat/Km: the paper PRINTS the kcat/KM cell 66 M^-1 s^-1 for this row, and that printed cell is the kcat_over_km value reported here; 66 M^-1 s^-1 divided by 1000 gives 0.066 s^(-1)*mM^(-1). The live export row holds kcat 1.0 s^(-1), km 2.0 mM and kcat_over_km 0.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Raw printed cells for `2-Octanone` `WT^17`: KM = 3.2 mM; kcat = 0.22 s^-1; kcat/KM = 66 M^-1 s^-1.

table_label: Table 1 (printed page 2563, PDF page 6), wave-12 decoded plain-numeral transcription of the steady-state kinetic parameters of PAMO


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


substrate_name: NADPH; (4R)-Dihydrocarvone; O2; H+

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

substrate: NADPH; (4R)-Dihydrocarvone; O2; H+


enzyme_display_name: Methanesulfonate monooxygenase ferredoxin subunit

organism: Methylosulfonomonas methylovora

source_db: uniprot

proof_lines: Cell-free extracts of MSA-grown strain M2 have been used. Vmax of a cytoplasmic fraction has shown to be lower as was that of a reconstituted enzyme from partially purified fractions which was increased by addition of FAD and Fe(2+).

source: uniprot


substrate_name: ethane sulfonic acid

smiles: CCS(=O)(=O)O

assay_conditions_summary: cofactor FAD

enzyme: Methanesulfonate monooxygenase ferredoxin subunit

substrate: ethane sulfonic acid


enzyme_display_name: Putative methanesulfonate monooxygenase ferredoxin reductase subunit


enzyme: Putative methanesulfonate monooxygenase ferredoxin reductase subunit


enzyme_display_name: Methanesulfonate monooxygenase hydroxylase subunit alpha


enzyme: Methanesulfonate monooxygenase hydroxylase subunit alpha


enzyme_display_name: Methanesulfonate monooxygenase hydroxylase subunit beta


enzyme: Methanesulfonate monooxygenase hydroxylase subunit beta


enzyme_display_name: 2,6-dihydroxypyridine 3-monooxygenase

organism: Arthrobacter nicotinovorans

enzyme: 2,6-dihydroxypyridine 3-monooxygenase


assay_conditions_summary: cofactor NAD+


enzyme_display_name: NO-associated protein 1, chloroplastic/mitochondrial

organism: Arabidopsis thaliana

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


substrate_name: methyl 4-tolylsulfide

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

substrate: methyl 4-tolylsulfide


enzyme_display_name: FAD-dependent urate hydroxylase

organism: Xanthomonas campestris

sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

assay_conditions_summary: pH 8; 298.15 K; buffer context; cofactor NADH

proof_lines: in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C

enzyme: FAD-dependent urate hydroxylase


substrate_name: Urate

assay_conditions_summary: pH 8; buffer context; cofactor FAD

substrate: Urate


assay_conditions_summary: pH 8; 298.15 K; buffer context; cofactor NADPH


organism: Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1)

substrate_name: urate

proof_lines: kcat is 56.0 sec(-1) for the NADH-dependent oxidation of urate. Exhibits a Michaelian behavior only toward urate and a cooperative behavior toward NADH and NADPH.

substrate: urate


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

proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=25°C, pH=8
kcat is 42 sec(-1).

source_databases_merged: skid uniprot


enzyme_display_name: 2-hydroxybiphenyl 3-monooxygenase

organism: Pseudomonas nitroreducens

sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NADH

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223A.

table_label: Table 1, Km and kcat values of engineered HbpA variants on 2HBP


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223E to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223E.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223I to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223I.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223K to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223K.

raw_value_unit_evidence: Table 1 row M223K: Km 6.5 uM; kcat 1.97 s^-1; kcat/Km 0.3 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223Q to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223Q.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321A to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321A.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321F to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321F.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321L to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321L.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321V to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321V.


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature W97A to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant W97A.

raw_value_unit_evidence: Table 1 row W97A: Km 6 uM; kcat 0.48 s^-1; kcat/Km 0.08 s^-1 uM^-1.

status: verified


organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)

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

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 1.06 sec(-1) for the NADPH-dependent oxidation of urate.


organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)

proof_lines: kcat is 23.6 sec(-1) for the NADH-dependent oxidation of urate. Exhibits a Michaelian behavior toward urate and NADPH and a cooperative behavior toward NADH.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W97Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

proof_lines:
2-hydroxybiphenyl 3-monooxygenase
2-substituted phenols
M321A


enzyme_display_name: 6-hydroxynicotinate 3-monooxygenase

organism: Bordetella bronchiseptica

assay_conditions_summary: pH 7.5; cofactor NADH

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

table_label: Table 3

enzyme: 6-hydroxynicotinate 3-monooxygenase


assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: kcat is 4.2 sec(-1) with 6-hydroxynicotinate as substrate (at pH 7.5 and 25 degrees Celsius) (PubMed:27218267). kcat is 5.1 sec(-1) with 6-hydroxynicotinate as substrate. kcat is 0.074 sec(-1) with 4-hydroxybenzoate as substrate. kcat is 2.


proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme


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

proof_lines:
pH 7.5, 25°C, recombinant mutant C202A
mutant enzyme C202A, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant H302A
mutant enzyme H302A, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant Y225F
mutant enzyme Y225F, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant H211A
mutant enzyme H211A, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant Y215F
mutant enzyme Y215F, at pH 7.5 and 25°C


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: 6-hydroxynicotinate (at pH 7.5 and 25 degrees Celsius)

proof_lines: kcat is 2.2 sec(-1) with 6-hydroxynicotinate as substrate (at pH 7.5 and 25 degrees Celsius).


substrate_name: NADH (at pH 7.5 and 25 degrees Celsius)

substrate: NADH (at pH 7.5 and 25 degrees Celsius)


organism: Thermobifida fusca

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q47PU3 and applied mutation signature P253F/G254A/R258M/L443F to reconstruct the assayed variant sequence.

smiles: CCCCCCC(C)=O

column_label: Table 1; row 2-Octanone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 2.3 s^-1; paper kcat 2.3 s^-1; current Km 0.25 mM; paper Km 0.25 mM; current kcat/Km 9.2 s^-1 mM^-1; paper kcat/Km 9.2 s^-1 mM^-1

raw_value_unit_evidence: current kcat 2.3 s^-1; paper kcat 2.3 s^-1; current Km 0.25 mM; paper Km 0.25 mM; current kcat/Km 9.2 s^-1 mM^-1; paper kcat/Km 9.2 x 10^3 M^-1 s^-1

table_label: Table 1. Steady-state kinetic parameters of PAMO WT and variants R258A, R258M and P253F/G254A/R258M/L443F


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q47PU3 and applied mutation signature R258A to reconstruct the assayed variant sequence.

column_label: Table 1; row 2-Octanone / R258A, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.091 s^-1; paper kcat 0.091 s^-1; current Km 2.1 mM; paper Km 2.1 mM; current kcat/Km 0.0433333333333 s^-1 mM^-1; paper kcat/Km 0.043 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.091 s^-1; paper kcat 0.091 s^-1; current Km 2.1 mM; paper Km 2.1 mM; current kcat/Km 0.0433333333333 s^-1 mM^-1; paper kcat/Km 43 M^-1 s^-1

row_label: 2-Octanone / R258A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q47PU3 and applied mutation signature R258M to reconstruct the assayed variant sequence.

column_label: Table 1; row 2-Octanone / R258M, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.067 s^-1; paper kcat 0.067 s^-1; current Km 0.3 mM; paper Km 0.3 mM; current kcat/Km 0.223333333333 s^-1 mM^-1; paper kcat/Km 0.23 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.067 s^-1; paper kcat 0.067 s^-1; current Km 0.3 mM; paper Km 0.3 mM; current kcat/Km 0.223333333333 s^-1 mM^-1; paper kcat/Km 2.3 x 10^2 M^-1 s^-1

row_label: 2-Octanone / R258M


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P253F/G254A/R258M/L443F to reconstruct the assayed variant sequence.

column_label: Table 1; row 2-Octanone / WT, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.22 s^-1; paper kcat 0.22 s^-1; current Km 3.2 mM; paper Km 3.2 mM; current kcat/Km 0.06875 s^-1 mM^-1; paper kcat/Km 0.066 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.22 s^-1; paper kcat 0.22 s^-1; current Km 3.2 mM; paper Km 3.2 mM; current kcat/Km 0.06875 s^-1 mM^-1; paper kcat/Km 66 M^-1 s^-1

row_label: 2-Octanone / WT


column_label: Table 1; row 2-Phenylcyclohexanone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.3 s^-1; paper kcat 0.3 s^-1; current Km 0.8 mM; paper Km 0.8 mM; current kcat/Km 0.375 s^-1 mM^-1; paper kcat/Km 0.37 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.3 s^-1; paper kcat 0.3 s^-1; current Km 0.8 mM; paper Km 0.8 mM; current kcat/Km 0.375 s^-1 mM^-1; paper kcat/Km 3.7 x 10^2 M^-1 s^-1


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


substrate_name: Cyclopentanone

column_label: Table 1; row Cyclopentanone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 1.6 s^-1; paper kcat 1.6 s^-1; current Km 1000 mM; paper Km 1000 mM; current kcat/Km 0.0016 s^-1 mM^-1; paper kcat/Km 0.0016 s^-1 mM^-1

raw_value_unit_evidence: current kcat 1.6 s^-1; paper kcat 1.6 s^-1; current Km 1000 mM; paper Km 1000 mM; current kcat/Km 0.0016 s^-1 mM^-1; paper kcat/Km 1.6 M^-1 s^-1

substrate: Cyclopentanone


substrate_name: phenylacetone

column_label: Table 1; row Phenylacetone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.04 s^-1; paper kcat 0.04 s^-1; current Km 1.4 mM; paper Km 1.4 mM; current kcat/Km 0.0285714285714 s^-1 mM^-1; paper kcat/Km 35 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.04 s^-1; paper kcat 0.04 s^-1; current Km 1.4 mM; paper Km 1.4 mM; current kcat/Km 0.0285714285714 s^-1 mM^-1; paper kcat/Km 3.5 x 10^4 M^-1 s^-1

row_label: Phenylacetone / P253F/G254A/R258M/L443F

substrate: phenylacetone


column_label: Table 1; row Phenylacetone / R258A, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 2.1 s^-1; paper kcat 2.1 s^-1; current Km 0.17 mM; paper Km 0.17 mM; current kcat/Km 12.3529411765 s^-1 mM^-1; paper kcat/Km 0.012 s^-1 mM^-1

raw_value_unit_evidence: current kcat 2.1 s^-1; paper kcat 2.1 s^-1; current Km 0.17 mM; paper Km 0.17 mM; current kcat/Km 12.3529411765 s^-1 mM^-1; paper kcat/Km 12 M^-1 s^-1

row_label: Phenylacetone / R258A


substrate_name: 6-Hydroxynicotinate; H+; NADH; O2

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

source_databases_merged: sabio_rk brenda uniprot

substrate: 6-Hydroxynicotinate; H+; NADH; O2


organism: Pseudomonas fluorescens


organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)

substrate_name: 4-hydroxybenzoate (at pH 7.5 and 25 degrees Celsius)

column_label: Table 1 row 4-HBA; column KSM; footnote states pH 7.5 and 25 C.

normalized_value_unit_evidence: Km 0.6 mM.

raw_value_unit_evidence: Table 1 row 4-HBA reports KSM 600 +/- 100 uM.

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


enzyme_display_name: UniProt H9N289

organism: Pseudomonas putida

substrate_name: Caffeine

enzyme: UniProt H9N289

substrate: Caffeine


column_label: Table 1 carries a substrate-block column, a PAMO construct column and three kinetic columns headed K_M [mM], k_cat [s^-1] and k_cat/K_M [M^-1 s^-1]. The cited cell set is the Phenylacetone block, PAMO row WT: K_M [mM] = 0.06; k_cat [s^-1] = 2.4; the efficiency cell = 40, read on the per second per mM scale that the Phenylacetone block's own printed cells follow.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.4 in the Phenylacetone block of PAMO row WT under the column head k_cat [s^-1]; the column is already per second, so no unit conversion applies and the paper value is 2.4 s^(-1). Km: printed Table 1 cell 0.06 under the column head K_M [mM]; the column is already in mM, so no unit conversion applies and the paper value is 0.06 mM. kcat/Km: printed Table 1 cell 40. Printed Table 1 efficiency cell 40 for the Phenylacetone block, PAMO row WT. The printed head of that column is k_cat/K_M [M^-1 s^-1], and the printed efficiency cells of the Phenylacetone block sit on the per second per mM scale: this line prints k_cat 2.4 s^-1 and K_M 0.06 mM, and 2.4 / 0.06 = 40 per second per mM, while the second line of the same block prints k_cat 2.1 s^-1 and K_M 0.17 mM with the efficiency cell 12, and 2.1 / 0.17 = 12.35 per second per mM; the paper's prose gives the step between those two lines as 3.2-fold, which is 40 / 12.35. The cell is therefore read as 40 s^-1 mM^-1 and no unit conversion applies to it. The paper value is 40.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Phenylacetone block, PAMO row WT: K_M = 0.06 mM; k_cat = 2.4 s^-1; printed efficiency cell = 40.

table_label: Table 1: Steady-state kinetic parameters of PAMO WT and variants for the conversion of 2-octanone (Phys. Chem. Chem. Phys., 2018, 20, 2558-2570)


organism: Mycobacterium tuberculosis

substrate_name: benzylacetone

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

substrate: benzylacetone


substrate_name: Ethionamide

substrate: Ethionamide


smiles: CCCCCCCCCCC(C)=O

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADPH

column_label: Table II 2-Dodecanone row, Km column 200 uM and kcat column 0.023 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 2-Dodecanone row: Km 200 uM; kcat 0.023 s^-1; FMT 94%.

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


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


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


substrate_name: Phenylacetone

substrate: Phenylacetone


organism: Rattus norvegicus

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P29476 and applied mutation signature F1395A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

column_label: Table 1: Steady-state kinetic parameters for ferricyanide reduction by wild-type and mutant forms of the nNOS FAD domain (Eur. J. Biochem. 2004, 271:2548-2560); nNOS row 'F1395A', NADH column group: column 'Km (uM)' = 3250; column 'kcat (s-1)' = 259.8; column 'kcat/Km (uM-1 s-1)' = 0.0799.

normalized_value_unit_evidence: kcat: printed Table 1 NADH cell 259.8 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 259.8 s^(-1); the exported value is 259.8 s^(-1). Km: printed Table 1 NADH cell 3250 uM; 3250 / 1000 = 3.25 mM; the exported value is 3.25 mM. kcat/Km: printed Table 1 NADH cell 0.0799 uM-1 s-1; 1 uM-1 s-1 is 1000 s-1 mM-1, so 0.0799 x 1000 = 79.9 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 259.8 / 3.25 = 79.93846153846154 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, nNOS row 'F1395A', NADH column group: Km = 3250 uM; kcat = 259.8 s-1; printed kcat/Km = 0.0799 uM-1 s-1.

row_label: Table 1, nNOS row 'F1395A', the NADH column group of that row (Km, kcat and kcat/Km)

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P29476 and applied mutation signature F1395S to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic parameters for ferricyanide reduction by wild-type and mutant forms of the nNOS FAD domain (Eur. J. Biochem. 2004, 271:2548-2560); nNOS row 'F1395S', NADH column group: column 'Km (uM)' = 1830; column 'kcat (s-1)' = 114.8; column 'kcat/Km (uM-1 s-1)' = 0.0627.

normalized_value_unit_evidence: kcat: printed Table 1 NADH cell 114.8 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 114.8 s^(-1); the exported value is 114.8 s^(-1). Km: printed Table 1 NADH cell 1830 uM; 1830 / 1000 = 1.83 mM; the exported value is 1.83 mM. kcat/Km: printed Table 1 NADH cell 0.0627 uM-1 s-1; 1 uM-1 s-1 is 1000 s-1 mM-1, so 0.0627 x 1000 = 62.7 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 114.8 / 1.83 = 62.73224043715847 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, nNOS row 'F1395S', NADH column group: Km = 1830 uM; kcat = 114.8 s-1; printed kcat/Km = 0.0627 uM-1 s-1.

row_label: Table 1, nNOS row 'F1395S', the NADH column group of that row (Km, kcat and kcat/Km)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P29476 and applied mutation signature F1395W to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic parameters for ferricyanide reduction by wild-type and mutant forms of the nNOS FAD domain (Eur. J. Biochem. 2004, 271:2548-2560); nNOS row 'F1395W', NADH column group: column 'Km (uM)' = 3550; column 'kcat (s-1)' = 34.6; column 'kcat/Km (uM-1 s-1)' = 0.0097.

normalized_value_unit_evidence: kcat: printed Table 1 NADH cell 34.6 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 34.6 s^(-1); the exported value is 34.6 s^(-1). Km: printed Table 1 NADH cell 3550 uM; 3550 / 1000 = 3.55 mM; the exported value is 3.55 mM. kcat/Km: printed Table 1 NADH cell 0.0097 uM-1 s-1; 1 uM-1 s-1 is 1000 s-1 mM-1, so 0.0097 x 1000 = 9.7 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 34.6 / 3.55 = 9.746478873239438 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, nNOS row 'F1395W', NADH column group: Km = 3550 uM; kcat = 34.6 s-1; printed kcat/Km = 0.0097 uM-1 s-1.

row_label: Table 1, nNOS row 'F1395W', the NADH column group of that row (Km, kcat and kcat/Km)


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

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.

substrate: NADPH


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, 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


enzyme_display_name: 7-methylxanthine demethylase

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


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.

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


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

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


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


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


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


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

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


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


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

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

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


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)

assay_conditions_summary: cofactor NADPH

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

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.


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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

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


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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

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.


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

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

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

enzyme: UniProt E9QYP0

substrate: L-ornithine


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_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


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

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

assay_conditions_summary: cofactor NADPH

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_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.


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