enzyme_display_name: Aldo-keto reductase family 1 member B1

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: Aldo-keto reductase family 1 member B1


enzyme_display_name: Aldo-keto reductase family 1 member B10

organism: Homo sapiens

substrate_name: GS-acrolein

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as

enzyme: Aldo-keto reductase family 1 member B10

substrate: GS-acrolein

status: unverified

source: uniprot


enzyme_display_name: Retinol dehydrogenase 13

substrate_name: Unknown

km_display: Not reported

enzyme: Retinol dehydrogenase 13

substrate: Unknown


enzyme_display_name: Retinol dehydrogenase 11

proof_lines: Vmax is measured per mg microsomal protein.

enzyme: Retinol dehydrogenase 11


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Sus scrofa

substrate_name: R-(+)-1-Phenyl-1-butanol (at pH7.4)

proof_lines: kcat is 45 min(-1) with all-trans-Retinal as substrate (at pH7.4) (PubMed:12604222). kcat is 990 min(-1) with isatin as substrate (at pH6) (PubMed:12604222). kcat is 1180 min(-1) with 1-phenyl-1,2-propanedione as substrate (at pH6) (PubMed:

substrate: R-(+)-1-Phenyl-1-butanol (at pH7.4)


organism: Oryctolagus cuniculus

proof_lines: kcat is 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4).

enzyme: Dehydrogenase/reductase SDR family member 4


enzyme_display_name: D-arabitol-phosphate dehydrogenase

organism: Enterococcus avium

substrate_name: Xlu5P (with NAD at 20 degrees Celsius and at pH 7.2)

enzyme: D-arabitol-phosphate dehydrogenase


enzyme_display_name: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

organism: Escherichia coli

substrate_name: UDPglucuronate; NAD+

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

assay_conditions_summary: cofactor NAD+

substrate: UDPglucuronate; NAD+


organism: Mycobacterium smegmatis

substrate_name: Mycothiol; Formaldehyde; NAD+

substrate: Mycothiol; Formaldehyde; NAD+


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Sungouiella intermedia

source_db: brenda

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

enzyme: D-xylose reductase [NAD(P)H]

source: brenda


organism: Yamadazyma tenuis

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines:
pH 7, 25°C
pH 7, 25°C, variable substrate: NADH


organism: Rasamsonia emersonii

substrate_name: D-xylose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K271R/N273D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: pH 6.5, 37°C, cosubstrate: NADH, mutant enzyme K271R/N273D

proof_lines: pH 6.5, 37°C, cosubstrate: NADPH, mutant enzyme K271R/N273D

data_origin: experimental

substrate: D-xylose


organism: Scheffersomyces stipitis

substrate_name: NAD(P)+

ki_unit: mM

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

assay_conditions_summary: cofactor NADPH

proof_lines:
concentration of NADH varied
concentration of NADPH varied
concentration of D-xylose varied

substrate: NAD(P)+


assay_conditions_summary: cofactor NADH

proof_lines:
concentration of NADH varied
concentration of D-xylose varied


substrate_name: cyclohexanecarboxaldehyde

substrate: cyclohexanecarboxaldehyde


substrate_name: NADH

source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K271R to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH

substrate: NADH

source: oed


substrate_name: NADPH

kcat_over_km_origin: calculated

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADPH

substrate: NADPH


verification_status: corrected

column_label: Table 2 (kinetic parameters for xylose reduction), body row 'TeXR wild type'; column 'NADPH Km [mM]' = 0.244; column 'kcat [s-1]' = 323974.10; column 'kcat/Km [mM-1.s-1]' = 1466242.00. The two 'Km xylose' columns of the same body row carry the xylose affinities and belong to the D-xylose substrate, not to this coenzyme block.

normalized_value_unit_evidence: Km: printed cell 0.244 mM; the printed unit is already the canonical mM, so no unit conversion applies; canonical value 0.244 mM. kcat: printed cell 323974.10 s^-1; the printed unit is already the canonical s^-1, so no unit conversion applies; canonical value 323974.1 s^(-1). kcat/Km: printed cell 1466242.00 mM^-1 s^-1; mM^-1 s^-1 is the canonical unit s^(-1)*mM^(-1), so no unit conversion applies; canonical value 1466242.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, wild-type enzyme row, NADPH coenzyme block: column 'NADPH Km [mM]' = 0.244; column 'kcat [s-1]' = 323974.10; printed catalytic-efficiency column 'kcat/Km [mM-1.s-1]' = 1466242.00.

table_label: Table 2 (kinetic parameters for xylose reduction by the wild-type and the double-substitution protein expressed in E. coli), J. Biosci. 34(6), December 2009, journal page 886

status: corrected


enzyme_display_name: NADPH-dependent D-xylose reductase

organism: Candida boidinii

proof_lines: Mutations at positions 272 to 274 modify the cofactor specificity and increase specificity for NADH over NADPH.

enzyme: NADPH-dependent D-xylose reductase


enzyme_display_name: Sulfopropanediol 3-dehydrogenase

organism: Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197)

enzyme: Sulfopropanediol 3-dehydrogenase


enzyme_display_name: (S)-1-phenylethanol dehydrogenase

organism: Aromatoleum aromaticum EbN1

substrate_name: NAD+; (S)-1-Phenylethanol

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

enzyme: (S)-1-phenylethanol dehydrogenase

substrate: NAD+; (S)-1-Phenylethanol


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: CHMS (with NADP as cofactor at 25 degrees Celsius and pH 8)

assay_conditions_summary: pH 8


enzyme_display_name: 11-cis-retinol dehydrogenase

substrate_name: 11-cis-retinol-[cellular retinaldehyde binding protein]

proof_lines: wild-type cellular retinaldehyde binding protein, recombinant wild-type RDH5, pH 7.5, temperature not specified in the publication

enzyme: 11-cis-retinol dehydrogenase


enzyme_display_name: Retinol dehydrogenase 16

substrate_name: CRBP-all-trans-retinol

enzyme: Retinol dehydrogenase 16

substrate: CRBP-all-trans-retinol


enzyme_display_name: Retinol dehydrogenase 5

organism: Bos taurus

enzyme: Retinol dehydrogenase 5


enzyme_display_name: Perakine reductase

organism: Rauvolfia serpentina

enzyme: Perakine reductase


enzyme_display_name: Eugenol synthase 1

organism: Ocimum basilicum

enzyme: Eugenol synthase 1


organism: Clarkia breweri

proof_lines: kcat is 0.26 sec(-1) with coniferyl acetate as substrate.


enzyme_display_name: Eugenol synthase 2

proof_lines: kcat is 0.25 sec(-1) with coniferyl acetate as substrate.

enzyme: Eugenol synthase 2


organism: Petunia hybrida

proof_lines: kcat is 0.60 sec(-1) with coniferyl acetate as substrate.


enzyme_display_name: Isoeugenol synthase 1

proof_lines: kcat is 1.3 sec(-1) with coniferyl acetate as substrate.

enzyme: Isoeugenol synthase 1


proof_lines: kcat is 0.99 sec(-1) with coniferyl acetate as substrate.


enzyme_display_name: Benzil reductase ((S)-benzoin forming)

organism: Bacillus cereus

substrate_name: 1-(4-fluoro-phenyl)-2-phenyl-ethane-1,2-dione (with NADPH at 37 degrees Celsius and pH 6.5)

proof_lines: kcat is 64.4 min(-1) with benzil as substrate. kcat is 165 min(-1) with 1-phenyl-1,2-propanedione as substrate. kcat is 7.4 min(-1) with 1,4-naphthoquinone as substrate. kcat is 1.2 min(-1) with p-nitrobenzaldehyde as substrate. kcat is 31.

enzyme: Benzil reductase ((S)-benzoin forming)


organism: Chlorobaculum tepidum

sequence_source: multiple

proof_lines: For the reverse reaction, accepts L-threo-dihydrobiopterin, D-threo-dihydrobiopterin, L-threo-dihydroneopterin, dihydrotepidopterin and L-erythro-dihydrobiopterin as substrates.

source_databases_merged: brenda uniprot


enzyme_display_name: nicotine blue oxidoreductase

organism: Arthrobacter nicotinovorans

substrate_name: Nicotine blue; H+; NADH

enzyme: nicotine blue oxidoreductase

substrate: Nicotine blue; H+; NADH


enzyme_display_name: chanoclavine-I dehydrogenase

organism: Aspergillus fumigatus

substrate_name: NAD+; Chanoclavine-I

enzyme: chanoclavine-I dehydrogenase

substrate: NAD+; Chanoclavine-I


enzyme_display_name: methylecgonone reductase

organism: Erythroxylum coca

substrate_name: NADPH; Ecgonone methyl ester; H+

assay_conditions_summary: pH 6.8; cofactor NADPH

proof_lines: substrate inhibition, pH 6.8, temperature not specified in the publication

enzyme: methylecgonone reductase

substrate: NADPH; Ecgonone methyl ester; H+


enzyme_display_name: UniProt Q7NQL0

organism: Chromobacterium violaceum

source_db: skid

verification_status: verified

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q7NQL0

status: verified

source: skid


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: Unknown


organism: Escherichia coli

substrate_name: NAD+; UDP-N-acetyl-D-mannosamine; H2O

substrate: NAD+; UDP-N-acetyl-D-mannosamine; H2O


organism: Methanococcus maripaludis

substrate_name: NAD+; H2O; UDP-N-acetyl-D-mannosamine

substrate: NAD+; H2O; UDP-N-acetyl-D-mannosamine


organism: Methanocaldococcus jannaschii

substrate_name: oxopropandioic acid

assay_conditions_summary: pH 8; 343.15 K; cofactor NADH

proof_lines:
pH 8.0, 70°C
cosubstrate NADH, pH 8.0, 70°C

substrate: oxopropandioic acid


organism: Weissella confusa

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


organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

substrate_name: 1-deoxy-11-beta-hydroxypentalenic acid

substrate: 1-deoxy-11-beta-hydroxypentalenic acid


enzyme_display_name: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating

organism: Gluconobacter oxydans (strain 621H)

proof_lines: kcat is 23 sec(-1). Can use NAD or NADP, but has a clear preference for NAD in vivo.

substrate: Unknown


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

proof_lines: The catalytic efficiency with NAD(+) is about 2000-fold higher than with NADP(+), indicating that NAD(+) is the physiological electron acceptor.

enzyme: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating


enzyme_display_name: GDP-L-colitose synthase

organism: Yersinia pseudotuberculosis

substrate_name: GDP-4-keto-3,6-dideoxy-D-mannose (with NADP at pH 7.5 and 37 degrees Celsius)

enzyme: GDP-L-colitose synthase


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Homo sapiens

substrate_name: Androstanediol; NAD+

proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase

substrate: Androstanediol; NAD+


substrate_name: NADPH; 5alpha-Pregnane-3,20-dione; H+

proof_lines: kcat is 1.99 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction. kcat is 1.79 min(-1) for 5alpha-androstan-3,17-dione reduction. kcat is 2.1 min(-1) for 5alpha-androstane-3alpha,17beta-diol oxydation. kcat is 1.39.1 min(-1) for 3al

substrate: NADPH; 5alpha-Pregnane-3,20-dione; H+


proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.3


substrate_name: Pregnanediol; NADP+

assay_conditions_summary: cofactor NADP+

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

substrate: Pregnanediol; NADP+


enzyme_display_name: Aldo-keto reductase family 1 member C4

organism: Macaca fuscata fuscata

proof_lines: kcat is 4.9 min(-1) for 5-beta-pregnan-20-alpha-ol-3-one as substrate. kcat is 4.9 min(-1) for 3alpha-hydroxy-5alpha-androstan-17-one as substrate. kcat is 23 min(-1) for 5alpha-pregnane-3alpha,21-diol-20-one.

enzyme: Aldo-keto reductase family 1 member C4


enzyme_display_name: NADPH-dependent conjugated polyketone reductase C2

organism: Candida parapsilosis


enzyme_display_name: aldose 1-dehydrogenase [NAD(P)+]

organism: Saccharolobus solfataricus

substrate_name: D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 8)

enzyme: aldose 1-dehydrogenase [NAD(P)+]


organism: Pseudomonas aeruginosa

substrate_name: Glucose 6-phosphate; NADP+

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

substrate: Glucose 6-phosphate; NADP+


organism: Leuconostoc mesenteroides

substrate_name: thionicotinamide-NADP+

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADP+

proof_lines: 25°C, pH 7.2, cosubstrate: D-glucose 6-phosphate

substrate: thionicotinamide-NADP+


enzyme_display_name: D-galacturonate reductase

organism: Trichoderma reesei

substrate_name: D-Galacturonate; H+; NADPH

enzyme: D-galacturonate reductase

substrate: D-Galacturonate; H+; NADPH


enzyme_display_name: L-idonate 5-dehydrogenase

organism: Vitis vinifera

substrate_name: L-idonate in the forward reaction

enzyme: L-idonate 5-dehydrogenase

substrate: L-idonate in the forward reaction


organism: Thauera aromatica


enzyme_display_name: D-chiro-inositol 1-dehydrogenase

organism: Bacillus subtilis

substrate_name: D-chiro-Inositol; NAD+

enzyme: D-chiro-inositol 1-dehydrogenase

substrate: D-chiro-Inositol; NAD+


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NAD+)

organism: Paracoccus laeviglucosivorans

substrate_name: NAD+; L-Glucose

enzyme: scyllo-inositol 2-dehydrogenase (NAD+)

substrate: NAD+; L-Glucose


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NADP(+)) IolW

organism: Bacillus subtilis (strain 168)


enzyme_display_name: D/L-glyceraldehyde reductase

substrate_name: H+; NADPH; Glyceraldehyde

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: D/L-glyceraldehyde reductase

substrate: H+; NADPH; Glyceraldehyde


enzyme_display_name: Aldo-keto reductase family 1 member A1

substrate_name: Unknown

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 959 min(-1) for S-nitroso-CoA as substrate (PubMed:30538128). kcat is 604 min(-1) for D-glucuronate as substrate (PubMed:30538128). kcat is 306 min(-1) for D,L-glyceraldehyde as substrate (PubMed:30538128). kcat is 948 min(-1) for S

enzyme: Aldo-keto reductase family 1 member A1


enzyme_display_name: 3-sulfolactaldehyde reductase

organism: Escherichia coli (strain K12)

substrate_name: 3-hydroxypropane sulfonate

proof_lines: kcat is 332 sec(-1) with 3-sulfolactaldehyde as substrate. kcat is 548 sec(-1) with NADH as substrate.

enzyme: 3-sulfolactaldehyde reductase

substrate: 3-hydroxypropane sulfonate


enzyme_display_name: UDP-N-acetylglucosamine 3-dehydrogenase

organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)

proof_lines: kcat is 0.9 sec(-) with UDP-GalNAc. kcat is 0.99 sec(-1) with NAD(+).

enzyme: UDP-N-acetylglucosamine 3-dehydrogenase


enzyme_display_name: L-malate dehydrogenase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: (S)-malate (in the presence of NAD(+))

proof_lines: kcat is 0.33 sec(-1) for the oxidation of (S)-malate with NAD(+). kcat is 0.069 sec(-1) for the oxidation of (S)-malate with NADP(+). kcat is 0.2 sec(-1) for the oxidation of (2S,3S)-tartrate with NAD(+). kcat is 0.15 sec(-1) for the oxidat

enzyme: L-malate dehydrogenase

substrate: (S)-malate (in the presence of NAD(+))


enzyme_display_name: L-arabinose 1-dehydrogenase [NAD(P)+]

organism: Azospirillum brasilense

substrate_name: L-Arabinose; NAD+

enzyme: L-arabinose 1-dehydrogenase [NAD(P)+]

substrate: L-Arabinose; NAD+


enzyme_display_name: L-rhamnose 1-dehydrogenase (NAD(P)(+))

organism: Azotobacter vinelandii (strain DJ / ATCC BAA-1303)

substrate_name: L-rhamnose (in the presence of NAD(+))

proof_lines: kcat is 2230 min(-1) with L-rhamnose as substrate (in the presence of NAD(+)) (PubMed:18505728). kcat is 4490 min(-1) with L-rhamnose as substrate (in the presence of NADP(+)) (PubMed:18505728). kcat is 5010 min(-1) with L-rhamnose as subst

enzyme: L-rhamnose 1-dehydrogenase (NAD(P)(+))

substrate: L-rhamnose (in the presence of NAD(+))


enzyme_display_name: 3-hydroxy acid dehydrogenase

organism: Saccharomyces cerevisiae

proof_lines: The highest catalytic efficiency was observed with L-allo-threonine.

enzyme: 3-hydroxy acid dehydrogenase


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase YdfG

substrate_name: L-3-hydroxyisobutyrate (at pH 9 and at 30 degrees Celsius)

assay_conditions_summary: pH 9


enzyme_display_name: ketol-acid reductoisomerase [NAD(P)+]

organism: Ignisphaera aggregans

substrate_name: (S)-2-Acetolactate; H+; NADPH

enzyme: ketol-acid reductoisomerase [NAD(P)+]

substrate: (S)-2-Acetolactate; H+; NADPH


enzyme_display_name: Ketol-acid reductoisomerase (NAD(P)(+))

organism: Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1)

substrate_name: S2AL (at pH 7 and 85 degrees Celsius)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: kcat is 3.3 sec(-1) for reductoisomerase activity with NADPH (at pH 7 and 85 degrees Celsius with S2AL as substrate) (PubMed:26644020). kcat is 0.03 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate) (PubMed:2

enzyme: Ketol-acid reductoisomerase (NAD(P)(+))

substrate: S2AL (at pH 7 and 85 degrees Celsius)


organism: Actinomadura kijaniata

proof_lines: kcat is 6.24 sec(-1) for dTDP-glucose as substrate.

substrate: Unknown


enzyme_display_name: ipsdienol dehydrogenase

organism: Ips pini

substrate_name: (4R)-Ipsdienol; NADP+

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

source_databases_merged: sabio_rk brenda uniprot

enzyme: ipsdienol dehydrogenase

substrate: (4R)-Ipsdienol; NADP+


enzyme_display_name: L-serine 3-dehydrogenase (NAD+)

organism: Pseudomonas aeruginosa

substrate_name: L-Serine; NAD+

assay_conditions_summary: cofactor NAD+

proof_lines: kcat is 10.4 sec(-1) with L-serine as substrate. kcat is 9.6 sec(-1) with methyl-DL-serine as substrate. kcat is 5.8 sec(-1) with DL-glycerate as substrate. kcat is 11.6 sec(-1) with methyl-2,2-dimethyl-3-hydroxypropionate as substrate. kca

enzyme: L-serine 3-dehydrogenase (NAD+)

substrate: L-Serine; NAD+


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

proof_lines: The catalytic efficiency with NAD(+) is about 230-fold higher than with NADP(+), indicating that NAD(+) is the physiological electron acceptor.


enzyme_display_name: Sulfoquinovose 1-dehydrogenase

organism: Pseudomonas putida

proof_lines: kcat is 33.8 sec(-1) for sulfoquinovose oxidation with NAD(+). kcat is 1.4 sec(-1) for sulfoquinovose oxidation with NADP(+).

enzyme: Sulfoquinovose 1-dehydrogenase


organism: Rhodococcus sp. (strain AD45)


enzyme_display_name: 2-oxoglutarate reductase

organism: Homo sapiens

substrate_name: 2-Oxoglutarate; H+; NADH

proof_lines: kcat is 4.5 min(-1) for 3-phosphoglycerate oxidation. kcat is 10.6 min(-1) for oxaloacetate reduction. kcat is 4.7 min(-1) for 2-oxoglutarate reduction.

enzyme: 2-oxoglutarate reductase

substrate: 2-Oxoglutarate; H+; NADH


organism: Escherichia coli

substrate_name: NAD+; (R)-2-Hydroxyglutarate

proof_lines: kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25

substrate: NAD+; (R)-2-Hydroxyglutarate


organism: Sphingomonas sp.

proof_lines: kcat is 51.8 min(-1) with 2-dehydro-3-deoxy-L-rhamnonate as substrate. kcat is 11 min(-1) with 2-dehydro-3-deoxy-L-lyxonate as substrate. kcat is 0.72 min(-1) with 2-dehydro-3-deoxy-L-mannonate as substrate.


organism: Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1)


enzyme_display_name: tetrachlorobenzoquinone reductase

organism: Sphingobium chlorophenolicum

substrate_name: cytochrome c

assay_conditions_summary: pH 7.6; 295.15 K; cofactor NADH

proof_lines: kcat is 20.1 sec(-1) for NADH as substrate (with 90 uM cytochrome c). kcat is 14.1 sec(-1) for 2,6-dichloroindophenol (DCIP) as substrate (with 100 uM NADH). kcat is 9.1 sec(-1) for cytochrome c as substrate (with 100 uM NADH). kcat is 3.7

enzyme: tetrachlorobenzoquinone reductase

substrate: cytochrome c


organism: Haemophilus influenzae

substrate_name: NADPH; H+; D-Ribulose 5-phosphate

substrate: NADPH; H+; D-Ribulose 5-phosphate


enzyme_display_name: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Acs1


enzyme_display_name: 4-phospho-D-threonate 3-dehydrogenase

organism: Cupriavidus necator

substrate_name: 4-hydroxy-L-threonine 4-phosphate

proof_lines: kcat is 3.4 sec(-1) with D-threonate 4-phosphate as substrate. kcat is 0.35 sec(-1) with 4-hydroxy-L-threonine 4-phosphate as substrate.

enzyme: 4-phospho-D-threonate 3-dehydrogenase

substrate: 4-hydroxy-L-threonine 4-phosphate


enzyme_display_name: D-threonate 4-phosphate dehydrogenase

organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: D-threonate 4-phosphate

proof_lines: kcat is 8.9 sec(-1) with D-threonate 4-phosphate as substrate. kcat is 0.37 sec(-1) with 4-hydroxy-L-threonine 4-phosphate as substrate (PubMed:27402745). kcat is 0.06 sec(-1) with 4-hydroxy-L-threonine 4-phosphate as substrate (PubMed:2729

enzyme: D-threonate 4-phosphate dehydrogenase

substrate: D-threonate 4-phosphate


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

proof_lines: kcat is 6.9 sec(-1) with D-threonate 4-phosphate as substrate. kcat is 2.2 sec(-1) with 4-hydroxy-L-threonine 4-phosphate as substrate.


organism: Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)

proof_lines: kcat is 8.6 sec(-1) with D-threonate 4-phosphate as substrate. kcat is 2.9 sec(-1) with 4-hydroxy-L-threonine 4-phosphate as substrate.


enzyme_display_name: D-erythronate 4-phosphate dehydrogenase

organism: Heliobacterium modesticaldum (strain ATCC 51547 / Ice1)

substrate_name: D-erythronate 4-phosphate

proof_lines: kcat is 2.1 sec(-1) with D-erythronate 4-phosphate as substrate. kcat is 0.024 sec(-1) with D-threonate 4-phosphate as substrate.

enzyme: D-erythronate 4-phosphate dehydrogenase

substrate: D-erythronate 4-phosphate


enzyme_display_name: 2-alkyl-3-oxoalkanoate reductase

organism: Stenotrophomonas maltophilia (strain K279a)

substrate_name: syn-2-decyl-3-hydroxytetradecanoic acid

proof_lines: kcat is 122 min(-1) for syn-2-octyl-3-hydroxydodecanoic acid as substrate. kcat is 85 min(-1) for syn-2-decyl-3-hydroxytetradecanoic acid as substrate. kcat is 79 min(-1) for (2R,3S)-2-hexyl-3-hydroxydecanoic acid as substrate. kcat is 72 m

enzyme: 2-alkyl-3-oxoalkanoate reductase

substrate: syn-2-decyl-3-hydroxytetradecanoic acid


enzyme_display_name: A-factor type gamma-butyrolactone 1'-reductase (1S-forming)

organism: Streptomyces virginiae


organism: Escherichia coli (strain K12)

substrate_name: Unknown

proof_lines: kcat is 0.51 sec(-1) with L-galactonate.


enzyme_display_name: plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)

organism: Arabidopsis thaliana

proof_lines: isoform 3betaHSD/D2, at 30°C, pH not specified in the publication


proof_lines: isoform 3betaHSD/D1, at 30°C, pH not specified in the publication

enzyme: plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)


organism: Nepeta racemosa

substrate_name: cis-trans-nepetalactol (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius)

proof_lines: kcat is 0.148 sec(-1) with cis-trans-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius). kcat is 0.32 sec(-1) with cis-cis-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Cel


enzyme_display_name: D-apiose dehydrogenase

organism: Agrobacterium tumefaciens

substrate_name: NAD+; D-Apiose

enzyme: D-apiose dehydrogenase

substrate: NAD+; D-Apiose


organism: Paraburkholderia graminis

substrate_name: D-Apiose; NAD+

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Supplementary Table 4. Kinetic parameters for D-apiose dehydrogenase; row/segment B1G894/BgramDRAFT_5562; D-Apiose; column/metric kcat (s-1) and KM (mM)

raw_value_unit_evidence: Supplementary Table 4 reports kcat 12 +/- 0.3 s-1 and KM 0.11 +/- 0.01 mM for B1G894/BgramDRAFT_5562 with D-apiose.

row_label: B1G894/BgramDRAFT_5562; D-Apiose

substrate: D-Apiose; NAD+


enzyme_display_name: D-apionate oxidoisomerase

substrate_name: NAD+; D-Apionate

enzyme: D-apionate oxidoisomerase

substrate: NAD+; D-Apionate


substrate_name: D-Apionate; NAD+

substrate: D-Apionate; NAD+


organism: Pectobacterium atrosepticum


organism: Blautia hydrogenotrophica


enzyme_display_name: Sulfoacetaldehyde reductase

organism: Bilophila wadsworthia (strain 3_1_6)

enzyme: Sulfoacetaldehyde reductase


enzyme_display_name: Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctC

organism: Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)

substrate_name: ferredoxin

substrate: ferredoxin


enzyme_display_name: Polyprenol dehydrogenase

organism: Homo sapiens

substrate_name: polyprenol (with 1 mM of NAD(+))

proof_lines: kcat is 0.44 sec(-1) with polyprenol in presence of NAD(+) (PubMed:38821050). kcat is 0.49 sec(-1) with polyprenol in presence of NADP(+) (PubMed:38821050).

enzyme: Polyprenol dehydrogenase

substrate: polyprenol (with 1 mM of NAD(+))


enzyme_display_name: (-)-trans-carveol dehydrogenase

organism: Rhodococcus erythropolis

enzyme: (-)-trans-carveol dehydrogenase

substrate: Unknown


enzyme_display_name: Succinic semialdehyde reductase

organism: Mus musculus

substrate_name: H+; NADPH; Succinate semialdehyde

smiles: O=CCCC(=O)O

assay_conditions_summary: cofactor NADPH

enzyme: Succinic semialdehyde reductase

substrate: H+; NADPH; Succinate semialdehyde


organism: Rattus norvegicus

substrate_name: Succinate semialdehyde; H+; NADPH

substrate: Succinate semialdehyde; H+; NADPH


substrate_name: NADPH; H+; Succinate semialdehyde

substrate: NADPH; H+; Succinate semialdehyde


substrate_name: H+; Succinate semialdehyde; NADPH

substrate: H+; Succinate semialdehyde; NADPH


enzyme_display_name: Aflatoxin B1 aldehyde reductase member 2


enzyme_display_name: (3R)-hydroxyacyl-CoA dehydrogenase

substrate_name: (R)-3-Hydroxyoctanoyl-CoA; NAD+

enzyme: (3R)-hydroxyacyl-CoA dehydrogenase

substrate: (R)-3-Hydroxyoctanoyl-CoA; NAD+


enzyme_display_name: Peroxisomal multifunctional enzyme type 2

organism: Drosophila melanogaster

proof_lines: Catalytic efficiency is similar using full-length protein or the individual (3R)-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase 2 domains in a 1:1 mixture.


enzyme_display_name: (3R)-3-hydroxyacyl-CoA dehydrogenase

enzyme: (3R)-3-hydroxyacyl-CoA dehydrogenase


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Saccharomyces cerevisiae

substrate_name: Hexacyanoferrate(III); L-Lactate

proof_lines: kcat is 207 sec(-1) with cytochrome c as electron acceptor. kcat is 400 sec(-1) with ferricyanide as electron acceptor.

enzyme: L-lactate dehydrogenase (cytochrome)

substrate: Hexacyanoferrate(III); L-Lactate


substrate_name: cytochrome c

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D72A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant D72A

substrate: cytochrome c


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K73A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant K73A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N69K with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant N69K


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E91K to reconstruct the assayed variant sequence.


enzyme_display_name: methanol dehydrogenase (cytochrome c)

organism: Methylacidiphilum fumariolicum

substrate_name: Methanol; Phenazine ethosulfate

enzyme: methanol dehydrogenase (cytochrome c)

substrate: Methanol; Phenazine ethosulfate


enzyme_display_name: alcohol dehydrogenase (cytochrome c)

substrate_name: Methanol; PQQ

smiles: CO

enzyme: alcohol dehydrogenase (cytochrome c)

substrate: Methanol; PQQ


organism: Pseudomonas putida

substrate_name: Ethanol; PQQ

smiles: CCO

column_label: Figure 3 panel D lists ethanol Vmax=6.1 +/- 0.3 U mg^-1, KM=85 +/- 18 uM, and kcat/KM=81 +/- 18 mM^-1 s^-1 for PedE.

normalized_value_unit_evidence: Vmax normalized_value=0.000101667 normalized_unit=kat g^-1 from 6.1 U mg^-1; KM normalized_value=0.085 normalized_unit=mM; kcat/KM normalized_value=81 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Vmax raw_value=6.1 +/- 0.3 raw_unit=U mg^-1; KM raw_value=85 +/- 18 raw_unit=uM; kcat/KM raw_value=81 +/- 18 raw_unit=mM^-1 s^-1

row_label: PedE, ethanol

table_label: Figure 3, panel D: Kinetic constants of PedE

substrate: Ethanol; PQQ


substrate_name: PQQ; Phenylethyl alcohol

substrate: PQQ; Phenylethyl alcohol


enzyme_display_name: Quinoprotein ethanol dehydrogenase

substrate_name: Unknown

enzyme: Quinoprotein ethanol dehydrogenase


organism: Methylorubrum extorquens

substrate_name: oxidized cytochrome cL

proof_lines: in the presence of La3+, at pH 7.0 and 30°C

proof_lines: in the presence of Ce3+, at pH 7.0 and 30°C

proof_lines: La-XoxF, pH 7.0, 30°C, determined using the XoxG/cyt c-linked activity

substrate: oxidized cytochrome cL


enzyme_display_name: Lanthanide-dependent methanol dehydrogenase XoxF

organism: Methylotuvimicrobium buryatense


organism: Methylacidiphilum fumariolicum (strain SolV)

substrate_name: methanol (in the presence of a mixture of La(3+), Ce(3+) and Pr(3+))

proof_lines: kcat is 0.20 sec(-1) for the Eu(3+)-dependent oxidation of methanol using artificial electron acceptor.


enzyme_display_name: UniProt Q44467

organism: Aerococcus viridans

substrate_name: L-alpha-hydroxy-beta-methylvalerate

enzyme: UniProt Q44467

substrate: L-alpha-hydroxy-beta-methylvalerate


enzyme_display_name: glucose oxidase

organism: Aspergillus niger

substrate_name: beta-D-Glucose; Acceptor

enzyme: glucose oxidase

substrate: beta-D-Glucose; Acceptor


organism: Penicillium amagasakiense

substrate_name: beta-D-Glucose; O2

proof_lines: recombinant enzyme yGOXpenag, pH 6.0, 50°C

substrate: beta-D-Glucose; O2


organism: Penicillium adametzii

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: Glucose oxidase

organism: Penicillium chrysogenum

substrate_name: D-gludose

enzyme: Glucose oxidase

substrate: D-gludose


enzyme_display_name: aryl-alcohol oxidase

organism: Pleurotus eryngii

substrate_name: Benzyl alcohol; O2

enzyme: aryl-alcohol oxidase

substrate: Benzyl alcohol; O2


organism: Pleurotus pulmonarius

substrate_name: 4-anisyl alcohol

proof_lines:
Pleurotus pulmonarius
aryl-alcohol oxidase
p-anisyl alcohol

substrate: 4-anisyl alcohol


enzyme_display_name: galactose oxidase

organism: Gibberella zeae

substrate_name: D-Galactose; O2

enzyme: galactose oxidase

substrate: D-Galactose; O2


organism: Fusarium sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y436H with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines:
mutant Y436H/v494A, pH 7.0, 25°C
mutant Y436H, pH 7.0, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y436A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y436A/V494A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


organism: Fusarium subglutinans

substrate_name: D-galactose

substrate: D-galactose


enzyme_display_name: pyranose oxidase

organism: Phlebiopsis gigantea

substrate_name: beta-Methyl-D-glucopyranoside; O2

enzyme: pyranose oxidase

substrate: beta-Methyl-D-glucopyranoside; O2


organism: Trametes ochracea

substrate_name: O2; D-Glucose

proof_lines:
pH 6.5, substrate: D-glucose
pH 6.5, 30°C

substrate: O2; D-Glucose


organism: Phanerochaete chrysosporium

substrate_name: D-Glucose; O2

proof_lines: substrate 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) cation radical (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled

substrate: D-Glucose; O2


substrate_name: ferricenium ion

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E542K to reconstruct the assayed variant sequence.

proof_lines: E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

substrate: ferricenium ion


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537G/E542R to reconstruct the assayed variant sequence.

proof_lines: L537G/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3

proof_lines: mutant enzyme L537G/E542R, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E542R to reconstruct the assayed variant sequence.

proof_lines: E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537G/E542K to reconstruct the assayed variant sequence.

proof_lines: L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537G/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3

proof_lines: mutant enzyme L537G/E542K, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537W/E542R to reconstruct the assayed variant sequence.

proof_lines: L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537W/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3

proof_lines: mutant enzyme L537W/E542R, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537W/E542K to reconstruct the assayed variant sequence.

proof_lines: L537W/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3

proof_lines: mutant enzyme L537W/E542K, at pH 6.5 and 30°C


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

proof_lines: wild-type, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: wild-type, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537G to reconstruct the assayed variant sequence.

proof_lines: L537G mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537W to reconstruct the assayed variant sequence.

proof_lines: L537W mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


organism: Lyophyllum shimeji

substrate_name: ferrocenium ion

proof_lines: using D-glucose as cosubstrate, at 30°C, pH 6.5

substrate: ferrocenium ion


substrate_name: methyl-beta-D-glucoside

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K312E to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag

substrate: methyl-beta-D-glucoside


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E540K to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag


enzyme_display_name: Pyranose 2-oxidase

organism: Trametes pubescens

substrate_name: Unknown

enzyme: Pyranose 2-oxidase

substrate: Unknown


organism: Tricholoma matsutake


enzyme_display_name: (S)-2-hydroxy-acid oxidase

organism: Rattus norvegicus

substrate_name: O2; L-Leucine

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

proof_lines: kcat is 0.99 sec(-1) for the oxidation of L-2-hydroxyoctanoate with DCIP instead of O2 as electron acceptor. kcat is 0.34 sec(-1) for the oxidation of L-2-hydroxyhexadecanoate with DCIP instead of O2 as electron acceptor (PubMed:15683236).

source_databases_merged: sabio_rk skid uniprot

enzyme: (S)-2-hydroxy-acid oxidase

substrate: O2; L-Leucine


organism: Homo sapiens

substrate_name: Glycolate; Acceptor

proof_lines: kcat is 3.6 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 4.1 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.5 and 37 degr

substrate: Glycolate; Acceptor


organism: Escherichia coli

substrate_name: (S)-2-Hydroxyglutarate; O2

substrate: (S)-2-Hydroxyglutarate; O2


organism: Oryza sativa

substrate_name: O2; Glycolate

substrate: O2; Glycolate


enzyme_display_name: Glycolate oxidase 2

organism: Arabidopsis thaliana

proof_lines: kcat is 30.10 sec(-1) with glycolate as substrate (at pH 8 and 30 degrees Celsius).

enzyme: Glycolate oxidase 2


enzyme_display_name: Glycolate oxidase

organism: Spinacia oleracea

proof_lines: kcat is 20 sec(-1) with glycolate as substrate. kcat is 11 sec(-1) with L-lactate as substrate. kcat is 13.2 sec(-1) with L-2-hydroxbyutanoate as substrate. kcat is 0.09 sec(-1) with L-mandelate as substrate.

enzyme: Glycolate oxidase


enzyme_display_name: Ecdysone oxidase

organism: Spodoptera littoralis

enzyme: Ecdysone oxidase


enzyme_display_name: choline oxidase

organism: Arthrobacter globiformis

substrate_name: Choline; O2

enzyme: choline oxidase

substrate: Choline; O2


enzyme_display_name: Choline oxidase

organism: Alcaligenes sp

sequence: DNPNHSR

wild_type_sequence: DNPNHSR

enzyme: Choline oxidase


enzyme_display_name: long-chain-alcohol oxidase

organism: Lotus japonicus

substrate_name: O2; 1-Dodecanol

smiles: CCCCCCCCCCCCO

enzyme: long-chain-alcohol oxidase

substrate: O2; 1-Dodecanol


substrate_name: 1-Dodecanol; O2

substrate: 1-Dodecanol; O2


enzyme_display_name: glycerol-3-phosphate oxidase

organism: Enterococcus casseliflavus

substrate_name: O2; sn-Glycerol 3-phosphate

enzyme: glycerol-3-phosphate oxidase

substrate: O2; sn-Glycerol 3-phosphate


organism: Mycoplasma pneumoniae

assay_conditions_summary: pH 7

proof_lines: kcat is 4.2 sec(-1) with sn-glycerol 3-phosphate as substrate (at pH 7 and 4 degrees Celsius). kcat is 60.1 sec(-1) with sn-glycerol 3-phosphate as substrate (at pH 7 and 25 degrees Celsius). kcat is 0.6 sec(-1) with sn-glycerol 3-phosphate


enzyme_display_name: vanillyl-alcohol oxidase

organism: Penicillium simplicissimum

substrate_name: O2; 4-Hydroxy-3-methoxy-benzenemethanol

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=10
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: sabio_rk brenda skid

enzyme: vanillyl-alcohol oxidase

substrate: O2; 4-Hydroxy-3-methoxy-benzenemethanol


proof_lines:
pH 10, 25°C, wild-type enzyme
pH 7.5, 25°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F454Y with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines:
pH 10, 25°C, mutant enzyme F454Y
pH 7.5, 25°C, mutant enzyme F454Y


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E502G with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 25°C, mutant enzyme E502G
pH 10, 25°C, mutant enzyme E502G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I238T with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines:
pH 10, 25°C, mutant enzyme I238T
pH 7.5, 25°C, mutant enzyme I238T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T505S to reconstruct the assayed variant sequence.

proof_lines:
pH 10, 25°C, mutant enzyme T505S
pH 7.5, 25°C, mutant enzyme T505S


enzyme_display_name: alditol oxidase

organism: Streptomyces coelicolor

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

proof_lines: in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C

enzyme: alditol oxidase


substrate_name: D-galactose

substrate: D-galactose


smiles: CC(CO)O


smiles: C(CO)C(CCO)O


enzyme_display_name: Alditol oxidase

organism: Streptomyces sp. (strain IKD472 / FERM P-14339)

enzyme: Alditol oxidase


enzyme_display_name: prosolanapyrone-II oxidase

organism: Alternaria solani

substrate_name: Prosolanapyrone II; O2

enzyme: prosolanapyrone-II oxidase

substrate: Prosolanapyrone II; O2


enzyme_display_name: Aclacinomycin-N/aclacinomycin-A oxidase

organism: Streptomyces galilaeus

substrate_name: AclA

proof_lines: kcat is 0.17 sec(-1) for oxidase activity with AclA.

enzyme: Aclacinomycin-N/aclacinomycin-A oxidase

substrate: AclA


enzyme_display_name: 5-(hydroxymethyl)furfural oxidase

organism: Methylovorus sp. MP688

enzyme: 5-(hydroxymethyl)furfural oxidase


enzyme_display_name: C-glycoside 3-oxidase

organism: Microbacterium sp

proof_lines: kcat is 4.3 sec(-1) with carminic acid as substrate.

enzyme: C-glycoside 3-oxidase


enzyme_display_name: glycerol-3-phosphate dehydrogenase

organism: Saccharomyces cerevisiae

substrate_name: NADH; H+; Glycerone phosphate

assay_conditions_summary: cofactor NADH

enzyme: glycerol-3-phosphate dehydrogenase

substrate: NADH; H+; Glycerone phosphate


organism: Sus scrofa

substrate_name: Acceptor; sn-Glycerol 3-phosphate

proof_lines: pig brain mitochondrial glycerol-3-phosphate dehydrogenase

substrate: Acceptor; sn-Glycerol 3-phosphate


enzyme_display_name: UniProt Q88JH0

organism: Pseudomonas putida

substrate_name: 5-(hydroxymethyl)furoic acid

proof_lines:
Raw SKiD Env: Temp=-----, pH=and
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt Q88JH0

substrate: 5-(hydroxymethyl)furoic acid


enzyme_display_name: Alcohol dehydrogenase (quinone), dehydrogenase subunit

organism: Gluconobacter oxydans (strain 621H)


enzyme_display_name: Alcohol dehydrogenase (quinone), cytochrome c subunit


enzyme_display_name: D-lactate dehydrogenase (quinone)

organism: Pseudomonas putida KT2440

substrate_name: cytochrome c

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

assay_conditions_summary: pH 7.4; 303.15 K; cofactor FAD

proof_lines: cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C

enzyme: D-lactate dehydrogenase (quinone)

substrate: cytochrome c


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: alcohol dehydrogenase (azurin)

substrate_name: 1-Butanol; Hexacyanoferrate(III)

enzyme: alcohol dehydrogenase (azurin)

substrate: 1-Butanol; Hexacyanoferrate(III)


enzyme_display_name: Quinohemoprotein alcohol dehydrogenase ADH-IIG

smiles: CCCCO


enzyme_display_name: Quinohemoprotein alcohol dehydrogenase

organism: Comamonas testosteroni

enzyme: Quinohemoprotein alcohol dehydrogenase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: pH 8

proof_lines: kcat is 4.1 min(-1) with farnesyl-phosphoryl-beta-D-ribofuranose as substrate (at pH 8 and 30 degrees Celsius).


enzyme_display_name: 2-hydroxyglutarate dehydrogenase

organism: Homo sapiens

substrate_name: Acceptor; (S)-2-Hydroxyglutarate

enzyme: 2-hydroxyglutarate dehydrogenase

substrate: Acceptor; (S)-2-Hydroxyglutarate


organism: Arabidopsis thaliana


enzyme_display_name: D-2-hydroxy-acid dehydrogenase

organism: Archaeoglobus fulgidus

substrate_name: D-Lactate; Phenazine methosulfate

enzyme: D-2-hydroxy-acid dehydrogenase

substrate: D-Lactate; Phenazine methosulfate


enzyme_display_name: cellobiose dehydrogenase (acceptor)

organism: Phanerodontia chrysosporium

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M65H with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 4.5, reaction with cellobiose, mutant enzyme M65H

enzyme: cellobiose dehydrogenase (acceptor)


substrate_name: cellulose

proof_lines:
ferricyanide as electron acceptor
pH 4.0, 30°C
pH 4.5, 22°C

substrate: cellulose


organism: Thermothielavioides terrestris

assay_conditions_summary: pH 6; 298.15 K; buffer 50 mM MES


proof_lines: pH 4.5, reaction with cellobiose, wild-type enzyme


organism: Termitomyces clypeatus


organism: Amesia atrobrunnea


organism: Thermothelomyces fergusii


organism: Schizophyllum commune


organism: Dichomera saubinetii


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F166Y with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: mutant F166Y, cellobiose oxidation with electron acceptors


enzyme_display_name: hydroxyacid-oxoacid transhydrogenase

organism: Rattus norvegicus

substrate_name: 2-Oxoglutarate; 4-Hydroxybutanoate

enzyme: hydroxyacid-oxoacid transhydrogenase

substrate: 2-Oxoglutarate; 4-Hydroxybutanoate


organism: Mus musculus


enzyme_display_name: pyranose dehydrogenase (acceptor)

organism: Agaricus campestris

substrate_name: ferrocenium ion

column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `Fc+PF6 (pH 8.5)` the AcPDH group prints Km 1.19, kcat 19.92 and kcat/Km 16.7.

normalized_value_unit_evidence: kcat: printed Table 4 cell 19.92 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 19.92 s^(-1). Km: printed cell 1.19 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 1.19 mM. kcat/Km: printed cell 16.7 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 16.7 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 19.92 / 1.19 = 16.73949579831933 s^-1 mM^-1, against the printed efficiency cell 16.7.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `Fc+PF6 (pH 8.5)`, AcPDH column group: Km = 1.19 mM; kcat = 19.92 s-1; kcat/Km = 16.7 mM-1 s-1.

row_label: Table 4, substrate row `Fc+PF6 (pH 8.5)`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)

table_label: Table 4: Apparent kinetic constants for selected electron acceptors determined at 30 °C with 25 mM D-glucose as the electron donor. (Biomolecules 2013, 3(3):535-552)

enzyme: pyranose dehydrogenase (acceptor)

substrate: ferrocenium ion


organism: Agaricus xanthodermus

column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `Fc+PF6 (pH 8.5)` the AxPDH group prints Km 0.03, kcat 22.07 and kcat/Km 735.7.

normalized_value_unit_evidence: kcat: printed Table 4 cell 22.07 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 22.07 s^(-1). Km: printed cell 0.03 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.03 mM. kcat/Km: printed cell 735.7 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 735.7 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 22.07 / 0.03 = 735.6666666666667 s^-1 mM^-1, against the printed efficiency cell 735.7.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `Fc+PF6 (pH 8.5)`, AxPDH column group: Km = 0.03 mM; kcat = 22.07 s-1; kcat/Km = 735.7 mM-1 s-1.

row_label: Table 4, substrate row `Fc+PF6 (pH 8.5)`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)


enzyme_display_name: UniProt Q3L245

organism: Leucoagaricus meleagris

substrate_name: ferricenium ion

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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=30°C, pH=4
Raw SKiD Env: Temp=30°C, pH=7.5

source_databases_merged: skid uniprot

enzyme: UniProt Q3L245

substrate: ferricenium ion


enzyme_display_name: Pyranose dehydrogenase

organism: Agaricus bisporus

enzyme: Pyranose dehydrogenase


enzyme_display_name: (S)-mandelate dehydrogenase

organism: Pseudomonas putida

substrate_name: (S)-Mandelate; Riboflavin-5-phosphate

assay_conditions_summary: pH 7.5; 293.15 K; buffer 0.1 M potassium phosphate; cofactor FMN

proof_lines: in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C

source_databases_merged: sabio_rk brenda skid uniprot

enzyme: (S)-mandelate dehydrogenase

substrate: (S)-Mandelate; Riboflavin-5-phosphate


substrate_name: (R,S)-p-chloromandelate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H274G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H274G, in presence of 20 mM imidazole

substrate: (R,S)-p-chloromandelate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 20°C, mutant enzyme G81A
mutant G81A
mutant G81A of chimera MDH-GOX2


substrate_name: ethyl-(S)-mandelate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R277G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5

substrate: ethyl-(S)-mandelate


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

proof_lines: pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach

proof_lines: pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach


proof_lines: wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5


substrate_name: methyl-(S)-mandelate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R277K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5

substrate: methyl-(S)-mandelate


organism: Rhodotorula graminis

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

proof_lines: pH 7.5, 25°C, cosubstrate ferricyanide, LMDH holoenzyme

proof_lines: pH 7.5, 25°C, cosubstrate cytochrome, LMDH holoenzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165K/R277K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165G/R277K to reconstruct the assayed variant sequence.


smiles: CCOC(=O)C(C#C)O

assay_conditions_summary: pH 7.5; buffer 0.1 M potassium phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165G to reconstruct the assayed variant sequence.


enzyme_display_name: soluble quinoprotein glucose dehydrogenase

organism: Acinetobacter calcoaceticus

substrate_name: D-Lyxose

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

mutation_type: truncation

proof_lines: stopped-flow measurement of reductive half-reaction, 15°C

substrate: D-Lyxose


proof_lines: free enzyme, pH and temperature not specified in the publication

enzyme: soluble quinoprotein glucose dehydrogenase


substrate_name: melibiose

mutation_signature: stopped-flow measurement of reductive half-reaction

substrate: melibiose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-fucose

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

substrate: D-fucose


substrate_name: lactose

substrate: lactose


enzyme_display_name: NDMA-dependent alcohol dehydrogenase

organism: Rhodococcus erythropolis

substrate_name: N,N-Dimethyl-4-nitrosoaniline; Ethanol

sequence: MKTKAAVLFETHKPFEIVELEL

wild_type_sequence: MKTKAAVLFETHKPFEIVELEL

proof_lines: The lower limit of the determination of KM with NDMA as electron acceptor was 0.001 mM. KM was even lower for hexan-1-ol, pentan-1-ol, and citronellol.

enzyme: NDMA-dependent alcohol dehydrogenase

substrate: N,N-Dimethyl-4-nitrosoaniline; Ethanol


enzyme_display_name: alcohol dehydrogenase (nicotinoprotein)

organism: Amycolatopsis methanolica

substrate_name: Unknown

proof_lines: uncompetitive inhibition term reflecting binding to the enzyme containing the oxidized coenzyme

proof_lines: competitive inhibition term with respect to NDMA

enzyme: alcohol dehydrogenase (nicotinoprotein)

substrate: Unknown


organism: Niallia circulans

substrate_name: DOIA

proof_lines: Kinetic parameter was determined with saturating SAM. DOIA displays substrate inhibition.

substrate: DOIA


organism: Homo sapiens


enzyme_display_name: D-2-hydroxyglutarate dehydrogenase

organism: Escherichia coli (strain K12)

enzyme: D-2-hydroxyglutarate dehydrogenase


organism: Stutzerimonas stutzeri (strain A1501)

substrate_name: electron transfer flavoprotein (at pH 7.4 and 37 degrees Celsius)

proof_lines: kcat is 7.9 sec(-1) with D-2-hydroxyglutarate as substrate and DCIP as the electron acceptor (at pH 7.4 and 37 degrees Celsius). kcat is 13.0 sec(-1) with D-2-hydroxyglutarate as substrate and electron transfer flavoprotein (ETF) as the ele


organism: Pantoea ananatis (strain AJ13355)


enzyme_display_name: aldehyde dehydrogenase (NAD+)

substrate_name: H2O; Propanal; NAD+

enzyme: aldehyde dehydrogenase (NAD+)

substrate: H2O; Propanal; NAD+


substrate_name: NAD+; H2O; Propanal

assay_conditions_summary: pH 7.5; 310.15 K; buffer 0.1 M sodium diphosphate; cofactor NAD+

proof_lines: isoform ALDH2, in 0.1 M sodium diphosphate buffer (pH 9.5), at 21-23°C

unit: lgwedgeoneswedgeone

substrate: NAD+; H2O; Propanal


substrate_name: NAD+; H2O; 20-CHO-Leukotriene B4

proof_lines: kcat is 2.18 sec(-1) for decanal as substrate. kcat is 2.23 sec(-1) for dodecanal as substrate. kcat is 0.86 sec(-1) for tetradecanal as substrate. kcat is 0.95 sec(-1) for hexadecanal as substrate. kcat is 1.52 sec(-1) for octadecanal as s

substrate: NAD+; H2O; 20-CHO-Leukotriene B4


substrate_name: H2O; NAD+; Citral

substrate: H2O; NAD+; Citral


substrate_name: NAD+; Glycolaldehyde; H2O

substrate: NAD+; Glycolaldehyde; H2O


substrate_name: H2O; Formaldehyde; NAD+

substrate: H2O; Formaldehyde; NAD+


substrate_name: H2O; NAD+; Betaine aldehyde

substrate: H2O; NAD+; Betaine aldehyde


substrate_name: 4-Carboxybenzaldehyde; H2O; NAD+

substrate: 4-Carboxybenzaldehyde; H2O; NAD+


substrate_name: NADP+; Benzaldehyde; H2O

assay_conditions_summary: cofactor NADP+

substrate: NADP+; Benzaldehyde; H2O


organism: Mesocricetus auratus

substrate_name: H2O; Acetaldehyde; NAD+

substrate: H2O; Acetaldehyde; NAD+


organism: Equus caballus

substrate_name: 3-Methylbutanal; H2O; NAD+

substrate: 3-Methylbutanal; H2O; NAD+


organism: Mus musculus

substrate_name: NAD+; H2O; Acetaldehyde

substrate: NAD+; H2O; Acetaldehyde


substrate_name: H2O; NAD+; Acetaldehyde

substrate: H2O; NAD+; Acetaldehyde


organism: Bos taurus

substrate_name: H2O; NAD+; D-Glyceraldehyde

substrate: H2O; NAD+; D-Glyceraldehyde


substrate_name: Propanal; H2O; NAD+

substrate: Propanal; H2O; NAD+


organism: Bacillus subtilis

substrate_name: 2,5-Dioxopentanoate; NAD+; H2O

substrate: 2,5-Dioxopentanoate; NAD+; H2O


organism: Arthrobacter nicotinovorans

substrate_name: H2O; NAD+; Butanal

substrate: H2O; NAD+; Butanal


substrate_name: Benzaldehyde; NAD+; H2O

substrate: Benzaldehyde; NAD+; H2O


substrate_name: H2O; Nonanal; NAD+

substrate: H2O; Nonanal; NAD+


organism: Cupriavidus necator

substrate_name: NADH; H+; Dimethylglyoxal

substrate: NADH; H+; Dimethylglyoxal


organism: Loktanella sp.

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


enzyme_display_name: UniProt Q92UV7

organism: Sinorhizobium meliloti

substrate_name: 3-oxopropyl phosphonate

enzyme: UniProt Q92UV7

substrate: 3-oxopropyl phosphonate


enzyme_display_name: Aldehyde dehydrogenase 1A1

proof_lines: Has a much higher catalytic efficiency toward all-trans retinal.

enzyme: Aldehyde dehydrogenase 1A1


enzyme_display_name: Aldehyde dehydrogenase family 3 member I1, chloroplastic

organism: Arabidopsis thaliana


enzyme_display_name: Aldehyde dehydrogenase family 3 member H1


organism: Macaca fascicularis

proof_lines: Has a nearly 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans and 13-cis retinal.


organism: Oryctolagus cuniculus


organism: Antirrhinum majus

proof_lines: kcat is 0.31 sec(-1) with benzaldehyde as substrate (PubMed:19292760). kcat is 2.08 sec(-1) with acetaldehyde as substrate (PubMed:19292760). kcat is 0.23 sec(-1) with phenylacetaldehyde as substrate (PubMed:19292760).


enzyme_display_name: Aldehyde dehydrogenase

organism: Craterostigma plantagineum

enzyme: Aldehyde dehydrogenase


enzyme_display_name: aldehyde dehydrogenase (NADP+)

organism: Escherichia coli

substrate_name: H2O; Acetaldehyde; NADP+

enzyme: aldehyde dehydrogenase (NADP+)

substrate: H2O; Acetaldehyde; NADP+


organism: Thermoplasma acidophilum

substrate_name: Glyceraldehyde; NADP+; H2O

substrate: Glyceraldehyde; NADP+; H2O


substrate_name: Butanal; NADP+; H2O

substrate: Butanal; NADP+; H2O


organism: Saccharomyces cerevisiae

substrate_name: NADP+; H2O; Propanal

substrate: NADP+; H2O; Propanal


organism: Acinetobacter calcoaceticus


organism: Acetobacter pasteurianus


enzyme_display_name: Aldehyde dehydrogenase 5, mitochondrial

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Aldehyde dehydrogenase 5, mitochondrial


enzyme_display_name: aldehyde dehydrogenase [NAD(P)+]

organism: Homo sapiens

substrate_name: Benzaldehyde; H2O; NAD+

enzyme: aldehyde dehydrogenase [NAD(P)+]

substrate: Benzaldehyde; H2O; NAD+


organism: Rattus norvegicus

substrate_name: Propanal; NAD+; H2O

substrate: Propanal; NAD+; H2O


organism: Mus musculus

substrate_name: H2O; all-trans-Retinal; NAD+

substrate: H2O; all-trans-Retinal; NAD+


substrate_name: NADP+; Propanal; H2O

substrate: NADP+; Propanal; H2O


enzyme_display_name: Aldehyde dehydrogenase family 3 member B1


enzyme_display_name: NADP/NAD-dependent aldehyde dehydrogenase PuuC

organism: Escherichia coli (strain K12)


enzyme_display_name: Aldehyde dehydrogenase 1

organism: Tanacetum cinerariifolium

substrate_name: trans-chrysanthemal (in the presence of NAD(+))

proof_lines: kcat is 0.11 sec(-1) with trans-chrysanthemal as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.096 sec(-1) with trans-chrysanthemal as substrate (in the presence of NADP(+)) (PubMed:29122986). kcat is 0.09 sec(-1) with

enzyme: Aldehyde dehydrogenase 1


enzyme: Aldehyde dehydrogenase family 3 member B1


enzyme_display_name: betaine-aldehyde dehydrogenase

substrate_name: Betaine aldehyde; NAD+; H2O

enzyme: betaine-aldehyde dehydrogenase

substrate: Betaine aldehyde; NAD+; H2O


substrate_name: Betaine aldehyde; H2O; NAD+

substrate: Betaine aldehyde; H2O; NAD+


organism: Oryza sativa

proof_lines: isozyme BADH1, pH and temperature not specified in the publication


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

organism: Arabidopsis thaliana


enzyme_display_name: Betaine aldehyde dehydrogenase

enzyme: Betaine aldehyde dehydrogenase


enzyme_display_name: Betaine aldehyde dehydrogenase 2

organism: Oryza sativa subsp. japonica

substrate_name: gamma-guanidinobutyraldehyde (GGBald)

enzyme: Betaine aldehyde dehydrogenase 2

substrate: gamma-guanidinobutyraldehyde (GGBald)


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

enzyme: Aminoaldehyde dehydrogenase 1a


enzyme_display_name: NAD/NADP-dependent betaine aldehyde dehydrogenase

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: betaine aldehyde (at pH 8.0 and 30 degrees Celsius, in the presence of NADP(+))

proof_lines: kcat is 261 sec(-1) for the NADP-dependent oxidation of betaine aldehyde. kcat is 276 sec(-1) for the NAD-dependent oxidation of betaine aldehyde.


enzyme_display_name: Aminoaldehyde dehydrogenase BADH

organism: Spinacia oleracea

enzyme: Aminoaldehyde dehydrogenase BADH


organism: Giardia duodenalis

substrate_name: acetyl-CoA

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

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA


substrate_name: NADH

substrate: NADH


substrate_name: CoA

substrate: CoA


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: propanal

smiles: CCC=O

substrate: propanal


organism: Synechococcus sp.

substrate_name: NADPH; Glycerate 3-phosphate; H+

substrate: NADPH; Glycerate 3-phosphate; H+


organism: Burkholderia xenovorans LB400

substrate_name: Coenzyme A; Acetaldehyde; NAD+

unit: Mswedgeone

substrate: Coenzyme A; Acetaldehyde; NAD+


organism: Thermus thermophilus

substrate_name: Acetaldehyde; Coenzyme A; NAD+

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat; cells Km 15.4+/-1.5, kcat 3.5+/-0.01.

normalized_value_unit_evidence: kcat normalized_value=3.5 normalized_unit=s^-1; Km normalized_value=15.4 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde: Km 15.4+/-1.5; kcat 3.5+/-0.01 s^-1.

substrate: Acetaldehyde; Coenzyme A; NAD+


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde; columns Km, kcat; cells Km 9.4+/-0.8, kcat 2.8+/-0.07.

normalized_value_unit_evidence: kcat normalized_value=2.8 normalized_unit=s^-1; Km normalized_value=9.4 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde: Km 9.4+/-0.8; kcat 2.8+/-0.07 s^-1.


organism: Burkholderia xenovorans

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat; cells Km 15.7+/-1.3, kcat 2.2+/-0.06.

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; Km normalized_value=15.7 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde: Km 15.7+/-1.3; kcat 2.2+/-0.06 s^-1.


substrate_name: NAD+; Coenzyme A; Acetaldehyde

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde; columns Km, kcat; cells Km 23.6+/-1.8, kcat 17.2+/-0.5.

normalized_value_unit_evidence: kcat normalized_value=17.2 normalized_unit=s^-1; Km normalized_value=23.6 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde: Km 23.6+/-1.8; kcat 17.2+/-0.5 s^-1.

substrate: NAD+; Coenzyme A; Acetaldehyde


substrate_name: Acetaldehyde

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 23.6+/-1.8, kcat 17.2+/-0.5, kcat/Km 7.3+/-0.06 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=17.2 normalized_unit=s^-1; Km normalized_value=23.6 normalized_unit=mM; kcat/Km normalized_value=0.73 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde: Km 23.6+/-1.8; kcat 17.2+/-0.5 s^-1; kcat/Km 7.3+/-0.06 x10^2 M^-1 s^-1.

substrate: Acetaldehyde


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 15.7+/-1.3, kcat 2.2+/-0.06, kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; Km normalized_value=15.7 normalized_unit=mM; kcat/Km normalized_value=0.14 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde: Km 15.7+/-1.3; kcat 2.2+/-0.06 s^-1; kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 9.4+/-0.8, kcat 2.8+/-0.07, kcat/Km 3.0+/-0.3 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.8 normalized_unit=s^-1; Km normalized_value=9.4 normalized_unit=mM; kcat/Km normalized_value=0.30 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde: Km 9.4+/-0.8; kcat 2.8+/-0.07 s^-1; kcat/Km 3.0+/-0.3 x10^2 M^-1 s^-1.


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 15.4+/-1.5, kcat 3.5+/-0.01, kcat/Km 2.3+/-0.3 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=3.5 normalized_unit=s^-1; Km normalized_value=15.4 normalized_unit=mM; kcat/Km normalized_value=0.23 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde: Km 15.4+/-1.5; kcat 3.5+/-0.01 s^-1; kcat/Km 2.3+/-0.3 x10^2 M^-1 s^-1.


organism: Saccharomyces cerevisiae

substrate_name: NAD+; D-Glyceraldehyde 3-phosphate; Phosphate


substrate_name: Glycerate 1,3-bisphosphate; H+; NADH

substrate: Glycerate 1,3-bisphosphate; H+; NADH


substrate_name: Phosphate; D-Glyceraldehyde 3-phosphate; NAD+


substrate_name: D-Glyceraldehyde 3-phosphate; NAD+; Phosphate


substrate_name: D-Glyceraldehyde 3-phosphate; Phosphate; NAD+


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

substrate_name: NADPH; Glycerate 1,3-bisphosphate; H+

substrate: NADPH; Glycerate 1,3-bisphosphate; H+


substrate_name: NADPH; H+; Glycerate 1,3-bisphosphate

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

substrate: NADPH; H+; Glycerate 1,3-bisphosphate


organism: Thermoanaerobacter ethanolicus

substrate_name: n-butyryl-CoA

substrate: n-butyryl-CoA


substrate_name: acetyl-CoA


substrate_name: NADH


substrate_name: CoA


substrate_name: NAD+

substrate: NAD+


substrate_name: acetaldehyde


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


organism: Crocosphaera subtropica

substrate_name: succinate semialdehyde

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

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

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

proof_lines: pH 9.0, 25°C, recombinant mutant K154A, with NADP+

proof_lines: pH 9.0, 25°C, recombinant mutant K154A, with NAD+

substrate: succinate semialdehyde


substrate_name: NADP+

substrate: NADP+


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

proof_lines: pH 9.0, 25°C, recombinant mutant S157E, with NAD+

proof_lines: pH 9.0, 25°C, recombinant mutant S157E, with NADP+


proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme, with NAD+

proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme, with NADP+


proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme


organism: Methanothermus fervidus

substrate_name: NADPH

column_label: Table 2 columns Reaction Reduction of GriP2; Variable substrate NADPH; fixed GriP2 0.7 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.002 mM.

raw_value_unit_evidence: Table 2 row NADPH: Km=0.002 mM and Vmax=7.5 U/mg protein.

row_label: Reduction of GriP2 row NADPH

table_label: Table 2

substrate: NADPH


column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate NADP+; fixed GraP 2 mM; fixed arsenate 120 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.003 mM.

raw_value_unit_evidence: Table 2 row NADP+: Km=0.003 mM and Vmax=4.3 U/mg protein.

row_label: Oxidation of GraP row NADP+


column_label: Table 2 columns Reaction Reduction of GriP2; Variable substrate NADH; fixed GriP2 0.7 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.066 mM.

raw_value_unit_evidence: Table 2 row NADH: Km=0.066 mM and Vmax=12.6 U/mg protein.

row_label: Reduction of GriP2 row NADH

substrate: NADH


column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate NAD+; fixed GraP 2 mM; fixed arsenate 120 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.65 mM.

raw_value_unit_evidence: Table 2 row NAD+: Km=0.65 mM and Vmax=12.0 U/mg protein.

row_label: Oxidation of GraP row NAD+


substrate_name: arsenate

column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate arsenate; fixed NAD+ 1 mM; fixed GraP 2 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=43 mM.

raw_value_unit_evidence: Table 2 row arsenate: Km=43 mM and Vmax=12.5 U/mg protein.

row_label: Oxidation of GraP row arsenate

substrate: arsenate


substrate_name: phosphate

smiles: OP(=O)(O)O

column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate phosphate; fixed NAD+ 1 mM; fixed GraP 2 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=53 mM.

raw_value_unit_evidence: Table 2 row phosphate: Km=53 mM and Vmax=13.7 U/mg protein.

row_label: Oxidation of GraP row phosphate

substrate: phosphate


organism: Propionibacterium freudenreichii

substrate: CoA


assay_conditions_summary: cofactor NAD+


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


substrate_name: propanal

substrate: propanal


substrate: acetaldehyde


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; cofactor NADPH

column_label: PMID 22841742 Table 4, Reduction / NADPH, Km (mM) = 0.18 +/- 0.07.

normalized_value_unit_evidence: Km normalized_value=0.18 mM.

raw_value_unit_evidence: Table 4 row Reduction / NADPH, Km column: 0.18 +/- 0.07 mM.

row_label: Reduction / NADPH

table_label: Table 4. Kinetic parameters of phosphorylating glyceraldehyde 3-phosphate dehydrogenase (St-GAPDH) for the oxidative and reductive reactions


substrate_name: DL-glyceraldehyde 3-phosphate

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

assay_conditions_summary: pH 8; cofactor NADP+

column_label: PMID 22841742 Table 4, Oxidation / DL-GAP row under NADP+ condition, Km (mM) = 0.21 +/- 0.04.

normalized_value_unit_evidence: Km normalized_value=0.21 mM.

raw_value_unit_evidence: Table 4 row Oxidation / DL-GAP with 0.5 mM NADP+ and 20 mM phosphate, Km column: 0.21 +/- 0.04 mM.

row_label: Oxidation / DL-GAP with NADP+

substrate: DL-glyceraldehyde 3-phosphate


normalized_value_unit_evidence: Km normalized_value=0.28 mM.

raw_value_unit_evidence: Table 4 row Oxidation / NADP+, Km column: 0.28 +/- 0.08 mM.

row_label: Oxidation / NADP+


assay_conditions_summary: pH 8; cofactor NADH

normalized_value_unit_evidence: Km normalized_value=0.61 mM.

raw_value_unit_evidence: Table 4 row Reduction / NADH, Km column: 0.61 +/- 0.07 mM.

row_label: Reduction / NADH


substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines: wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C

substrate: 3-phospho-D-glyceroyl phosphate


column_label: PMID 22841742 Table 4, Oxidation / Phosphate, Km (mM) = 107 +/- 22; no phosphate Km = 10.7 mM cell.

normalized_value_unit_evidence: Km normalized_value=107 mM for phosphate row; expected 10.7 mM is not a Km cell.

raw_value_unit_evidence: Table 4 row Oxidation / Phosphate, Km column: 107 +/- 22 mM. The 10.7 +/- 5.3 mM value appears in the Ki column for the adjacent NAD+ row, not the phosphate Km cell.

row_label: Oxidation / Phosphate


assay_conditions_summary: pH 8; cofactor NAD+

normalized_value_unit_evidence: Km normalized_value=16.8 mM.

raw_value_unit_evidence: Table 4 row Oxidation / NAD+, Km column: 16.8 +/- 8.9 mM.

row_label: Oxidation / NAD+


substrate_name: Unknown

substrate: Unknown


organism: Thermoanaerobacter sp.

substrate_name: butyryl-CoA

assay_conditions_summary: pH 7.9; 333.15 K; cofactor CoA

substrate: butyryl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: Butyraldehyde

substrate: Butyraldehyde


organism: Leuconostoc mesenteroides

substrate_name: CoA


substrate_name: NAD+

substrate: NAD+


substrate_name: acetaldehyde


assay_conditions_summary: cofactor ATP


organism: Clostridium kluyveri


substrate_name: Butanal

substrate: Butanal


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


organism: Bacillus anthracis

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: at pH 8.5, temperature not specified in the publication

proof_lines: pH 8.6, temperature not specified in the publication


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Thermoproteus tenax

substrate_name: NADP+

substrate: NADP+


substrate_name: arsenate

substrate: arsenate


substrate_name: phosphate

substrate: phosphate


substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+


substrate_name: Succinic semialdehyde

proof_lines: with NAD+ as cosubstrate, at pH 6.5 and 70°C

proof_lines: with NADP+ as cosubstrate, at pH 6.5 and 70°C

substrate: Succinic semialdehyde


substrate_name: 2-oxoglutarate semialdehyde

substrate: 2-oxoglutarate semialdehyde


assay_conditions_summary: pH 6.5; 343.15 K; cofactor NAD+


substrate_name: NADPH

assay_conditions_summary: pH 6.5; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 7.5; cofactor NADP+


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: malonate-semialdehyde dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: malonate semialdehyde

enzyme: malonate-semialdehyde dehydrogenase

substrate: malonate semialdehyde


substrate_name: Unknown

substrate: Unknown


organism: Bacillus subtilis

assay_conditions_summary: 303.15 K; cofactor NAD+

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


assay_conditions_summary: 303.15 K; cofactor NADP+

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

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


organism: Pyrococcus woesei

assay_conditions_summary: cofactor NADP+


organism: Synechococcus sp.

assay_conditions_summary: cofactor NADPH


organism: Kluyveromyces lactis

assay_conditions_summary: pH 9.2; cofactor NADP+

column_label: Official ACS article visible text, Affinity for NADP, NAD, and D-glyceraldehyde 3-phosphate section

row_label: GDP1/NADP-GAPDH; NADP substrate

table_label: Official ACS article visible prose


assay_conditions_summary: pH 9.2; cofactor NAD+

row_label: GDP1/NADP-GAPDH; NAD substrate


raw_value_unit_evidence: D-glyceraldehyde 3-phosphate Km 750 uM

row_label: GDP1/NADP-GAPDH; D-glyceraldehyde 3-phosphate substrate


assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 313.15 K; cofactor NADP+

proof_lines:
pH 8.0, 40°C, cosubstrate: NAD+
pH 8.0, 40°C, cosubstrate: NADP+
pH 8.0, 60°C, cosubstrate: NAD+


assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+


substrate_name: 3-phospho-D-glyceroyl phosphate

substrate: 3-phospho-D-glyceroyl phosphate


organism: Rattus norvegicus

proof_lines:
synaptosomes
mitochondria of non-synaptic origin


assay_conditions_summary: cofactor NAD+

proof_lines:
mitochondria of non-synaptic origin
synaptosomes


organism: Thermococcus kodakarensis


organism: Euglena gracilis


organism: Thermus thermophilus


organism: Chlamydomonas reinhardtii

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: pH 7.0, temperature not specified in the publication

substrate: acetyl-CoA


organism: Hippoglossus hippoglossus

substrate_name: NADH; H+; Glycerate 1,3-bisphosphate

substrate: NADH; H+; Glycerate 1,3-bisphosphate


organism: Trichoderma koningii


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 338.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7.5; 323.15 K; cofactor NAD+


organism: Paraburkholderia xenovorans

substrate_name: picolinaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I171A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 100 mM HEPES

proof_lines: mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)

substrate: picolinaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I171F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)


substrate_name: propionaldehyde

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature I171F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES

source_databases_merged: brenda oed

substrate: propionaldehyde


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature I171A to reconstruct the assayed variant sequence.


organism: Geobacillus stearothermophilus

sequence_variant_note: Mutation signature S48G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E276G 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 S186G with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


substrate_name: D-glyceraldehyde 3-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y46G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: D-glyceraldehyde 3-phosphate


sequence_variant_note: Mutation signature D186G/S48G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D186G and mutant enzyme S48G


substrate_name: phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E276G/S48G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E276G and mutant enzyme S48G

substrate: phosphate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.


substrate_name: NADP+

sequence_variant_note: Mutation signature D32A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: NADP+


sequence_variant_note: Mutation signature D32A/L187N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.


proof_lines:
mutant enzyme D32A/L187N
mutant enzyme D32A and L187N


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

proof_lines: wild-type enzyme and mutant enzyme L187N


organism: Staphylococcus aureus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C151S/H178N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H178N with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C151S to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.7; cofactor NAD+


enzyme_display_name: UniProt Q6GIL8

assay_conditions_summary: pH 8.7; 298.15 K; cofactor NAD+

proof_lines: kcat is 70 sec(-1) for dehydrogenase activity.

enzyme: UniProt Q6GIL8


organism: Spinacia oleracea

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.


proof_lines: GapB, analyzed under reducing conditions

proof_lines: AB-GAPDH, analyzed under reducing conditions


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R77A to reconstruct the assayed variant sequence.


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

proof_lines: mutant B(188)A, analyzed under oxidizing conditions

proof_lines: A(plusCTE) mutant, analyzed under oxidizing conditions


proof_lines: A(plusCTE) mutant, analyzed under reducing conditions


proof_lines: GapB, analyzed under oxidizing conditions


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C

proof_lines: mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C


proof_lines: wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C

proof_lines: wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C


proof_lines: mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C

proof_lines: mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C


assay_conditions_summary: pH 8; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y139R with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R136K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E141D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L138T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K137E to reconstruct the assayed variant sequence.


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y317A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N313T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y317G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature T34Q/T39S/L43Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant T34Q/T39S/L43Q


sequence_variant_note: Mutation signature D282G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant D282G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant N313T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W310F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant W310F


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

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, wild-type


sequence_variant_note: Mutation signature Y283V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant Y283V


organism: Corynebacterium glutamicum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L36T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D35G/L36T/T37K/P192S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant D35G/L36T/T37K/P192S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D35G/L36T/P192S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant D35G/L36T/P192S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D35G/L36T/T37K to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant D35G/L36T/T37K


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D35G to reconstruct the assayed variant sequence.


proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme


assay_conditions_summary: cofactor NADPH

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


sequence_variant_note: Mutation signature S195A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme S195A, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature R82D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme R82D, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature R82A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme R82A, pH and temperature not specified in the publication


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


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

assay_conditions_summary: cofactor NADH

proof_lines: mutant enzyme R190A, pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetaldehyde (in the presence of HsaF)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 9.4 sec(-1) with acetaldehyde as substrate (in the presence of HsaF). kcat is 19.0 sec(-1) with acetaldehyde as substrate (in the absence of HsaF). kcat is 11.1 sec(-1) with propanal as substrate (in the presence of HsaF). kcat is 2

substrate: acetaldehyde (in the presence of HsaF)


substrate_name: propanal (in the presence of HsaF)

substrate: propanal (in the presence of HsaF)


substrate_name: coenzyme A (in the presence of HsaF)

substrate: coenzyme A (in the presence of HsaF)


substrate_name: NAD(+) (in the presence or absence of HsaF)


substrate_name: NADP(+) (in the presence of HsaF)

substrate: NADP(+) (in the presence of HsaF)


organism: Nitrosomonas europaea

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde


substrate_name: succinate semialdehyde

assay_conditions_summary: pH 8.5; cofactor NADP+

proof_lines: pH 8.5, 30°C, recombinant enzyme, with NAD+

proof_lines: pH 8.5, 30°C, recombinant enzyme, with NADP+

substrate: succinate semialdehyde


substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines: GapB, analyzed under reducing conditions

proof_lines: GapB, analyzed under oxidizing conditions


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R77A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W84F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature W48F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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