enzyme_display_name: coenzyme F420 oxidoreductase (ferredoxin)

organism: Methanosarcina acetivorans

substrate_name: oxidized coenzyme F420

proof_lines: 21°C, pH not specified in the publication

substrate: oxidized coenzyme F420


enzyme_display_name: trimethylamine dehydrogenase

organism: Pseudomonas putida

substrate_name: trimethylamine

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

smiles: CN(C)C

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

enzyme: trimethylamine dehydrogenase

substrate: trimethylamine

status: unverified

source: brenda


enzyme_display_name: sarcosine dehydrogenase

organism: Sinorhizobium meliloti

substrate_name: sarcosine

smiles: CNCC(=O)O

enzyme: sarcosine dehydrogenase

substrate: sarcosine


proof_lines:
pH 7.5, 37°C, immobilized enzyme
pH 7.5, 37°C, non-immobilized enzyme


organism: Methylophilus methylotrophus

protein_accession_database: UniProt

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y442G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant Y442G, electron acceptor: electron transferring flavoprotein

data_origin: experimental


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y442L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant Y442L, electron acceptor: electron transferring flavoprotein


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y442F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant Y442F, electron acceptor: electron transferring flavoprotein


enzyme_display_name: Hydroxyproline dehydrogenase

organism: Homo sapiens

substrate_name: oxygen

source_db: uniprot

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

smiles: O=O

proof_lines: kcat with trans-4-L-hydroxyproline (Hyp) and ubiquinone-1 is 0.19 sec(-1). Proline is unable to saturate PRODH2 at least up to 750mM. kcat/KM with proline and ubiquinone-10: 0.075 M(-1)/sec. kcat with oxygen, duroquinone, menadione and CoQ1

enzyme: Hydroxyproline dehydrogenase

substrate: oxygen

source: uniprot


substrate_name: duroquinone

substrate: duroquinone


substrate_name: menadione

substrate: menadione


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Δ725 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: mutant delta725-729, electron acceptor: phenazine methosulfate

proof_lines: mutant DELTA725-729, electron acceptor: phenazine methosulfate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Δ720 to reconstruct the assayed variant sequence.

proof_lines: mutant delta720-729, electron acceptor: phenazine methosulfate

proof_lines: mutant DELTA720-729, electron acceptor: phenazine methosulfate


proof_lines: recombinant wild-type form, electron acceptor: phenazine methosulfate

proof_lines: native wild-type form, electron acceptor: phenazine methosulfate

proof_lines: wild-type form, electron acceptor: electron transferring flavoprotein


organism: Chromohalobacter israelensis (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)

substrate_name: NAD(+)

proof_lines: kcat is 0.312 sec(-1) with DMG as substrate. kcat is 0.280 sec(-1) with sarcosine as substrate. kcat is 0.202 sec(-1) with NAD(+) as substrate. kcat is 0.136 sec(-1) with NADP(+) as substrate.

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: Proline dehydrogenase

organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: proline (at 23 degrees Celsius and pH 7.5)

proof_lines: kcat 8.7 sec(-1) is for proline. kcat is 14 sec(-1) for coenzyme Q1.

enzyme: Proline dehydrogenase


substrate_name: coenzyme Q1 (at 23 degrees Celsius and pH 7.5)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V344I with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant V344I, electron acceptor: electron transferring flavoprotein


enzyme_display_name: UniProt Q72IB8

organism: Thermus thermophilus

substrate_name: L-proline

source_db: skid

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

sequence_source: multiple

proof_lines: kcat is 13 sec(-1) for L-proline. kcat is 75 sec(-1) for 3,4-dehydro-L-proline.

source_databases_merged: skid uniprot

enzyme: UniProt Q72IB8

substrate: L-proline

source: skid


substrate_name: L-proline (at 25 degrees Celsius)

substrate: L-proline (at 25 degrees Celsius)


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: 3,4-dehydro-L-proline (at 25 degrees Celsius)


organism: Chromohalobacter israelensis

assay_conditions_summary: pH 7.5; cofactor NADP+

source_databases_merged: brenda uniprot


proof_lines: electron acceptor: electron transferring flavoprotein

proof_lines: recombinant enzyme, electron acceptor: ferricenium hexafluorophosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C30A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant C30A, electron acceptor: ferricenium hexafluorophosphate

proof_lines: electron acceptor: ferricenium hexafluorophosphate, mutant C30A


substrate_name: N,N-dimethylglycine

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

proof_lines: kcat is 213 min(-1) for N,N-dimethylglycine.

substrate: N,N-dimethylglycine


organism: Methanopyrus kandleri

substrate_name: methylenetetrahydromethanopterin

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

assay_conditions_summary: pH 6

proof_lines: native enzyme, pH 6.0, 65°C, N2-atmosphere

substrate: methylenetetrahydromethanopterin


organism: Rattus norvegicus

substrate_name: N,N-dimethylglycine for precursor enzyme


proof_lines: enzyme from Methanopyrus kandleri, pH and temperature not specified in the publication

proof_lines: recombinant enzyme expressed in Escherichia coli, pH and temperature not specified in the publication


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

proof_lines: KM for coenzyme F420-(gamma-Glu)(n) is greater than 100 uM.


substrate_name: coenzyme F420

substrate: coenzyme F420


organism: Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

substrate_name: reduced coenzyme F420

substrate: reduced coenzyme F420


enzyme_display_name: Phloroglucinol reductase

organism: Eubacterium oxidoreducens

substrate_name: 1,3,5-trihydroxybenzene at pH 6.8

assay_conditions_summary: pH 6.8; cofactor NADPH

proof_lines: The KM and Vmax for 1,3,5-trihydroxybenzene (phloroglucinol) are pH dependent, indicating the substrate or enzyme are ionized (PubMed:2925649).

enzyme: Phloroglucinol reductase

substrate: 1,3,5-trihydroxybenzene at pH 6.8


enzyme_display_name: proline dehydrogenase

organism: Deinococcus radiodurans

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G63A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)

enzyme: proline dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E64A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)


substrate_name: coenzyme Q1

proof_lines: wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)

substrate: coenzyme Q1


proof_lines: kcat with trans-4-L-hydroxyproline (Hyp) and ubiquinone-1 is 0.19 sec(-1). Proline is unable to saturate PRODH2 at least up to 750mM. kcat/KM with proline and ubiquinone-10: 0.075 M(-1)/sec. kcat with oxygen, duroquinone, menadione and CoQ1


substrate_name: Unknown

substrate: Unknown


organism: Methanosarcina mazei

substrate_name: reduced ferredoxin

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: coenzyme F420 oxidoreductase (ferredoxin)

substrate: reduced ferredoxin


substrate_name: DMG

proof_lines: kcat is 0.312 sec(-1) with DMG as substrate. kcat is 0.280 sec(-1) with sarcosine as substrate. kcat is 0.202 sec(-1) with NAD(+) as substrate. kcat is 0.136 sec(-1) with NADP(+) as substrate.

substrate: DMG


organism: Macaca mulatta

ki_unit: mM


substrate_name: oxidized coenzyme F420

substrate: oxidized coenzyme F420


substrate_name: 5,10-Methylenetetrahydromethanopterin; Reduced coenzyme F420

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


enzyme_display_name: F(420)H(2) dehydrogenase subunit F

organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)

substrate_name: F(420)H(2) (at 37 degrees Celsius and pH 7)

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

enzyme: F(420)H(2) dehydrogenase subunit F


enzyme_display_name: Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial


substrate_name: alphaR237K mutant electron transferring flavoprotein


organism: uncultured archaeon


enzyme_display_name: F(420)H(2) dehydrogenase subunit B

enzyme: F(420)H(2) dehydrogenase subunit B

substrate: F(420)H(2) (at 37 degrees Celsius and pH 7)


enzyme_display_name: F(420)H(2) dehydrogenase subunit D

enzyme: F(420)H(2) dehydrogenase subunit D


enzyme_display_name: F(420)H(2) dehydrogenase subunit H

enzyme: F(420)H(2) dehydrogenase subunit H


enzyme_display_name: F(420)H(2) dehydrogenase subunit A

enzyme: F(420)H(2) dehydrogenase subunit A


enzyme_display_name: F(420)H(2) dehydrogenase subunit O

enzyme: F(420)H(2) dehydrogenase subunit O


enzyme_display_name: F(420)H(2) dehydrogenase subunit M

enzyme: F(420)H(2) dehydrogenase subunit M


enzyme_display_name: F(420)H(2) dehydrogenase subunit N

enzyme: F(420)H(2) dehydrogenase subunit N


enzyme_display_name: F(420)H(2) dehydrogenase subunit I

enzyme: F(420)H(2) dehydrogenase subunit I


enzyme_display_name: F(420)H(2) dehydrogenase subunit J

enzyme: F(420)H(2) dehydrogenase subunit J


enzyme_display_name: F(420)H(2) dehydrogenase subunit C

enzyme: F(420)H(2) dehydrogenase subunit C


enzyme_display_name: F(420)H(2) dehydrogenase subunit K

enzyme: F(420)H(2) dehydrogenase subunit K


enzyme_display_name: F(420)H(2) dehydrogenase subunit L

enzyme: F(420)H(2) dehydrogenase subunit L


substrate_name: ubiquinone-1 (in the presence of 6 mM CHAPS)

verification_status: verified

assay_conditions_summary: cofactor CoA

column_label: Table 2; section Ubiquinone reduction; row Q1 / ubiquinone-1; column Km (uM); cell 8.1 +/- 1.0 uM.

normalized_value_unit_evidence: Km=0.0081 mM for Q1 / ubiquinone-1 after uM -> mM conversion.

raw_value_unit_evidence: Table 2 row Q1 / ubiquinone-1; Km (uM) cell = 8.1 +/- 1.0 uM.

row_label: Q1 / ubiquinone-1

table_label: Table 2: Kinetic constants of human ETF-QO assayed by ubiquinone reduction and by disproportionation of ETF semiquinones

enzyme: Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

status: verified


substrate_name: ubiquinone-2 (in the presence of 6 mM CHAPS)

column_label: Table 2; section Ubiquinone reduction; row Q2 / ubiquinone-2; column Km (uM); cell 4.9 +/- 0.7 uM.

normalized_value_unit_evidence: Km=0.0049 mM for Q2 / ubiquinone-2 after uM -> mM conversion.

raw_value_unit_evidence: Table 2 row Q2 / ubiquinone-2; Km (uM) cell = 4.9 +/- 0.7 uM.

row_label: Q2 / ubiquinone-2


substrate_name: ubiquinone-4 (in the presence of 11 mM CHAPS)

column_label: Table 2; section Ubiquinone reduction; row Q4 / ubiquinone-4; column Km (uM); cell 14.8 +/- 1.4 uM.

normalized_value_unit_evidence: Km=0.0148 mM for Q4 / ubiquinone-4 after uM -> mM conversion.

raw_value_unit_evidence: Table 2 row Q4 / ubiquinone-4; Km (uM) cell = 14.8 +/- 1.4 uM.

row_label: Q4 / ubiquinone-4


column_label: Table 2; section Ubiquinone reduction; row DQ / decylubiquinone / 6-decylubiquinone; column Km (uM); cell 8.4 +/- 0.8 uM.

normalized_value_unit_evidence: Km=0.0084 mM for DQ / 6-decylubiquinone after uM -> mM conversion.

raw_value_unit_evidence: Table 2 row DQ / decylubiquinone / 6-decylubiquinone; Km (uM) cell = 8.4 +/- 0.8 uM.


enzyme_display_name: dimethylglycine dehydrogenase

substrate_name: Ferrocene

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H109R with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

enzyme: dimethylglycine dehydrogenase

substrate: Ferrocene

source: oed


verification_status: corrected

column_label: Table 1 (Summary of kinetic parameters obtained with steady-state kinetics), column heads KM (mM), vmax (uM min^-1), kcat (min^-1), Aspec (umol mg^-1 min^-1) and kcat/KM (mM^-1 min^-1). The cited cell block is the assay row 'WT ferrocene': KM = 1.4, vmax = 22.1, kcat = 213, Aspec = 2.0, kcat/KM = 137.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.4 under the column head KM (mM); the printed unit is already mM, so no unit conversion applies and the normalized value is 1.4 mM. kcat: printed Table 1 cell 213 under the column head kcat (min^-1); 1 min^-1 is 1/60 s^-1, so 213 / 60 = 3.55 s^-1. kcat/Km: printed Table 1 cell 137 under the column head kcat/KM (mM^-1 min^-1); 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 137 / 60 = 2.283333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, assay row 'WT ferrocene': printed KM cell 1.4 under the column head KM (mM); printed vmax cell 22.1 under the column head vmax (uM min^-1); printed kcat cell 213 under the column head kcat (min^-1); printed Aspec cell 2.0 under the column head Aspec (umol mg^-1 min^-1); printed kcat/KM cell 137 under the column head kcat/KM (mM^-1 min^-1).

row_label: Table 1, assay row 'WT ferrocene'

table_label: Table 1: Summary of kinetic parameters obtained with steady-state kinetics with two activity assays, DCPIP and ferrocene (The FEBS Journal 2016, 283:3587-3603); printed column heads KM (mM) | vmax (uM min^-1) | kcat (min^-1) | Aspec (umol mg^-1 min^-1) | kcat/KM (mM^-1 min^-1)

status: corrected


substrate_name: N,N-dimethylglycine


substrate_name: oxidized 2,6-dichlorophenolindophenol

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UI17 and applied mutation signature H109R to reconstruct the assayed variant sequence.

column_label: Table 1 (Summary of kinetic parameters obtained with steady-state kinetics), column heads KM (mM), vmax (uM min^-1), kcat (min^-1), Aspec (umol mg^-1 min^-1) and kcat/KM (mM^-1 min^-1). The cited cell block is the assay row 'H109R DCPIP': KM = 4.7, vmax = 7.4, kcat = 91, Aspec = 1, kcat/KM = 20.

normalized_value_unit_evidence: Km: printed Table 1 cell 4.7 under the column head KM (mM); the printed unit is already mM, so no unit conversion applies and the normalized value is 4.7 mM. kcat: printed Table 1 cell 91 under the column head kcat (min^-1); 1 min^-1 is 1/60 s^-1, so 91 / 60 = 1.5166666666666666 s^-1, carried here at the three significant figures the catalog row uses, 1.52 s^(-1). kcat/Km: printed Table 1 cell 20 under the column head kcat/KM (mM^-1 min^-1); 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 20 / 60 = 0.3333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, assay row 'H109R DCPIP': printed KM cell 4.7 under the column head KM (mM); printed vmax cell 7.4 under the column head vmax (uM min^-1); printed kcat cell 91 under the column head kcat (min^-1); printed Aspec cell 1 under the column head Aspec (umol mg^-1 min^-1); printed kcat/KM cell 20 under the column head kcat/KM (mM^-1 min^-1).

row_label: Table 1, assay row 'H109R DCPIP'

substrate: oxidized 2,6-dichlorophenolindophenol


column_label: Table 1 (Summary of kinetic parameters obtained with steady-state kinetics), column heads KM (mM), vmax (uM min^-1), kcat (min^-1), Aspec (umol mg^-1 min^-1) and kcat/KM (mM^-1 min^-1). The cited cell block is the assay row 'WT DCPIP': KM = 0.3, vmax = 4.7, kcat = 44, Aspec = 0.5, kcat/KM = 146.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.3 under the column head KM (mM); the printed unit is already mM, so no unit conversion applies and the normalized value is 0.3 mM. kcat: printed Table 1 cell 44 under the column head kcat (min^-1); 1 min^-1 is 1/60 s^-1, so 44 / 60 = 0.7333333333333333 s^-1, carried here at the two decimal places the catalog row uses, 0.73 s^(-1). kcat/Km: printed Table 1 cell 146 under the column head kcat/KM (mM^-1 min^-1); 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 146 / 60 = 2.433333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, assay row 'WT DCPIP': printed KM cell 0.3 under the column head KM (mM); printed vmax cell 4.7 under the column head vmax (uM min^-1); printed kcat cell 44 under the column head kcat (min^-1); printed Aspec cell 0.5 under the column head Aspec (umol mg^-1 min^-1); printed kcat/KM cell 146 under the column head kcat/KM (mM^-1 min^-1).

row_label: Table 1, assay row 'WT DCPIP'


enzyme_display_name: hydroxyproline dehydrogenase

enzyme: hydroxyproline dehydrogenase


substrate_name: duroquinone

substrate: duroquinone


substrate_name: menaquinone

proof_lines: PRODH2 menadione duroquinone

substrate: menaquinone


enzyme_display_name: phloroglucinol reductase

substrate_name: NADPH

enzyme: phloroglucinol reductase

substrate: NADPH


substrate_name: phloroglucinol

assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines:
at pH 7.6
at pH 7.2
at pH 6.8

substrate: phloroglucinol


enzyme_display_name: pyrimidodiazepine synthase

organism: Drosophila melanogaster

substrate_name: dihydroneopterin triphosphate

enzyme: pyrimidodiazepine synthase

substrate: dihydroneopterin triphosphate


substrate_name: glutathione

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

substrate: glutathione


enzyme_display_name: proline dehydrogenase

substrate_name: L-proline

enzyme: proline dehydrogenase

substrate: L-proline


proof_lines:
Chromohalobacter salexigens DSM 3043
N,N-dimethylglycine
sarcosine

substrate: N,N-dimethylglycine


proof_lines: coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase


organism: Methanolobus tindarius

substrate_name: reduced coenzyme F420

column_label: PMID 1735436 Table 3, catalytic property rows: Turnover number kcat = 25.5 s^-1 and App. Km for F420H2 = 5.4 uM.

raw_value_unit_evidence: Turnover number kcat 25.5 s^-1; App. Km for F420H2 5.4 uM.

table_label: Table 3: Properties of F420H2-dehydrogenase from Methanolobus tindarius

substrate: reduced coenzyme F420


enzyme_display_name: D-arabinono-1,4-lactone oxidase

organism: Candida albicans

proof_lines:
D-arabinose dehydrogenase
erythroascorbic acid biosynthesis

enzyme: D-arabinono-1,4-lactone oxidase


organism: Escherichia coli

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


substrate_name: Unknown


organism: Homo sapiens

substrate_name: menadione

substrate: menadione


substrate_name: pentadecylubiquinone

proof_lines: disproportionation of semiquinone electron-transferring flavoprotein

substrate: pentadecylubiquinone


substrate_name: decylubiquinone

substrate: decylubiquinone


proof_lines: pH 8.0, 25°C, Y540F mutant of PutA86-601


proof_lines: pH 8.0, 25°C, Y540F/D370A mutant of PutA86-601


proof_lines: pH 8.0, 25°C, D370A mutant of PutA86-601


proof_lines: truncated mutant W194F/W211F, pH 7.5, 25°C


organism: Methanosarcina barkeri


substrate_name: coenzyme F420

substrate: coenzyme F420


organism: Mycobacterium tuberculosis

proof_lines: wild type enzyme, at 25°C and pH 7.1 in 20 mM Tris-HCl


proof_lines: mutant enzyme Y203F, at 25°C and pH 7.1 in 20 mM Tris-HCl


organism: Archaeoglobus fulgidus

substrate_name: oxidized coenzyme F420

substrate: oxidized coenzyme F420


substrate_name: methylenetetrahydromethanopterin

substrate: methylenetetrahydromethanopterin


proof_lines:
25°C, wild-type PutA86-669
pH 8.0, 25°C, wild-type PutA86-601
truncated wild-type, pH 7.5, 25°C


substrate_name: phenazine

substrate: phenazine


proof_lines: in 50 mM potassium phosphate (pH 7.4, 50 mM NaCl), temperature not specified in the publication


organism: Sus scrofa


substrate_name: electron-transferring flavoprotein

proof_lines: comproportionation of electron-transferring flavoprotein and hydroquinone electron-transferring flavoprotein

substrate: electron-transferring flavoprotein


organism: Thermus thermophilus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor FAD

proof_lines: recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol

proof_lines: recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol

proof_lines: recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol


organism: Trypanosoma cruzi

proof_lines: recombinant enzyme, pH 7.5, 37°C, with 2,6-dichlorphenol-indophenol


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 294.15 K; cofactor NAD+

proof_lines: overall reaction of bifunctional enzyme, pH 7.5, 21°C

substrate: NAD+


organism: Saccharomyces cerevisiae

substrate_name: D-arabinose

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

substrate: D-arabinose


enzyme_display_name: nicotine 6-hydroxylase

organism: Agrobacterium tumefaciens

substrate_name: (S)-nicotine

proof_lines: cosubstrate 2,6-dichlorophenolindophenol, pH 7, 30°C

enzyme: nicotine 6-hydroxylase

substrate: (S)-nicotine


substrate_name: pseudoazurin

substrate: pseudoazurin


enzyme_display_name: UniProt Q9T0N8

organism: Zea mays

substrate_name: caffeic acid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q9T0N8

substrate: caffeic acid


substrate_name: o-coumaric acid

substrate: o-coumaric acid


substrate_name: rosmarinic acid

substrate: rosmarinic acid


substrate_name: daphnoretin

substrate: daphnoretin


substrate_name: vitamin K1

substrate: vitamin K1


substrate_name: scopoletin

substrate: scopoletin


substrate_name: zeatin riboside

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7

substrate: zeatin riboside


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=6.5
Raw SKiD Env: Temp=37°C, pH=-----


substrate_name: zeatin

substrate: zeatin


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=6.5


substrate_name: vitamin K3

substrate: vitamin K3


substrate_name: coenzyme Q1

substrate: coenzyme Q1


enzyme_display_name: NAD(P)+ transhydrogenase (Si-specific)

organism: Nocardia jiangxiensis

substrate_name: NADH

enzyme: NAD(P)+ transhydrogenase (Si-specific)

substrate: NADH


substrate_name: NADPH

substrate: NADPH


organism: Pseudarthrobacter oxydans

substrate_name: brilliant cresyl blue

substrate: brilliant cresyl blue


substrate_name: methylene blue

substrate: methylene blue


substrate_name: Nicotine

substrate: Nicotine


substrate_name: menadione

substrate: menadione


substrate_name: vitamin K5

substrate: vitamin K5


enzyme_display_name: methylglutamate dehydrogenase

organism: Aminobacter aminovorans

enzyme: methylglutamate dehydrogenase


substrate_name: N-methyl DL-aspartate

substrate: N-methyl DL-aspartate


substrate_name: N-methyl L-alanine

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

substrate: N-methyl L-alanine


substrate_name: N-methyl D-alanine

substrate: N-methyl D-alanine


substrate_name: sarcosine

substrate: sarcosine


organism: bacterium AT2


substrate_name: N-Methyl-L-glutamate

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

substrate: N-Methyl-L-glutamate


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: horse heart cytochrome c

substrate: horse heart cytochrome c


organism: Oryctolagus cuniculus

substrate_name: (S)-nicotine

proof_lines: respiratory olfactory

substrate: (S)-nicotine


enzyme_display_name: spermidine dehydrogenase

organism: Citrobacter freundii

substrate_name: spermine

smiles: C(CCNCCCN)CNCCCN

enzyme: spermidine dehydrogenase

substrate: spermine


substrate_name: spermidine

smiles: C(CCNCCCN)CN

proof_lines:
enzyme II
enzyme I

substrate: spermidine


organism: Pseudomonas aeruginosa


organism: Glycine max


organism: Serratia marcescens

proof_lines: does not inhibit the enzyme when spermidine is used as substrate


enzyme_display_name: L-pipecolate dehydrogenase

organism: Pseudomonas putida

substrate_name: L-pipecolate

proof_lines:
pipecolate oxidase
Pseudomonas putida
pipecolate

enzyme: L-pipecolate dehydrogenase

substrate: L-pipecolate


enzyme_display_name: Cytochrome b5 reductase 4

organism: Homo sapiens

enzyme: Cytochrome b5 reductase 4


enzyme_display_name: UniProt P00388

organism: Rattus norvegicus

substrate_name: NADPH

enzyme: UniProt P00388

substrate: NADPH


enzyme_display_name: cytochrome-b5 reductase

organism: Phascolopsis gouldii

substrate_name: cytochrome b5

enzyme: cytochrome-b5 reductase

substrate: cytochrome b5


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: ferricyanide

substrate: ferricyanide


enzyme_display_name: NAD(P)+ transhydrogenase (ferredoxin)

organism: Clostridium kluyveri

assay_conditions_summary: pH 7; 310.15 K; cofactor NADP+

enzyme: NAD(P)+ transhydrogenase (ferredoxin)


substrate_name: NAD+

substrate: NAD+


organism: Saccharomyces cerevisiae

substrate_name: Ferricytochrome b5; H+; NADH

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

substrate: Ferricytochrome b5; H+; NADH


substrate_name: Ferricytochrome b5; NADH; H+

substrate: Ferricytochrome b5; NADH; H+


enzyme_display_name: NADPH--hemoprotein reductase

organism: Andrographis paniculata

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

enzyme: NADPH--hemoprotein reductase


substrate_name: ferricytochrome c

substrate: ferricytochrome c


organism: Gossypium hirsutum


organism: Propsilocerus akamusi

substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


enzyme_display_name: NADPH-hemoprotein reductase

enzyme: NADPH-hemoprotein reductase


organism: Alburnus tarichi

assay_conditions_summary: pH 8; 323.15 K; cofactor NADPH


organism: Nitrobacter winogradskyi

assay_conditions_summary: cofactor NADPH


proof_lines: electron donor NADH, electron acceptor dichlorophenolindophenol


organism: Spodoptera eridania

substrate_name: cytochrome c

substrate: cytochrome c


organism: Chelon saliens

substrate_name: Unknown

assay_conditions_summary: pH 7.7; 297.15 K; cofactor NADPH

substrate: Unknown


organism: Coleus scutellarioides

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADPH

proof_lines: recombinant yeast microsomal CPR, pH 7.5, 35°C

proof_lines: recombinant yeast internal CPR, pH 7.5, 35°C


organism: Starmerella apicola


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase 1

organism: Bacillus subtilis (strain 168)

substrate_name: stearic acid

smiles: CCCCCCCCCCCCCCCCCC(=O)O

proof_lines: kcat is 430 min(-1) for stearic acid hydroxylation. kcat is 5430 min(-1) for phytanic acid hydroxylation. kcat is 6105 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 11400 min(-1) for the reduction of cytochrome c. kcat is 38150

substrate: stearic acid


substrate_name: phytanic acid

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

enzyme: Bifunctional cytochrome P450/NADPH--P450 reductase 1

substrate: phytanic acid


substrate_name: 15-methylpalmitic acid

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

substrate: 15-methylpalmitic acid


substrate_name: ferricyanide (in the reductase assay)

substrate: ferricyanide (in the reductase assay)


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase 2

substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

proof_lines: kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytan

substrate: lauric acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

enzyme: Bifunctional cytochrome P450/NADPH--P450 reductase 2

substrate: myristic acid


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitic acid


substrate_name: arachidonic acid

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

substrate: arachidonic acid


substrate_name: NADPH

substrate: NADPH


substrate_name: NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179V with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer triplicate in 116 mM MOPS; cofactor NADPH

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179V'; column 'kcat (s^-1), NADPH:FR activity group' = 8; column 'Km NADPH (uM), NADPH:FR activity group' = 375; column 'kcat/Km NADPH (s^-1 M^-1), NADPH:FR activity group' = 2.2 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 8.0 s^(-1). Km: printed Table 2 cell 375 uM; 375 / 1000 = 0.375 mM. kcat/Km: printed Table 2 cell 2.2 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.2 x 10^4 / 1000 = 22.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, protein row G179V, NADPH:FR activity columns: kcat = 8 s^-1; Km = 375 uM; printed kcat/Km = 2.2 x 10^4 s^-1 M^-1.


substrate_name: ferricyanide

assay_conditions_summary: pH 7; 298.15 K; buffer triplicate in 116 mM MOPS; cofactor NADH

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179V'; column 'kcat (s^-1), NADH:FR activity group' = 12; column 'Km Fe(CN)6 (uM), NADH:FR activity group' = 7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 12.0 s^(-1). Km: printed Table 2 cell 7 uM; 7 / 1000 = 0.007 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement, so the canonical value is the full-precision quotient of the two printed cells, 12.0 / 0.007 = 1714.2857142857142 s^(-1)*mM^(-1), typed derived_same_measurement.

raw_value_unit_evidence: Table 2, protein row G179V, NADH:FR activity columns with ferricyanide as the varied substrate: kcat = 12 s^-1; Km = 7 uM.

substrate: ferricyanide


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179T with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179T'; column 'kcat (s^-1), NADPH:FR activity group' = 12; column 'Km NADPH (uM), NADPH:FR activity group' = 507; column 'kcat/Km NADPH (s^-1 M^-1), NADPH:FR activity group' = 2.6 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 12.0 s^(-1). Km: printed Table 2 cell 507 uM; 507 / 1000 = 0.507 mM. kcat/Km: printed Table 2 cell 2.6 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.6 x 10^4 / 1000 = 26.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, protein row G179T, NADPH:FR activity columns: kcat = 12 s^-1; Km = 507 uM; printed kcat/Km = 2.6 x 10^4 s^-1 M^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179P with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179P'; column 'kcat (s^-1), NADPH:FR activity group' = 17; column 'Km NADPH (uM), NADPH:FR activity group' = 2317; column 'kcat/Km NADPH (s^-1 M^-1), NADPH:FR activity group' = 8.4 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 17 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 17.0 s^(-1). Km: printed Table 2 cell 2317 uM; 2317 / 1000 = 2.317 mM. kcat/Km: printed Table 2 cell 8.4 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.4 x 10^3 / 1000 = 8.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, protein row G179P, NADPH:FR activity columns: kcat = 17 s^-1; Km = 2317 uM; printed kcat/Km = 8.4 x 10^3 s^-1 M^-1.


column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179T'; column 'kcat (s^-1), NADH:FR activity group' = 33; column 'Km Fe(CN)6 (uM), NADH:FR activity group' = 8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 33 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 33.0 s^(-1). Km: printed Table 2 cell 8 uM; 8 / 1000 = 0.008 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement, so the canonical value is the full-precision quotient of the two printed cells, 33.0 / 0.008 = 4125.0 s^(-1)*mM^(-1), typed derived_same_measurement.

raw_value_unit_evidence: Table 2, protein row G179T, NADH:FR activity columns with ferricyanide as the varied substrate: kcat = 33 s^-1; Km = 8 uM.


column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179P'; column 'kcat (s^-1), NADH:FR activity group' = 42; column 'Km Fe(CN)6 (uM), NADH:FR activity group' = 7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 42 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 42.0 s^(-1). Km: printed Table 2 cell 7 uM; 7 / 1000 = 0.007 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement, so the canonical value is the full-precision quotient of the two printed cells, 42.0 / 0.007 = 6000.0 s^(-1)*mM^(-1), typed derived_same_measurement.

raw_value_unit_evidence: Table 2, protein row G179P, NADH:FR activity columns with ferricyanide as the varied substrate: kcat = 42 s^-1; Km = 7 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179A with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179A'; column 'kcat (s^-1), NADPH:FR activity group' = 48; column 'Km NADPH (uM), NADPH:FR activity group' = 1360; column 'kcat/Km NADPH (s^-1 M^-1), NADPH:FR activity group' = 3.9 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 48 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 48.0 s^(-1). Km: printed Table 2 cell 1360 uM; 1360 / 1000 = 1.36 mM. kcat/Km: printed Table 2 cell 3.9 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.9 x 10^4 / 1000 = 39.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, protein row G179A, NADPH:FR activity columns: kcat = 48 s^-1; Km = 1360 uM; printed kcat/Km = 3.9 x 10^4 s^-1 M^-1.


column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179A'; column 'kcat (s^-1), NADH:FR activity group' = 559; column 'Km Fe(CN)6 (uM), NADH:FR activity group' = 8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 559 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 559.0 s^(-1). Km: printed Table 2 cell 8 uM; 8 / 1000 = 0.008 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement, so the canonical value is the full-precision quotient of the two printed cells, 559.0 / 0.008 = 69875.0 s^(-1)*mM^(-1), typed derived_same_measurement.

raw_value_unit_evidence: Table 2, protein row G179A, NADH:FR activity columns with ferricyanide as the varied substrate: kcat = 559 s^-1; Km = 8 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G179A with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G179P with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G179T with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G179V with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


enzyme_display_name: NADH oxidase

organism: Lactococcus lactis subsp. cremoris (strain MG1363)

substrate_name: beta-NADH (in the presence of oxygen)

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

enzyme: NADH oxidase

substrate: beta-NADH (in the presence of oxygen)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D239E with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D239S with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D239T with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.


organism: Sus scrofa

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P83686 and applied mutation signature R63A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

column_label: Table III (Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+), printed enzyme-form row 'R63A', NADH metric group; column 'Km^NADH (uM)' = 104; column 'kcat^NADH (s-1)' = 403; column 'kcat^NADH/Km^NADH (uM-1 s-1)' = 3.9. The value printed after the plus/minus sign beside each of those cells is the printed uncertainty and is not an exported metric (18, 27 and 0.9 respectively). The same printed line also carries the Pb5 metric group ('Km^Pb5 (uM)' = 42.1, 'kcat^Pb5 (s-1)' = 121, 'kcat^Pb5/Km^Pb5 (uM-1 s-1)' = 2.9) and a dissociation-constant column for NAD+.

normalized_value_unit_evidence: Km: printed Table III cell 104 in a column headed Km^NADH (uM); 104 / 1000 = 0.104 mM. kcat: printed Table III cell 403 in a column headed kcat^NADH (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 403.0 s^(-1). kcat/Km: printed Table III cell 3.9 in a column headed kcat^NADH/Km^NADH (uM-1 s-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 3.9 x 1000 = 3900.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, printed enzyme-form row 'R63A', NADH metric group: Km^NADH = 104 uM; kcat^NADH = 403 s-1; printed kcat^NADH/Km^NADH = 3.9 uM-1 s-1.

table_label: Table III: Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+ (J. Biochem. 2001, 130(4):481-490). Printed column heads: Enzyme; under the group head NADH: Km^NADH (uM), kcat^NADH (s-1), kcat^NADH/Km^NADH (uM-1 s-1); under the group head Pb5: Km^Pb5 (uM), kcat^Pb5 (s-1), kcat^Pb5/Km^Pb5 (uM-1 s-1); then Kd^NAD+ (uM).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P83686 and applied mutation signature R63Q to reconstruct the assayed variant sequence.

column_label: Table III (Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+), printed enzyme-form row 'R63Q', NADH metric group; column 'Km^NADH (uM)' = 21; column 'kcat^NADH (s-1)' = 412; column 'kcat^NADH/Km^NADH (uM-1 s-1)' = 19.6. The value printed after the plus/minus sign beside each of those cells is the printed uncertainty and is not an exported metric (1, 5 and 1.2 respectively). The same printed line also carries the Pb5 metric group ('Km^Pb5 (uM)' = 18.5, 'kcat^Pb5 (s-1)' = 105, 'kcat^Pb5/Km^Pb5 (uM-1 s-1)' = 5.7) and a dissociation-constant column for NAD+.

normalized_value_unit_evidence: Km: printed Table III cell 21 in a column headed Km^NADH (uM); 21 / 1000 = 0.021 mM. kcat: printed Table III cell 412 in a column headed kcat^NADH (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 412.0 s^(-1). kcat/Km: printed Table III cell 19.6 in a column headed kcat^NADH/Km^NADH (uM-1 s-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 19.6 x 1000 = 19600.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, printed enzyme-form row 'R63Q', NADH metric group: Km^NADH = 21 uM; kcat^NADH = 412 s-1; printed kcat^NADH/Km^NADH = 19.6 uM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P83686 and applied mutation signature R63K to reconstruct the assayed variant sequence.

column_label: Table III (Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+), printed enzyme-form row 'R63K', NADH metric group; column 'Km^NADH (uM)' = 2.1; column 'kcat^NADH (s-1)' = 515; column 'kcat^NADH/Km^NADH (uM-1 s-1)' = 245. The value printed after the plus/minus sign beside each of those cells is the printed uncertainty and is not an exported metric (0.3, 8 and 39 respectively). The same printed line also carries the Pb5 metric group ('Km^Pb5 (uM)' = 7.3, 'kcat^Pb5 (s-1)' = 347, 'kcat^Pb5/Km^Pb5 (uM-1 s-1)' = 47.5) and a dissociation-constant column for NAD+.

normalized_value_unit_evidence: Km: printed Table III cell 2.1 in a column headed Km^NADH (uM); 2.1 / 1000 = 0.0021000000000000003 mM. kcat: printed Table III cell 515 in a column headed kcat^NADH (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 515.0 s^(-1). kcat/Km: printed Table III cell 245 in a column headed kcat^NADH/Km^NADH (uM-1 s-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 245 x 1000 = 245000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, printed enzyme-form row 'R63K', NADH metric group: Km^NADH = 2.1 uM; kcat^NADH = 515 s-1; printed kcat^NADH/Km^NADH = 245 uM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P83686 and applied mutation signature K97R to reconstruct the assayed variant sequence.

column_label: Table III (Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+), printed enzyme-form row 'K97R', NADH metric group; column 'Km^NADH (uM)' = 2.9; column 'kcat^NADH (s-1)' = 909; column 'kcat^NADH/Km^NADH (uM-1 s-1)' = 313. The value printed after the plus/minus sign beside each of those cells is the printed uncertainty and is not an exported metric (0.2, 17 and 28 respectively). The same printed line also carries the Pb5 metric group ('Km^Pb5 (uM)' = 6.9, 'kcat^Pb5 (s-1)' = 415, 'kcat^Pb5/Km^Pb5 (uM-1 s-1)' = 60.1) and a dissociation-constant column for NAD+.

normalized_value_unit_evidence: Km: printed Table III cell 2.9 in a column headed Km^NADH (uM); 2.9 / 1000 = 0.0029 mM. kcat: printed Table III cell 909 in a column headed kcat^NADH (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 909.0 s^(-1). kcat/Km: printed Table III cell 313 in a column headed kcat^NADH/Km^NADH (uM-1 s-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 313 x 1000 = 313000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, printed enzyme-form row 'K97R', NADH metric group: Km^NADH = 2.9 uM; kcat^NADH = 909 s-1; printed kcat^NADH/Km^NADH = 313 uM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P83686 and applied mutation signature K97A to reconstruct the assayed variant sequence.

column_label: Table III (Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+), printed enzyme-form row 'K97A', NADH metric group; column 'Km^NADH (uM)' = 4.4; column 'kcat^NADH (s-1)' = 1060; column 'kcat^NADH/Km^NADH (uM-1 s-1)' = 240. The value printed after the plus/minus sign beside each of those cells is the printed uncertainty and is not an exported metric (0.3, 19 and 21 respectively). The same printed line also carries the Pb5 metric group ('Km^Pb5 (uM)' = 16.1, 'kcat^Pb5 (s-1)' = 191, 'kcat^Pb5/Km^Pb5 (uM-1 s-1)' = 11.9) and a dissociation-constant column for NAD+.

normalized_value_unit_evidence: Km: printed Table III cell 4.4 in a column headed Km^NADH (uM); 4.4 / 1000 = 0.0044 mM. kcat: printed Table III cell 1060 in a column headed kcat^NADH (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1060.0 s^(-1). kcat/Km: printed Table III cell 240 in a column headed kcat^NADH/Km^NADH (uM-1 s-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 240 x 1000 = 240000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, printed enzyme-form row 'K97A', NADH metric group: Km^NADH = 4.4 uM; kcat^NADH = 1060 s-1; printed kcat^NADH/Km^NADH = 240 uM-1 s-1.


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G291D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D239G with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature ΔF272 with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


enzyme_display_name: NADH-cytochrome b5 reductase 3

proof_lines: kcat is 570 sec(-1) with NADH as substrate (PubMed:10082957). kcat is 560 sec(-1) with 2 Fe(II)-[cytochrome b5] as substrate (PubMed:10082957). kcat is 1100 sec(-1) with NADH as substrate (PubMed:11574067, PubMed:12459552). kcat is 661 sec(

enzyme: NADH-cytochrome b5 reductase 3


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase

organism: Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)

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

proof_lines: kcat is 84.1 sec(-1) for lauric acid (PubMed:16403573). kcat is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N-palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine.


substrate_name: indole

enzyme: Bifunctional cytochrome P450/NADPH--P450 reductase

substrate: indole


organism: Anopheles minimus

proof_lines: mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L148P with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


organism: Capsicum annuum


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


enzyme_display_name: UniProt A1B9E3

organism: Paracoccus denitrificans

enzyme: UniProt A1B9E3


enzyme_display_name: UniProt P0A8G6

organism: Escherichia coli

enzyme: UniProt P0A8G6


enzyme_display_name: Monodehydroascorbate reductase

organism: Pisum sativum

enzyme: Monodehydroascorbate reductase


substrate_name: monodehydroascorbate

substrate: monodehydroascorbate


enzyme_display_name: Monodehydroascorbate reductase II

organism: Glycine max

sequence: AKTFKYIILG

wild_type_sequence: AKTFKYIILG

enzyme: Monodehydroascorbate reductase II


enzyme_display_name: Monodehydroascorbate reductase, fruit isozyme

organism: Cucumis sativus


enzyme: Monodehydroascorbate reductase, fruit isozyme


enzyme_display_name: NADPH--cytochrome P450 reductase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.

enzyme: NADPH--cytochrome P450 reductase


enzyme_display_name: NADPH:quinone reductase

enzyme: NADPH:quinone reductase


enzyme_display_name: p-benzoquinone reductase (NADPH)

organism: Mucor ambiguus

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

enzyme: p-benzoquinone reductase (NADPH)


substrate_name: isatin

substrate: isatin


substrate_name: beta-naphthoquinone

substrate: beta-naphthoquinone


substrate_name: acenaphthenequinone

substrate: acenaphthenequinone


substrate_name: p-toluquinone

substrate: p-toluquinone


substrate_name: ketopantoyl lactone

substrate: ketopantoyl lactone


substrate_name: alloxan

substrate: alloxan


organism: Arabidopsis thaliana

substrate_name: Ferricytochrome

substrate: Ferricytochrome


substrate_name: decyl-plastoquinone

substrate: decyl-plastoquinone


assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: pH 7.5, cosubstrate: 9,10-phenanthrenequinone


organism: Synechocystis sp.

substrate_name: coenzyme Q10

assay_conditions_summary: pH 7.5; 283.15 K; cofactor NADPH

substrate: coenzyme Q10


substrate_name: duroquinone

substrate: duroquinone


substrate_name: menadione

substrate: menadione


substrate_name: dibromothymoquinone

substrate: dibromothymoquinone


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

organism: Phanerodontia chrysosporium

assay_conditions_summary: pH 6

proof_lines: pH 6.0, temperature not specified in the publication

enzyme: NAD(P)H dehydrogenase (quinone)


assay_conditions_summary: pH 6; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: pH 6; cofactor NADH

substrate: NADH


organism: Clostridium tyrobutyricum

substrate_name: FMN

assay_conditions_summary: cofactor FMN

substrate: FMN


assay_conditions_summary: cofactor NADH


organism: Camelus dromedarius


substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


organism: Giardia duodenalis

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

column_label: Table 1: Kinetic parameters of glQR for the electron acceptors; Table 1, Menadione rows under NADPH and NADH donors; NADPH/Menadione: Kapp_m 0.240 uM, kcat 34.83 s^-1, kcat/Km 145.12 uM^-1 s^-1. NADH/Menadione: Kapp_m 0.188 uM, kcat 23.07 s^-1, kcat/Km 121.39 uM^-1 s^-1.

normalized_value_unit_evidence: Paper Km values converted uM to mM where needed; paper kcat/Km values converted uM^-1 s^-1 to s^-1 mM^-1 by multiplying by 1000.


substrate_name: naphthoquinone

column_label: Table 1: Kinetic parameters of glQR for the electron acceptors; Table 1, Naphthoquinone rows under NADPH and NADH donors; NADPH/Naphthoquinone: Kapp_m 0.59 uM, kcat 39.29 s^-1, kcat/Km 66.59 uM^-1 s^-1. NADH/Naphthoquinone: Kapp_m 0.437 uM, kcat 29.93 s^-1, kcat/Km 68.03 uM^-1 s^-1.

substrate: naphthoquinone


column_label: Table 2: Kinetic parameters of glQR for the electron donors; Table 2, Naphthoquinone / NADH electron donor row; Kapp_m 44.91 +/- 2.73 uM; kcat 62.66 +/- 5.06 s^-1; kcat/Km 1.40 uM^-1 s^-1


column_label: Table 2: Kinetic parameters of glQR for the electron donors; Table 2, Menadione / NADPH electron donor row; Kapp_m 30.85 +/- 4.70 uM; kcat 52.68 +/- 1.95 s^-1; kcat/Km 1.71 uM^-1 s^-1.


substrate_name: Unknown

proof_lines:
cofactor NADH
cofactor NADPH

substrate: Unknown


organism: Halobacterium salinarum


proof_lines: in untreated vesicles, in low salt disrupted membranes and in French-press treated preparations

proof_lines: in low-salt and detergent-solubilized fractions


organism: Octopus vulgaris


enzyme_display_name: monodehydroascorbate reductase (NADH)

organism: Oryctolagus cuniculus

proof_lines:
with substrate monodehydroascorbate
with ferricyanide as substrate

enzyme: monodehydroascorbate reductase (NADH)


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: monodehydroascorbate

substrate: monodehydroascorbate


organism: Saccharomyces cerevisiae

substrate_name: benzoquinone

substrate: benzoquinone


assay_conditions_summary: pH 6; 296.15 K; cofactor NADH


organism: Pleurotus ostreatus


organism: Neurospora crassa

substrate_name: semidehydroascorbic acid

substrate: semidehydroascorbic acid


organism: Rattus norvegicus


proof_lines: reaction with semidehydro-D(-)-ascorbic acid and semidehydro-L(+)-ascorbic acid


assay_conditions_summary: cofactor NADPH


organism: Gammarus pulex


organism: Plasmodium falciparum

proof_lines:
cosubstrate: decylubiquinone
cosubstrate: ubiquinone-1


organism: Burkholderia sp. SJ98

substrate_name: p-benzoquinone

proof_lines: pH 7.4, temperature not specified in the publication

substrate: p-benzoquinone


organism: Paracoccus denitrificans

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E77L with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80L with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80E with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80M with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G115I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G115F to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature E77M could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80K with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature E77A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R95E 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 S113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R95A 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 Y78A with inferred residue-numbering offset -9 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 7.4, 25°C, recombinant wild-type enzyme


enzyme_display_name: Quinone reductase

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

substrate_name: benzoquinone (at pH 7.5 and 70 degrees Celsius)

proof_lines: kcat is 930 sec(-1) with benzoquinone as substrate (at pH 7.5 and 70 degrees Celsius) (PubMed:15840577). kcat is 440 sec(-1) with menaquinone as substrate (at pH 8.0 and 60 degrees Celsius) (PubMed:15840577). kcat is 25 sec(-1) with duroqui

enzyme: Quinone reductase


substrate_name: menaquinone (at pH 8.0 and 60 degrees Celsius)

assay_conditions_summary: pH 8


substrate_name: duroquinone (at pH 8.0 and 70 degrees Celsius)


substrate_name: coenzyme Q1 (at pH 8.5 and 60 degrees Celsius)


enzyme_display_name: Zeta-crystallin

organism: Homo sapiens

proof_lines: kcat is 170 min(-1) with 1,2-naphthoquinone as substrate. kcat is 130 min(-1) with 9,10-phenanthroquinone as substrate.

enzyme: Zeta-crystallin


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


enzyme_display_name: NAD(P)H dehydrogenase [quinone] 1

proof_lines: kcat is 0.075 min(-1) NADH with as substrate. kcat is 0.074 min(-1) with NADPH as substrate.

enzyme: NAD(P)H dehydrogenase [quinone] 1


proof_lines: kcat is 250 min(-1) with 1,2-naphthoquinone as substrate. kcat is 250 min(-1) with 9,10-phenanthroquinone as substrate.


substrate_name: menadione


enzyme_display_name: Dioscorin dioA3

organism: Dioscorea japonica

substrate_name: dehydroascorbate (DHA) (at ph 7.0 and 30 degrees Celsius)

proof_lines: kcat is 0.0152 min(-1) for DHA. kcat is 30500 min(-1) for sodium bicarbonate.

enzyme: Dioscorin dioA3


substrate_name: sodium bicarbonate (at ph 7.1 and 4 degrees Celsius)


organism: Escherichia coli (strain K12)

substrate_name: chromate (at pH 5 and 35 degrees Celsius)

assay_conditions_summary: pH 5

proof_lines: kcat is 3.7 sec(-1) with chromate as substrate (at pH 5 and 35 degrees Celsius) (PubMed:14766567). kcat is 29 sec(-1) with uranyl as substrate (at pH 7 and 37 degrees Celsius) (PubMed:17088379). kcat is 30 sec(-1) with chromate as substrate


substrate_name: chromate (at pH 5 and 70 degrees Celsius)


enzyme_display_name: NADPH-dependent quinone oxidoreductase VAT1

proof_lines: kcat is 1.13 sec(-1) with 9,10-phenanthroquinone as substrate.


enzyme_display_name: cytochrome-b5 reductase

organism: Badhamia polycephala

substrate_name: ferricytochrome b5

enzyme: cytochrome-b5 reductase

substrate: ferricytochrome b5


organism: Bos taurus

substrate_name: NADH; Ferricytochrome b5

assay_conditions_summary: cofactor NAD+

substrate: NADH; Ferricytochrome b5


enzyme_display_name: NADH-cytochrome b5 reductase 3

organism: Canis lupus familiaris

substrate_name: 2 Fe(II)-[cytochrome b5

enzyme: NADH-cytochrome b5 reductase 3

substrate: 2 Fe(II)-[cytochrome b5


substrate_name: Hexacyanoferrate(III); NADPH

assay_conditions_summary: cofactor NADP+

substrate: Hexacyanoferrate(III); NADPH


substrate_name: 2 Fe(III)-[cytochrome b5]

substrate: 2 Fe(III)-[cytochrome b5]


enzyme_display_name: NADH-cytochrome b5 reductase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: cytochrome b5

enzyme: NADH-cytochrome b5 reductase 1

substrate: cytochrome b5


enzyme_display_name: NADPH---hemoprotein reductase

organism: Arabidopsis thaliana

substrate_name: NADPH; Cytochrome c; H+

enzyme: NADPH---hemoprotein reductase

substrate: NADPH; Cytochrome c; H+


substrate_name: H+; NADPH; Cytochrome c

substrate: H+; NADPH; Cytochrome c


enzyme_display_name: NADPH--cytochrome P450 reductase 1

organism: Artemisia annua

substrate_name: cytochrome P450

enzyme: NADPH--cytochrome P450 reductase 1

substrate: cytochrome P450


enzyme_display_name: NADPH-hemoprotein reductase

organism: Botryococcus braunii

substrate_name: ferricytochrome c

enzyme: NADPH-hemoprotein reductase

substrate: ferricytochrome c


organism: Candida tropicalis

substrate_name: Cytochrome c; H+; NADPH

substrate: Cytochrome c; H+; NADPH


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase

organism: Fusarium oxysporum

substrate_name: laurate/dodecanoic acid

substrate: laurate/dodecanoic acid


organism: Archaeoglobus fulgidus

substrate_name: NADH; Hexacyanoferrate(III)

substrate: NADH; Hexacyanoferrate(III)


organism: Escherichia coli


substrate_name: NADPH; Methyl-1,4-benzoquinone

substrate: NADPH; Methyl-1,4-benzoquinone


substrate_name: H+; 2,6-Dichloroindophenol; NADH

substrate: H+; 2,6-Dichloroindophenol; NADH


organism: Leishmania major

substrate_name: NADH; H+; Menadione

substrate: NADH; H+; Menadione


organism: Mycobacterium tuberculosis

substrate_name: NADH; Menadione; H+

substrate: NADH; Menadione; H+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T59F with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

smiles: CC(=O)C=C


smiles: CCCC=CC=O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T53F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: propenal

smiles: C=CC=O

substrate: propenal


smiles: CCC(C=CC=O)O


smiles: CC=CC(=O)C


smiles: CCCCCC=CC(=O)C


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

substrate: NADPH


substrate_name: H+; NADH; Ferricytochrome b5

substrate: H+; NADH; Ferricytochrome b5


substrate_name: ferricytochrome b5

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L41A to reconstruct the assayed variant sequence.

substrate: ferricytochrome b5


organism: Rattus norvegicus

substrate_name: ferricytochome b5

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L148P with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: ferricytochome b5


substrate_name: ferrocytochrome b5

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179A with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer triplicate in 116 mM MOPS; cofactor NADH

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179A'; column 'kcat (s^-1), NADH:BR activity group' = 245; column 'Km cyt b5 (uM), NADH:BR activity group' = 8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 245 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 245.0 s^(-1). Km: printed Table 2 cell 8 uM; 8 / 1000 = 0.008 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement and this catalog row carries no catalytic-efficiency value, so none is claimed.

raw_value_unit_evidence: Table 2, protein row G179A, NADH:BR activity columns: kcat = 245 s^-1; Km = 8 uM.

substrate: ferrocytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179T with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179T'; column 'kcat (s^-1), NADH:BR activity group' = 18; column 'Km cyt b5 (uM), NADH:BR activity group' = 43.

normalized_value_unit_evidence: kcat: printed Table 2 cell 18 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 18.0 s^(-1). Km: printed Table 2 cell 43 uM; 43 / 1000 = 0.043 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement and this catalog row carries no catalytic-efficiency value, so none is claimed.

raw_value_unit_evidence: Table 2, protein row G179T, NADH:BR activity columns: kcat = 18 s^-1; Km = 43 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179V with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179V'; column 'kcat (s^-1), NADH:BR activity group' = 17; column 'Km cyt b5 (uM), NADH:BR activity group' = 107.

normalized_value_unit_evidence: kcat: printed Table 2 cell 17 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 17.0 s^(-1). Km: printed Table 2 cell 107 uM; 107 / 1000 = 0.107 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement and this catalog row carries no catalytic-efficiency value, so none is claimed.

raw_value_unit_evidence: Table 2, protein row G179V, NADH:BR activity columns: kcat = 17 s^-1; Km = 107 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6AY12 and applied mutation signature G179P with inferred residue-numbering offset -24 to reconstruct the assayed variant sequence.

column_label: Table 2: NAD(P)H:FR and NADH:BR Kinetic Constants Obtained for the Various cb5r G179 Mutants (Biochemistry 2005, 44, 13467-13476), protein row 'G179P'; column 'kcat (s^-1), NADH:BR activity group' = 10; column 'Km cyt b5 (uM), NADH:BR activity group' = 1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 10 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 10.0 s^(-1). Km: printed Table 2 cell 1 uM; 1 / 1000 = 0.001 mM. kcat/Km: the paper prints no catalytic-efficiency cell for this measurement and this catalog row carries no catalytic-efficiency value, so none is claimed.

raw_value_unit_evidence: Table 2, protein row G179P, NADH:BR activity columns: kcat = 10 s^-1; Km = 1 uM.


organism: Sus scrofa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature ΔF272 with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: NADH; H+; Ferricytochrome b5

proof_lines: kcat is 570 sec(-1) with NADH as substrate (PubMed:10082957). kcat is 560 sec(-1) with 2 Fe(II)-[cytochrome b5] as substrate (PubMed:10082957). kcat is 1100 sec(-1) with NADH as substrate (PubMed:11574067, PubMed:12459552). kcat is 661 sec(

substrate: NADH; H+; Ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K97A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R63A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R63Q with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


organism: Gallus gallus

substrate_name: NADPH; Cytochrome c; H+

substrate: NADPH; Cytochrome c; H+


organism: Homo sapiens

substrate_name: Ferricytochrome c; NADPH; H+

substrate: Ferricytochrome c; NADPH; H+


organism: Oryza sativa subsp. japonica

substrate_name: cytochrome c

substrate: cytochrome c


enzyme_display_name: NADPH--cytochrome P450 reductase 2

enzyme: NADPH--cytochrome P450 reductase 2


organism: Picrorhiza kurrooa

substrate_name: oxidized cytochrome c

substrate: oxidized cytochrome c


organism: Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)

substrate_name: lauric acid at pH 7.4 at room temperature

proof_lines: kcat is 84.1 sec(-1) for lauric acid (PubMed:16403573). kcat is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N-palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine.

enzyme: Bifunctional cytochrome P450/NADPH--P450 reductase


organism: Saccharomyces cerevisiae

substrate_name: Cytochrome c; H+; NADPH

proof_lines: The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.

substrate: Cytochrome c; H+; NADPH


organism: Escherichia coli (strain K12)

substrate_name: uranyl (at pH 7 and 37 degrees Celsius)

assay_conditions_summary: pH 7

substrate: uranyl (at pH 7 and 37 degrees Celsius)


organism: Kluyveromyces marxianus

substrate_name: 1,4-Benzoquinone; H+; NADPH

substrate: 1,4-Benzoquinone; H+; NADPH


organism: Mus musculus

substrate_name: Unknown

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K97R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R63K with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


organism: Anopheles minimus

substrate_name: ferricytochrome c

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature L86F/L219F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C

substrate: ferricytochrome c


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase 1

organism: Bacillus subtilis (strain 168)

substrate_name: cytochrome c (in the reductase assay)

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

proof_lines: kcat is 430 min(-1) for stearic acid hydroxylation. kcat is 5430 min(-1) for phytanic acid hydroxylation. kcat is 6105 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 11400 min(-1) for the reduction of cytochrome c. kcat is 38150

substrate: cytochrome c (in the reductase assay)


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase 2

proof_lines: kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytan


organism: Capsicum annuum


enzyme_display_name: Monodehydroascorbate reductase

organism: Pisum sativum

enzyme: Monodehydroascorbate reductase


organism: Triphysaria versicolor

proof_lines: kcat is 23.3 sec(-1) with 9,10-phenanthrenequinone as substrate. kcat is 2.44 sec(-1) with 1,2-naphthoquinone as substrate. kcat is 0.31 sec(-1) with 5-hydroxy-1,4-naphthoquinone as substrate. kcat is 0.09 sec(-1) with 2,6-dimethoxy-p-benzo


enzyme_display_name: 2-hydroxy-1,4-benzoquinone reductase

organism: Burkholderia sp

enzyme: 2-hydroxy-1,4-benzoquinone reductase


enzyme_display_name: Quinone reductase

organism: Pseudomonas putida


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


organism: Rattus norvegicus


enzyme_display_name: NAD(P)H dehydrogenase (quinone)


enzyme_display_name: Monodehydroascorbate reductase, fruit isozyme

organism: Cucumis sativus


enzyme_display_name: Monodehydroascorbate reductase II

organism: Glycine max

enzyme: Monodehydroascorbate reductase II


enzyme_display_name: monodehydroascorbate reductase (NADH)

organism: Arabidopsis thaliana

substrate_name: Monodehydroascorbate; H+; NADH

substrate: Monodehydroascorbate; H+; NADH


enzyme_display_name: NADPH:quinone reductase

organism: Cavia porcellus

assay_conditions_summary: pH 7.5; cofactor NADPH

enzyme: NADPH:quinone reductase


organism: Homo sapiens


enzyme_display_name: p-benzoquinone reductase (NADPH)

organism: Pseudomonas sp.

enzyme: p-benzoquinone reductase (NADPH)


enzyme_display_name: Self-sufficient cytochrome P450 monooxygenase CYP505E3

organism: Phanerodontia chrysosporium

substrate_name: nonanol

smiles: CCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 9 nonanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=3.8 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 9 nonanol: Km 3,800 uM (3.8 mM); kcat 250 min^-1; kcat/Km 6.6 × 10−2 min^-1 uM^-1.

row_label: C 9 nonanol

substrate: nonanol


substrate_name: decanol

smiles: CCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 10 decanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=1.1 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 10 decanol: Km 1,100 uM (1.1 mM); kcat 220 min^-1; kcat/Km 2.0 × 10−3 min^-1 uM^-1.

row_label: C 10 decanol

enzyme: Self-sufficient cytochrome P450 monooxygenase CYP505E3

substrate: decanol


substrate_name: undecanol

smiles: CCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 11 undecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.42 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 11 undecanol: Km 420 uM (0.42 mM); kcat 310 min^-1; kcat/Km 0.74 min^-1 uM^-1.

row_label: C 11 undecanol

substrate: undecanol


substrate_name: dodecanol

smiles: CCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 12 dodecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.35 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 12 dodecanol: Km 350 uM (0.35 mM); kcat 350 min^-1; kcat/Km 1.0 min^-1 uM^-1.

row_label: C 12 dodecanol

substrate: dodecanol


substrate_name: tridecanol

smiles: CCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 13 tridecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.12 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 13 tridecanol: Km 120 uM (0.12 mM); kcat 370 min^-1; kcat/Km 3.1 min^-1 uM^-1.

row_label: C 13 tridecanol

substrate: tridecanol


substrate_name: tetradecanol

smiles: CCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 14 tetradecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.02 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 14 tetradecanol: Km 20 uM (0.02 mM); kcat 450 min^-1; kcat/Km 23 min^-1 uM^-1.

row_label: C 14 tetradecanol

substrate: tetradecanol


substrate_name: pentadecanol

smiles: CCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 15 pentadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.01 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 15 pentadecanol: Km 10 uM (0.01 mM); kcat 490 min^-1; kcat/Km 49 min^-1 uM^-1.

row_label: C 15 pentadecanol

substrate: pentadecanol


substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 16 hexadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.018 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 16 hexadecanol: Km 18 uM (0.018 mM); kcat 510 min^-1; kcat/Km 28 min^-1 uM^-1.

row_label: C 16 hexadecanol

substrate: hexadecanol


substrate_name: heptadecanol

smiles: CCCCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 17 heptadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.015 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 17 heptadecanol: Km 15 uM (0.015 mM); kcat 340 min^-1; kcat/Km 23 min^-1 uM^-1.

row_label: C 17 heptadecanol

substrate: heptadecanol


substrate_name: octadecanol

smiles: CCCCCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 18 octadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.019 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 18 octadecanol: Km 19 uM (0.019 mM); kcat 330 min^-1; kcat/Km 17 min^-1 uM^-1.

row_label: C 18 octadecanol

substrate: octadecanol


enzyme_display_name: cytochrome-b5 reductase

organism: Sus scrofa

substrate_name: ferricytochrome b5

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K97A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row K97A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); K97A / ferricytochrome b5: Km 16.1 +/- 2.7 uM; kcat 191 +/- 18 s^-1; kcat/Km 11.9 +/- 3.1 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0161 mM; kcat=191.0 s^-1; kcat/Km=11900.0 s^-1*mM^-1.

row_label: K97A / ferricytochrome b5

substrate: ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K97R to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row K97R / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); K97R / ferricytochrome b5: Km 6.9 +/- 0.5 uM; kcat 415 +/- 12 s^-1; kcat/Km 60.1 +/- 6.1 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0069 mM; kcat=415.0 s^-1; kcat/Km=60100.0 s^-1*mM^-1.

row_label: K97R / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature R63A to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row R63A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); R63A / ferricytochrome b5: Km 42.1 +/- 4.7 uM; kcat 121 +/- 10 s^-1; kcat/Km 2.9 +/- 0.6 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0421 mM; kcat=121.0 s^-1; kcat/Km=2900.0 s^-1*mM^-1.

row_label: R63A / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature R63K to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row R63K / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); R63K / ferricytochrome b5: Km 7.3 +/- 0.4 uM; kcat 347 +/- 9 s^-1; kcat/Km 47.5 +/- 3.8 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0073 mM; kcat=347.0 s^-1; kcat/Km=47500.0 s^-1*mM^-1.

row_label: R63K / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature R63Q to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row R63Q / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); R63Q / ferricytochrome b5: Km 18.5 +/- 1.4 uM; kcat 105 +/- 4 s^-1; kcat/Km 5.7 +/- 0.6 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0185 mM; kcat=105.0 s^-1; kcat/Km=5700.0 s^-1*mM^-1.

row_label: R63Q / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature S99A to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row S99A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); S99A / ferricytochrome b5: Km 14.8 +/- 2.2 uM; kcat 295 +/- 23 s^-1; kcat/Km 19.9 +/- 4.5 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0148 mM; kcat=295.0 s^-1; kcat/Km=19900.0 s^-1*mM^-1.

row_label: S99A / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature S99T to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row S99T / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); S99T / ferricytochrome b5: Km 11.8 +/- 2.3 uM; kcat 520 +/- 49 s^-1; kcat/Km 44.1 +/- 12.8 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0118 mM; kcat=520.0 s^-1; kcat/Km=44100.0 s^-1*mM^-1.

row_label: S99T / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature S99V to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row S99V / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); S99V / ferricytochrome b5: Km 9.9 +/- 2.0 uM; kcat 165 +/- 14 s^-1; kcat/Km 16.7 +/- 4.8 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0099 mM; kcat=165.0 s^-1; kcat/Km=16700.0 s^-1*mM^-1.

row_label: S99V / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature Y65A to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row Y65A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); Y65A / ferricytochrome b5: Km 5.0 +/- 0.7 uM; kcat 107 +/- 5 s^-1; kcat/Km 21.4 +/- 4.0 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.005 mM; kcat=107.0 s^-1; kcat/Km=21400.0 s^-1*mM^-1.

row_label: Y65A / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature Y65F to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row Y65F / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); Y65F / ferricytochrome b5: Km 6.2 +/- 0.4 uM; kcat 375 +/- 9 s^-1; kcat/Km 60.5 +/- 5.4 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0062 mM; kcat=375.0 s^-1; kcat/Km=60500.0 s^-1*mM^-1.

row_label: Y65F / ferricytochrome b5


substrate_name: nonanoic acid

smiles: CCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 9 nonanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=4.5 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 9 nonanoic acid: Km 4,500 uM (4.5 mM); kcat 200 min^-1; kcat/Km 4.4 × 10−2 min^-1 uM^-1.

row_label: C 9 nonanoic acid

substrate: nonanoic acid


substrate_name: decanoic acid

smiles: CCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 10 decanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=1.4 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 10 decanoic acid: Km 1,400 uM (1.4 mM); kcat 230 min^-1; kcat/Km 0.16 min^-1 uM^-1.

row_label: C 10 decanoic acid

substrate: decanoic acid


substrate_name: undecanoic acid

smiles: CCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 11 undecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.61 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 11 undecanoic acid: Km 610 uM (0.61 mM); kcat 230 min^-1; kcat/Km 0.38 min^-1 uM^-1.

row_label: C 11 undecanoic acid

substrate: undecanoic acid


substrate_name: dodecanoic acid

smiles: CCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 12 dodecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.45 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 12 dodecanoic acid: Km 450 uM (0.45 mM); kcat 250 min^-1; kcat/Km 0.56 min^-1 uM^-1.

row_label: C 12 dodecanoic acid

substrate: dodecanoic acid


substrate_name: tridecanoic acid

smiles: CCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 13 tridecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.23 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 13 tridecanoic acid: Km 230 uM (0.23 mM); kcat 310 min^-1; kcat/Km 1.4 min^-1 uM^-1.

row_label: C 13 tridecanoic acid

substrate: tridecanoic acid


substrate_name: tetradecanoic acid

smiles: CCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 14 tetradecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.065 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 14 tetradecanoic acid: Km 65 uM (0.065 mM); kcat 320 min^-1; kcat/Km 4.9 min^-1 uM^-1.

row_label: C 14 tetradecanoic acid

substrate: tetradecanoic acid


substrate_name: pentadecanoic acid

smiles: CCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 15 pentadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.03 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 15 pentadecanoic acid: Km 30 uM (0.03 mM); kcat 390 min^-1; kcat/Km 13 min^-1 uM^-1.

row_label: C 15 pentadecanoic acid

substrate: pentadecanoic acid


substrate_name: hexadecanoic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 16 hexadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.038 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 16 hexadecanoic acid: Km 38 uM (0.038 mM); kcat 330 min^-1; kcat/Km 8.7 min^-1 uM^-1.

row_label: C 16 hexadecanoic acid

substrate: hexadecanoic acid


substrate_name: heptadecanoic acid

smiles: CCCCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 17 heptadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.036 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 17 heptadecanoic acid: Km 36 uM (0.036 mM); kcat 280 min^-1; kcat/Km 7.8 min^-1 uM^-1.

row_label: C 17 heptadecanoic acid

substrate: heptadecanoic acid


substrate_name: octadecanoic acid

smiles: CCCCCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 18 octadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.028 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 18 octadecanoic acid: Km 28 uM (0.028 mM); kcat 260 min^-1; kcat/Km 9.3 min^-1 uM^-1.

row_label: C 18 octadecanoic acid

substrate: octadecanoic acid


organism: Paracoccus denitrificans

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

column_label: Table 2 / row FerBHis6-E77A / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77A normalized: K_m 0.18 mM; kcat 17.9 s^-1; kcat/K_m 99 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-E77A: K_m 180±30 uM; kcat 17.9±3.0 s^-1; kcat/K_m 99±23 mM^-1 s^-1.

table_label: Table 2

enzyme: NAD(P)H dehydrogenase (quinone)

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77K to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-E77K / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77K normalized: K_m 0.03 mM; kcat 0.75 s^-1; kcat/K_m 25 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-E77K: K_m 30±8 uM; kcat 0.75±0.05 s^-1; kcat/K_m 25±7 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77L to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-E77L / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77L normalized: K_m 0.25 mM; kcat 0.072 s^-1; kcat/K_m 0.29 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77M to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-E77M / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77M normalized: K_m 0.42 mM; kcat 2.5 s^-1; kcat/K_m 6 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G115F to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G115F; columns Km NADH 410 uM (normalized 0.41 mM); kcat 2.2 s^-1; printed kcat/Km 5.4 mM^-1 s^-1; export-normalized kcat/Km 5.36585365853659 from same-row values

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; Km normalized_value=0.41 normalized_unit=mM from 410 uM; kcat/Km normalized_value=5.36585365853659 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=2.2 raw_unit=s^-1; Km raw_value=410 raw_unit=uM for NADH; printed kcat/Km=5.4 mM^-1 s^-1

table_label: Table 2. Kinetic parameters and standard redox potentials of FerBHis6 for the wild-type and mutant variants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G115I to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G115I; columns Km NADH 630 uM (normalized 0.63 mM); kcat 1.7 s^-1; printed kcat/Km 2.7 mM^-1 s^-1; export-normalized kcat/Km 2.6984126984127 from same-row values

normalized_value_unit_evidence: kcat normalized_value=1.7 normalized_unit=s^-1; Km normalized_value=0.63 normalized_unit=mM from 630 uM; kcat/Km normalized_value=2.6984126984127 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=1.7 raw_unit=s^-1; Km raw_value=630 raw_unit=uM for NADH; printed kcat/Km=2.7 mM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G118F to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G118F; columns Km NADH 85 uM (normalized 0.085 mM); kcat 77 s^-1; printed kcat/Km 906 mM^-1 s^-1; export-normalized kcat/Km 905.882352941176 from same-row values

normalized_value_unit_evidence: kcat normalized_value=77 normalized_unit=s^-1; Km normalized_value=0.085 normalized_unit=mM from 85 uM; kcat/Km normalized_value=905.882352941176 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=77 raw_unit=s^-1; Km raw_value=85 raw_unit=uM for NADH; printed kcat/Km=906 mM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G118I to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G118I; columns Km NADH 38 uM (normalized 0.038 mM); kcat 12 s^-1; printed kcat/Km 316 mM^-1 s^-1; export-normalized kcat/Km 315.789473684211 from same-row values

normalized_value_unit_evidence: kcat normalized_value=12 normalized_unit=s^-1; Km normalized_value=0.038 normalized_unit=mM from 38 uM; kcat/Km normalized_value=315.789473684211 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; Km raw_value=38 raw_unit=uM for NADH; printed kcat/Km=316 mM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature R80E to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-R80E / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-R80E normalized: K_m 0.03 mM; kcat 0.275 s^-1; kcat/K_m 9.2 s^-1 mM^-1.