substrate_name: L-Met

substrate: L-Met


enzyme_display_name: monoamine oxidase

organism: Homo sapiens

substrate_name: dopamine

source_db: brenda

verification_status: unverified

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.

enzyme: monoamine oxidase

substrate: dopamine

status: unverified

source: brenda


substrate_name: serotonin

proof_lines:
11°C
monoamine oxidase A
monoamine oxidase B

substrate: serotonin


substrate_name: Phenylethylamine

proof_lines: pH 7.5, MAO-A incorporated into phospholipid nanodisks

substrate: Phenylethylamine


substrate_name: kynuramine

substrate: kynuramine


enzyme_display_name: D-amino-acid oxidase

substrate_name: D-alanine

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

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

mutation_type: substitution

enzyme: D-amino-acid oxidase

substrate: D-alanine


assay_conditions_summary: cofactor FAD


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

enzyme: glutamate dehydrogenase [NAD(P)+]

substrate: NADH


enzyme_display_name: dihydrofolate reductase

proof_lines: recombinant wild-type enzyme, pH 7.4, 37°C

proof_lines: pH 7.4, 37°C, wild-type enzyme and mutant N64F

enzyme: dihydrofolate reductase


substrate_name: Unknown

kcat_display: Not reported

km_display: Not reported

ki_unit: mM

proof_lines:
wild-type, pH 7.6, 23°C
pH 7.4, 37°C, wild-type enzyme
wild-type, pH 7.0, 25°C

substrate: Unknown


proof_lines: mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C


substrate_name: NADPH

assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADPH

substrate: NADPH


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


substrate_name: D-serine

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

assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM sodium diphosphate

proof_lines:
pH 8.5, 25°C, recombinant EGFP-DAAO
pH 8.3, 25°C
pH 8.5, 25°C

substrate: D-serine


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


substrate_name: dihydrofolate

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines:
pH 7.5, 25°C, cosubstrate: NADPH
pH 7.5, 25°C

substrate: dihydrofolate


proof_lines: pH 7.5, 25°C, cosubstrate: dihydrofolate

proof_lines: for native and recombinant enzymes, monophasic


enzyme_display_name: pyrroline-5-carboxylate reductase

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

enzyme: pyrroline-5-carboxylate reductase


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


enzyme_display_name: 6,7-dihydropteridine reductase

substrate_name: tetrahydrobiopterin

enzyme: 6,7-dihydropteridine reductase

substrate: tetrahydrobiopterin


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: wild-type, cosubstrate NADPH, pH 7.5, 37°C

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, with NADPH


enzyme_display_name: primary-amine oxidase

substrate_name: tyramine

proof_lines: recombinant enzyme expressed in CHO cells

enzyme: primary-amine oxidase

substrate: tyramine


substrate_name: tryptamine

substrate: tryptamine


substrate_name: folate

substrate: folate


proof_lines:
pH 6.0
recombinant enzyme
pH 7.4, 37°C


assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines: pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM)

proof_lines: pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM)


organism: Lathyrus oleraceus

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: tetrahydropteroylglutamic acid

substrate: tetrahydropteroylglutamic acid


organism: Mus musculus

substrate_name: benzylamine

substrate: benzylamine


substrate_name: hexakis(benzylammonium) decavanadate (V) dihydrate


smiles: O=O

assay_conditions_summary: pH 7.2; 310.15 K; buffer 100 mM potassium phosphate

proof_lines: cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C

proof_lines: copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C


substrate_name: putrescine

smiles: C(CCN)CN

proof_lines: copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C

substrate: putrescine


proof_lines:
pH 7.4, 37°C, enzyme from brain
pH 7.4, 37°C, enzyme from liver
monoamine oxidase B


proof_lines:
pH 7.4, 37°C, enzyme from brain
pH 7.4, 37°C, enzyme from liver


enzyme_display_name: D-aspartate oxidase

substrate_name: D-Aspartate

assay_conditions_summary: pH 8.3; 310.15 K; buffer 40 mM sodium diphosphate

proof_lines: wild type enzyme fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

proof_lines: His-tagged wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

enzyme: D-aspartate oxidase

substrate: D-Aspartate


substrate_name: N-Methyl-D-aspartate

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

substrate: N-Methyl-D-aspartate


enzyme_display_name: alanine dehydrogenase

organism: Mycobacterium tuberculosis

substrate_name: NAD+

assay_conditions_summary: pH 6.4; 295.15 K; cofactor NAD+

proof_lines: pH 6.4, 22°C, recombinant His6-tagged enzyme

proof_lines: pH and temperature not specified in the publication

enzyme: alanine dehydrogenase

substrate: NAD+


smiles: N


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: with NADH as cosubstrate, at 25°C and 100 mM HEPES, pH 7.5

proof_lines: with NAPH as cosubstrate, at 25°C and 100 mM HEPES, pH 7.5


proof_lines: Km less than 0.001 mM, at 25°C and 100 mM HEPES, pH 7.5


substrate_name: NADH


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: formyltetrahydrofolate dehydrogenase

organism: Oryctolagus cuniculus

enzyme: formyltetrahydrofolate dehydrogenase


assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADH

proof_lines:
recombinant enzyme
enzyme from brain
37°C, pH 7.2

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

proof_lines:
recombinant enzyme
37°C, pH 7.2


organism: Papio sp.


organism: Plasmodium falciparum

substrate_name: Unknown

proof_lines:
wild-type, pH 7.0, 25°C
wild-type, 25°C, pH 7.0
wild-type, pH 5.0, 25°C

substrate: Unknown


organism: Paenarthrobacter nicotinovorans

substrate_name: sarcosine

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

smiles: CNCC(=O)O

assay_conditions_summary: pH 10

proof_lines: pH 10, temperature not specified in the publication

data_origin: experimental

substrate: sarcosine


organism: Pneumocystis jirovecii

proof_lines: His-tagged human-derived enzyme, pH 7.65


assay_conditions_summary: pH 7.65; cofactor NADPH

substrate: NADPH


enzyme_display_name: diaminopimelate dehydrogenase

organism: Porphyromonas gingivalis

assay_conditions_summary: pH 10.5; 298.15 K; cofactor NADP+

enzyme: diaminopimelate dehydrogenase


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


organism: Plasmodium vivax

proof_lines:
wild-type
wild-type enzyme


organism: Priestia megaterium

assay_conditions_summary: cofactor NADH


enzyme_display_name: flavin reductase (NADH)

organism: Pseudomonas putida

enzyme: flavin reductase (NADH)


substrate_name: FAD

substrate: FAD


enzyme_display_name: glutamate synthase (NADPH)

organism: Pseudomonas aeruginosa

substrate_name: L-glutamine

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

assay_conditions_summary: cofactor NADPH

enzyme: glutamate synthase (NADPH)

substrate: L-glutamine


enzyme_display_name: methylamine dehydrogenase (amicyanin)

organism: Pseudomonas sp.

smiles: C(CCCCCCN)CCCCCN

enzyme: methylamine dehydrogenase (amicyanin)


substrate_name: 12-aminododecanoic acid

smiles: C(CCCCCC(=O)O)CCCCCN

substrate: 12-aminododecanoic acid


mutation_signature: Δ1

mutation_type: deletion

assay_conditions_summary: pH 8; 308.15 K; cofactor NADPH

proof_lines: pH 8.0, 35°C, with substrate DELTA1-pyrroline-2-carboxylate

proof_lines: pH 8.0, 35°C, with substrate DELTA1-piperideine-2-carboxylate


assay_conditions_summary: pH 10; 308.15 K; cofactor NADP+

proof_lines: pH 10.0, 35°C, with substrate L-pipecolate


organism: Rattus norvegicus


proof_lines:
37°C
37°C, 60 min preincubation
37°C, no preincubation

substrate: hexakis(benzylammonium) decavanadate (V) dihydrate


enzyme_display_name: dihydromonapterin reductase

enzyme: dihydromonapterin reductase


assay_conditions_summary: pH 7; cofactor NADP+

proof_lines: with 10-formyl-5,8-dideazafolate as substrate

proof_lines: with 10-formyltetrahydrofolate as substrate


assay_conditions_summary: pH 7

proof_lines:
at pH 7
racemic


proof_lines:
native liver enzyme
recombinant liver enzyme
NADH-specific liver enzyme


proof_lines:
mixed inhibition
noncompetitive inhibition
competitive inhibition


substrate_name: D-Asp

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

substrate: D-Asp


enzyme_display_name: pyridoxal 5'-phosphate synthase

organism: Saccharomyces cerevisiae

substrate_name: pyridoxamine 5'-phosphate

proof_lines: enzyme species FI which is assumed to be an artefact of the purification procedure

enzyme: pyridoxal 5'-phosphate synthase

substrate: pyridoxamine 5'-phosphate


substrate_name: pyridoxine 5'-phosphate

substrate: pyridoxine 5'-phosphate


enzyme_display_name: glutamate synthase (NADH)

enzyme: glutamate synthase (NADH)


proof_lines:
with N10-formyldihydrofolate
with 7,8-dihydrofolate
with NADPH


enzyme_display_name: saccharopine dehydrogenase (NAD+, L-lysine-forming)

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+


substrate_name: saccharopine

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

enzyme: saccharopine dehydrogenase (NAD+, L-lysine-forming)

substrate: saccharopine


organism: Staphylococcus aureus


enzyme_display_name: D-amino-acid oxidase

organism: Sus scrofa

substrate_name: D-valine

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

enzyme: D-amino-acid oxidase

substrate: D-valine


substrate_name: D-serine

proof_lines:
wild-type
wild-type enzyme
pH 8.3, 37°C, wild-type enzyme

substrate: D-serine


enzyme_display_name: diamine oxidase

proof_lines: pH 7.9, 30°C, higher KM-value compared with N-methylputrescine or cadaverine as substrates, Vmax: 21.9 pkat

enzyme: diamine oxidase


substrate_name: N-methylputrescine

smiles: CNCCCCN

proof_lines: pH 7.9, 30°C, lowest KM-value compared with putrescine or cadaverine as substrates, Vmax: 23.3 pkat

substrate: N-methylputrescine


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: cadaverine

smiles: C(CCN)CCN

proof_lines: pH 7.9, 30°C, higher KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 20.5 pkat

substrate: cadaverine


enzyme_display_name: dihydrofolate reductase

enzyme: dihydrofolate reductase


proof_lines:
racemic, fluorimetric assay
racemic, spectrophotometric assay
(-)-isomer


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines:
spectrophotometric assay
fluorimetric assay

substrate: NADP+


enzyme_display_name: monoamine oxidase

substrate_name: Phenylethylamine

enzyme: monoamine oxidase

substrate: Phenylethylamine


substrate: Unknown


enzyme_display_name: pyrroline-5-carboxylate reductase

organism: Trypanosoma cruzi

enzyme: pyrroline-5-carboxylate reductase


substrate_name: NADPH

assay_conditions_summary: pH 7; 301.15 K; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADPH

proof_lines: cosubstrate 5,10-methylenetetrahydrofolate, pH 7.2, 25°C


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

proof_lines:
cosubstrate NADPH, pH 7.2, 25°C
cosubstrate NADH, pH 7.2, 25°C
pH 7.2, 30°C


enzyme_display_name: aspartate dehydrogenase

organism: Archaeoglobus fulgidus

assay_conditions_summary: 323.15 K; cofactor NADH

proof_lines: pH not specified in the publication, 50°C, with NADH

enzyme: aspartate dehydrogenase


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Aspergillus niger

assay_conditions_summary: pH 8; 301.15 K; cofactor NADPH

enzyme: glutamate dehydrogenase (NADP+)


proof_lines: mutant enzyme W230I/W430R, pH and temperature not specified in the publication


organism: Azospirillum brasilense

assay_conditions_summary: pH 8.5; 298.15 K; buffer Hepes, pH 8; cofactor NADPH

proof_lines: holoenzyme, buffer: Hepes, pH 8.5 or 7.5

proof_lines: dimeric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 2.5 mM 2-oxoglutarate, and 0.1 mM NADPH


substrate_name: thio-NADPH

proof_lines: in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 54% that obtained in the presence of NADPH

proof_lines: in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 3.7% that obtained in the presence of NADPH

proof_lines: inhibitor of the holoenzyme, competitive with NADPH

substrate: thio-NADPH


enzyme_display_name: FMN reductase (NADPH)

organism: Bacillus cereus

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

enzyme: FMN reductase (NADPH)


enzyme_display_name: L-aspartate oxidase

organism: Arabidopsis thaliana

substrate_name: L-aspartate

enzyme: L-aspartate oxidase

substrate: L-aspartate


enzyme_display_name: glycine oxidase

organism: Bacillus subtilis

substrate_name: glycine

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

proof_lines: pH 8.5, 37°C, mutant enzyme T42A/C245S/L301V

enzyme: glycine oxidase

substrate: glycine


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM HEPES/KOH; cofactor NADPH

proof_lines: dimeric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 0.1 mM NADPH

proof_lines: hexameric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 0.1 mM NADPH


enzyme_display_name: primary-amine oxidase

organism: Bos taurus

substrate_name: Benzylamine; H2O; O2

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

enzyme: primary-amine oxidase

substrate: Benzylamine; H2O; O2


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

enzyme: glutamate dehydrogenase [NAD(P)+]


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
pH 8.0, 25°C, recombinant enzyme
pH 8.0, 25°C, native enzyme

substrate: NAD+


enzyme_display_name: alanine dehydrogenase

substrate_name: L-Ala

proof_lines:
at pH 8.6
at pH 7.4

enzyme: alanine dehydrogenase

substrate: L-Ala


substrate_name: benzylamine

substrate: benzylamine


enzyme_display_name: 6,7-dihydropteridine reductase

substrate_name: tetrahydrobiopterin

proof_lines: NADH-specific liver enzyme, cofactor NADPH

proof_lines: NADH-specific liver enzyme, cofactor NADH

proof_lines: NADPH-specific liver enzyme, cofactor NADPH

enzyme: 6,7-dihydropteridine reductase

substrate: tetrahydrobiopterin


substrate_name: kynuramine

substrate: kynuramine


enzyme_display_name: D-aspartate oxidase

substrate_name: D-glutamate

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

proof_lines:
at pH 8.3
at pH 7.4

enzyme: D-aspartate oxidase

substrate: D-glutamate


substrate_name: dihydrobiopterin

substrate: dihydrobiopterin


proof_lines: reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme

proof_lines: NADPH specific liver enzyme, substrate 6-methyl-tetrahydropterin

proof_lines: reduction of quinonoid 7,8-dihydropterin, NADPH-specific enzyme


assay_conditions_summary: pH 5


organism: Candida albicans

substrate_name: Unknown


enzyme_display_name: L-amino-acid oxidase

organism: Crotalus adamanteus

enzyme: L-amino-acid oxidase


organism: Burkholderia cepacia

proof_lines:
strain PC 174
strain PC 178


organism: Corynebacterium sp. P-1

proof_lines: pH and temperature not specified in the publication


organism: Drosophila melanogaster

substrate_name: L-proline

substrate: L-proline


organism: Enterococcus faecalis

substrate_name: NADPH; Dihydrofolate; H+

assay_conditions_summary: cofactor NADPH

substrate: NADPH; Dihydrofolate; H+


organism: Cyprinus carpio

substrate_name: D-alanine

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

proof_lines:
apparent value, at 25°C
pH 8.0, 37°C

substrate: D-alanine


organism: Equus caballus


organism: Escherichia coli

proof_lines: wild type enzyme, at 15°C, pH not specified in the publication


substrate_name: Dihydrofolate; H+; NADH

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADH

proof_lines: pH 7.5, temperature not specified in the publication

substrate: Dihydrofolate; H+; NADH


organism: Enterococcus faecium


enzyme_display_name: dihydromonapterin reductase

enzyme: dihydromonapterin reductase


enzyme_display_name: pyridoxal 5'-phosphate synthase

enzyme: pyridoxal 5'-phosphate synthase


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: chimera with Homo sapiens enzyme, pH 7, 25°C

proof_lines: chimera with Haemophilus influenzae enzyme, pH 7, 25°C


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: pH 7.5, temperature not specified in the publication, cosubstrate: 10-formyl-dihydrofolate


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: glutamate synthase (NADPH)

enzyme: glutamate synthase (NADPH)

substrate: Unknown


proof_lines: NH3-dependent glutamate synthase and apoglutamate synthase


substrate_name: pyridoxal 5'-phosphate

proof_lines: recombinant enzyme after cleavage from fusion protein

substrate: pyridoxal 5'-phosphate


enzyme_display_name: dihydrofolate reductase

substrate_name: dihydrofolate

proof_lines: pH 7.0, 25°C, under atmospheric pressure

enzyme: dihydrofolate reductase

substrate: dihydrofolate


organism: Glycine max

substrate: NADPH


substrate_name: L-aspartate

proof_lines:
oxygen electron acceptor
fumarate electron acceptor
at aspartate concentration 1-20 mM

substrate: L-aspartate


enzyme_display_name: leucine dehydrogenase

organism: Heyndrickxia coagulans

enzyme: leucine dehydrogenase


enzyme_display_name: monoamine oxidase

organism: Homo sapiens

substrate_name: p-tyramine

enzyme: monoamine oxidase

substrate: p-tyramine


enzyme_display_name: D-amino-acid oxidase

substrate_name: Gly

proof_lines:
pH 8.3, 25°C
pH 8.5, 25°C
at pH 7.0 and 25°C

enzyme: D-amino-acid oxidase

substrate: Gly


enzyme_display_name: pyrroline-5-carboxylate reductase

enzyme: pyrroline-5-carboxylate reductase


substrate_name: benzylamine

proof_lines:
recombinant MAO-B
pH 7.4, 30°C, oxidative half-reaction
pH 7.4, 30°C, reductive half-reaction

substrate: benzylamine


substrate_name: hexakis(benzylammonium) decavanadate (V) dihydrate


substrate_name: tyramine

substrate: tyramine


assay_conditions_summary: pH 8

proof_lines: hGDH1, pH 8.0, temperature not specified in the publication

proof_lines: hGDH2, pH 8.0, temperature not specified in the publication

proof_lines: hGDH2, pH 7.5, temperature not specified in the publication


substrate_name: D-Dopa

assay_conditions_summary: pH 8.3; 298.15 K; buffer 50 mM sodium diphosphate

proof_lines: in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C

substrate: D-Dopa


proof_lines:
isoform MAO B, at pH 7.4 and 37°C
isoform MAO A, at pH 7.4 and 37°C
pH 7.0, 37°C


enzyme_display_name: formyltetrahydrofolate dehydrogenase

enzyme: formyltetrahydrofolate dehydrogenase


substrate_name: pyridoxine 5'-phosphate

proof_lines:
mutant enzyme R95C, at pH 8.0 and 37°C
pH 7.6, 37°C, mutant enzyme R95C

substrate: pyridoxine 5'-phosphate


substrate_name: quinonoid 7,8-(6H)-dihydropterin

assay_conditions_summary: pH 7.2; 293.15 K; cofactor NADH

proof_lines:
at 20°C
recombinant enzyme
at 25°C

substrate: quinonoid 7,8-(6H)-dihydropterin


substrate_name: Unknown

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


substrate_name: glycine

proof_lines: pH 7.0, 25°C, recombinant individually expressed wild-type enzyme in presence of lipoic acid

proof_lines: pH 7.0, 25°C, recombinant individually expressed wild-type enzyme in presence of lipoylated H-protein

substrate: glycine


proof_lines:
recombinant enzyme
pH 7.4, 25°C
pH 7.3, 22.6°C


enzyme_display_name: flavin reductase (NADH)

organism: Lactobacillus johnsonii

substrate_name: FMN

assay_conditions_summary: pH 7; 310.15 K; cofactor NADH

enzyme: flavin reductase (NADH)

substrate: FMN


organism: Lathyrus oleraceus

smiles: C(C#CCN)N


substrate_name: tryptamine

substrate: tryptamine


organism: Mesocricetus auratus

substrate_name: Phenylethylamine

substrate: Phenylethylamine


organism: Methylorubrum extorquens


organism: Mycobacterium sp.

proof_lines:
dimeric enzyme
tetrameric enzyme


organism: Mus musculus

proof_lines:
pH 8.3, 37°C
at pH 8.3 and 37°C


substrate_name: D-Asp

substrate: D-Asp


organism: Mycobacterium tuberculosis

proof_lines: in 25 mM potassium phosphate, pH 7.8 and 25°C


substrate: Unknown


substrate_name: L-alanine

proof_lines: pH 6.4, 22°C, recombinant His6-tagged enzyme

proof_lines: pH and temperature not specified in the publication

substrate: L-alanine


substrate_name: L-Phe

substrate: L-Phe


organism: Ophiophagus hannah

substrate_name: L-leucine

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

substrate: L-leucine


organism: Oryctolagus cuniculus

proof_lines: with excess substrate, reaction cycle in combination with C1-tetrahydrofolate synthase, lower value than for dehydrogenase alone


organism: Papio sp.


organism: Plasmodium berghei

proof_lines:
trimethoprim-sensitive strain
trimethoprim-resistant sdtrain
trimethoprim-resistant strain


organism: Pneumocystis jirovecii

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


organism: Priestia megaterium


substrate_name: pyruvate

proof_lines: wild type enzyme, in 1 M NH4Cl/NH3, pH 7.4, at 25°C

substrate: pyruvate


organism: Rattus norvegicus

substrate_name: p-tyramine

substrate: p-tyramine


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


smiles: O=O

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM potassium phosphate assay

proof_lines: isoform MAO A, in 50 mM potassium phosphate assay buffer (pH 7.5), at 25°C


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: L-Lys

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

substrate: L-Lys


organism: Rhodococcus sp. AIU LAB-3


enzyme_display_name: saccharopine dehydrogenase (NAD+, L-lysine-forming)

organism: Saccharomyces cerevisiae

substrate_name: L-lysine

substrate: L-lysine


substrate_name: quinonoid dihydrobiopterin

proof_lines:
enzyme form III
enzyme form I
enzyme form II

substrate: quinonoid dihydrobiopterin


enzyme_display_name: glutamate synthase (NADH)

substrate_name: NADH

enzyme: glutamate synthase (NADH)

substrate: NADH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


assay_conditions_summary: cofactor FMN

substrate: FMN


substrate_name: Unknown


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Sus scrofa

substrate_name: cephalosporin C

substrate: cephalosporin C


proof_lines: apparent value, using D-glutamate as substrate

proof_lines: apparent value, using D-aspartate as substrate

proof_lines: apparent value, using N-methyl-D-aspartate as substrate


organism: Staphylococcus aureus

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


enzyme_display_name: diamine oxidase

substrate_name: histamine

proof_lines:
free enzyme
at pH 7.4
at pH 6.3

enzyme: diamine oxidase

substrate: histamine


enzyme_display_name: primary-amine oxidase

proof_lines:
vs. O2, deduced from slope
vs. benzylamine
vs. O2, deduced from intercept

enzyme: primary-amine oxidase


substrate_name: NADP+; H2O; 10-Formyltetrahydrofolate

proof_lines: (-)-isomer (+)-isomer

substrate: NADP+; H2O; 10-Formyltetrahydrofolate


assay_conditions_summary: pH 8.3; 298.15 K; cofactor FAD

proof_lines:
at pH 8.3 and 25°C
with D-alanine


proof_lines: mutant Y228L/F242I/R283G, pH not specified in the publication, temperature not specified in the publication


substrate_name: benzylamine

assay_conditions_summary: pH 9

proof_lines: enzyme from cultured aortic smooth muscle cells, Km decreases with increasing pH

substrate: benzylamine


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

enzyme: saccharopine dehydrogenase (NAD+, L-lysine-forming)


organism: Trypanosoma cruzi

substrate: Unknown


substrate_name: D-tryptophan

proof_lines:
immobilized enzyme
free enzyme

substrate: D-tryptophan


organism: Azospirillum brasilense

proof_lines: inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of wild type-beta subunit


organism: Escherichia coli

substrate_name: L-glutamine

substrate: L-glutamine


enzyme_display_name: diaminopimelate dehydrogenase

organism: Lysinibacillus sphaericus

proof_lines: competitive inhibition of L-2-amino-6-oxoheptanedioate

proof_lines: noncompetitive inhibition of meso-diaminopimelate

enzyme: diaminopimelate dehydrogenase


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

organism: Homo sapiens

substrate_name: NH3; NADH; 2-Oxoglutarate; H+

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

assay_conditions_summary: cofactor NAD+

enzyme: glutamate dehydrogenase [NAD(P)+]

substrate: NH3; NADH; 2-Oxoglutarate; H+


organism: Sulfitobacter sp.

substrate_name: NADPH; H+; 1-Pyrroline-2-carboxylate

substrate: NADPH; H+; 1-Pyrroline-2-carboxylate


substrate_name: NADP+; 5,10-Methylenetetrahydrofolate

substrate: NADP+; 5,10-Methylenetetrahydrofolate


enzyme_display_name: alanine dehydrogenase

organism: Thermus thermophilus

substrate_name: L-Ala

enzyme: alanine dehydrogenase

substrate: L-Ala


organism: Mesocricetus auratus

substrate_name: H2O; Serotonin; O2

substrate: H2O; Serotonin; O2


enzyme_display_name: putrescine oxidase

organism: Kocuria rosea

protein_accession_database: UniProt

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

enzyme: putrescine oxidase


substrate_name: tyramine

substrate: tyramine


substrate_name: cadaverine

substrate: cadaverine


organism: Lens culinaris


smiles: C(CBr)N


enzyme_display_name: polyvinyl-alcohol oxidase

organism: Stenotrophomonas rhizophila

substrate_name: polyvinyl alcohol

proof_lines: pH 7.2, 30°C, presence of pyrroloquinoline quinone

proof_lines: pH 7.2, 30°C, absence of pyrroloquinoline quinone

enzyme: polyvinyl-alcohol oxidase

substrate: polyvinyl alcohol


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

organism: Leishmania donovani

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


enzyme_display_name: phloroglucinol reductase

organism: Coprococcus sp.

substrate_name: phloroglucinol

enzyme: phloroglucinol reductase

substrate: phloroglucinol


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: dimethylamine dehydrogenase

organism: Hyphomicrobium sp.

substrate_name: Dimethylamine

smiles: CNC

enzyme: dimethylamine dehydrogenase

substrate: Dimethylamine


substrate_name: N,N,N,N-tetramethyl-o-phenylenediamine

substrate: N,N,N,N-tetramethyl-o-phenylenediamine


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


enzyme_display_name: sarcosine dehydrogenase

organism: Macaca mulatta

substrate_name: sarcosine

smiles: CNCC(=O)O

enzyme: sarcosine dehydrogenase

substrate: sarcosine


organism: Eubacterium oxidoreducens

substrate_name: NADP+

assay_conditions_summary: pH 7.2; cofactor NADP+

substrate: NADP+


substrate_name: dihydrophloroglucinol

substrate: dihydrophloroglucinol


enzyme_display_name: trimethylamine dehydrogenase

organism: methylotrophic bacterium

substrate_name: trimethylamine

smiles: CN(C)C

proof_lines: electron acceptor: phenazine methosulfate

enzyme: trimethylamine dehydrogenase

substrate: trimethylamine


substrate_name: ethyldimethylamine

smiles: CCN(C)C

substrate: ethyldimethylamine


smiles: CN(C)CCCl


smiles: CN(C)CCO


substrate_name: diethylmethylamine

smiles: CCN(C)CC

substrate: diethylmethylamine


smiles: CN(C)CCN


substrate_name: triethylamine

smiles: CCN(CC)CC

substrate: triethylamine


substrate_name: Diethylamine

smiles: CCNCC

substrate: Diethylamine


organism: Pseudomonas putida


substrate_name: potassium ferricyanide

substrate: potassium ferricyanide


substrate_name: N-Methylalanine

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

substrate: N-Methylalanine


substrate_name: N-methyl-L-valine

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

substrate: N-methyl-L-valine


substrate_name: N-Methyl-L-leucine

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

substrate: N-Methyl-L-leucine


enzyme_display_name: Polyvinylalcohol dehydrogenase

substrate_name: polyvinyl alcohol

source_db: oed

kcat_over_km_origin: calculated

smiles: C=CO

enzyme: Polyvinylalcohol dehydrogenase

substrate: polyvinyl alcohol

source: oed


enzyme_display_name: proline dehydrogenase

organism: Pyrobaculum calidifontis

substrate_name: L-hydroxyproline

assay_conditions_summary: pH 8; 323.15 K; buffer 200 mM Tris-HCl

proof_lines: in 200 mM Tris-HCl buffer (pH 8.0), at 50°C

enzyme: proline dehydrogenase

substrate: L-hydroxyproline


substrate_name: L-proline

substrate: L-proline


proof_lines: with L-hydroxyproline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C

proof_lines: with L-proline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C


organism: Clostridium formicaceticum

substrate_name: benzyl viologen

substrate: benzyl viologen


organism: Neomoorella thermoacetica

proof_lines: pH 7.5, 45°C, recombinant enzyme, with 5-methyltetrahydrofolate


proof_lines: pH 7.5, 45°C, recombinant enzyme, with benzyl viologen


enzyme_display_name: dimethylglycine dehydrogenase

organism: Chromohalobacter israelensis

enzyme: dimethylglycine dehydrogenase


substrate_name: N,N-dimethylglycine

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

substrate: N,N-dimethylglycine


organism: Pyrococcus furiosus

proof_lines: PF1246 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: PF1798 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C


organism: Thermococcus kodakarensis

proof_lines: TK0117 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: TK0122 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C


organism: Pyrococcus horikoshii

proof_lines: pH and temperature not specified in the publication

proof_lines: PF1364 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: PH1751 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C


organism: Thermococcus profundus

proof_lines: TPpdhB2 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: TPpdhB (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C


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


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


organism: Sinorhizobium meliloti

substrate_name: sarcosine

substrate: sarcosine


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


organism: Methylophilus methylotrophus

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.

proof_lines: mutant Y442G, electron acceptor: electron transferring flavoprotein


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

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


substrate_name: trimethylamine

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

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

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

substrate: trimethylamine


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

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

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)


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


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


organism: Methanopyrus kandleri

substrate_name: methylenetetrahydromethanopterin

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


organism: Deinococcus radiodurans

substrate_name: L-proline

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)


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


substrate: L-proline


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


substrate_name: oxidized coenzyme F420

substrate: oxidized coenzyme F420


substrate_name: 5,10-Methylenetetrahydromethanopterin; Reduced coenzyme F420


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

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


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: 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


organism: Chromohalobacter israelensis

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


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


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

substrate: L-proline


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

substrate: N-methyl L-alanine


substrate_name: N-methyl D-alanine

substrate: N-methyl D-alanine


substrate_name: sarcosine

smiles: CNCC(=O)O

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

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.