column_label: Table 2 AtALDH10A8 Km [uM] column TMABAL row = 15+/-3.

normalized_value_unit_evidence: Km=0.015 mM converted from 15+/-3 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for TMABAL reports 15+/-3 uM.

row_label: AtALDH10A8 / Km column / TMABAL row

table_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

organism: Arabidopsis thaliana

source_db: uniprot

verification_status: verified

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.

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

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Table 2 AtALDH10A8 Km [uM] column GBAL row = 4+/-2.

normalized_value_unit_evidence: Km=0.004 mM converted from 4+/-2 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for GBAL reports 4+/-2 uM.

row_label: AtALDH10A8 / Km column / GBAL row

data_origin: experimental

status: verified

source: uniprot


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal

smiles: C[N+](C)(C)CCCC=O

column_label: Table 2 AtALDH10A9 Km [uM] column TMABAL row = 17+/-2.

normalized_value_unit_evidence: Km=0.017 mM converted from 17+/-2 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for TMABAL reports 17+/-2 uM.

row_label: AtALDH10A9 / Km column / TMABAL row


column_label: Table 2 AtALDH10A9 Km [uM] column GBAL row = 7+/-0.5.

normalized_value_unit_evidence: Km=0.007 mM converted from 7+/-0.5 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for GBAL reports 7+/-0.5 uM.

row_label: AtALDH10A9 / Km column / GBAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Oxygen-dependent choline dehydrogenase

organism: Escherichia coli (strain K12)

substrate_name: NAD (at pH 7.5 and 37 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Prose in soluble NAD-dependent glycine betaine-aldehyde dehydrogenase paragraph: apparent Km values of glycine betaine aldehyde, NAD, and NADP were 0.13, 0.06, and 0.5 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.06 raw_unit=mM raw_cell=0.06

row_label: NAD / soluble glycine betaine-aldehyde dehydrogenase

table_label: Prose kinetic constants for soluble glycine betaine-aldehyde dehydrogenase

enzyme: Oxygen-dependent choline dehydrogenase

substrate: NAD (at pH 7.5 and 37 degrees Celsius)


substrate_name: glycine betaine aldehyde (at pH 7.5 and 37 degrees Celsius)

raw_value_unit_evidence: Km raw_value=0.13 raw_unit=mM raw_cell=0.13

row_label: glycine betaine aldehyde / soluble glycine betaine-aldehyde dehydrogenase


substrate_name: NADP (at pH 7.5 and 37 degrees Celsius)

raw_value_unit_evidence: Km raw_value=0.5 raw_unit=mM raw_cell=0.5

row_label: NADP / soluble glycine betaine-aldehyde dehydrogenase

substrate: NADP (at pH 7.5 and 37 degrees Celsius)


substrate_name: choline (at pH 7.5 and 37 degrees Celsius)

verification_status: unverified

smiles: C[N+](C)(C)CCO

status: unverified


enzyme_display_name: Potassium-activated aldehyde dehydrogenase, mitochondrial

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADP (with acetaldehyde as cosubstrate)

substrate: NADP (with acetaldehyde as cosubstrate)


substrate_name: NAD (with propanal as cosubstrate)

assay_conditions_summary: pH 7.4; buffer 100 mM sodium phosphate

column_label: PMC Table 3 row ALDH2 under Propionaldehyde-NAD lists NAD Km 1,100 uM.

raw_value_unit_evidence: 1,100 uM in Table 3.

row_label: ALDH2 / Propionaldehyde-NAD / NAD

table_label: PMC106960 Table 3, kinetic properties of yeast ALDHs

enzyme: Potassium-activated aldehyde dehydrogenase, mitochondrial

substrate: NAD (with propanal as cosubstrate)


substrate_name: acetaldehyde (with NADP as cosubstrate)

smiles: CC=O

column_label: PMC Table 3 row ALDH2 under Acetaldehyde-NADP lists aldehyde Km 10 uM.

raw_value_unit_evidence: 10 uM in Table 3.

row_label: ALDH2 / Acetaldehyde-NADP / aldehyde

substrate: acetaldehyde (with NADP as cosubstrate)


substrate_name: propanal (with NADP as cosubstrate)

smiles: CCC=O

substrate: propanal (with NADP as cosubstrate)


enzyme_display_name: Aldehyde dehydrogenase family 3 member B1

organism: Homo sapiens

substrate_name: octanal

smiles: CCCCCCCC=O

assay_conditions_summary: pH 8.5; buffer B: 50 mM Tris-HCl pH 8; cofactor NAD+

column_label: Figure 3 kinetic-parameter prose / ALDH3B1-catalyzed oxidation of octanal: Km 25.0 uM; normalized Km 0.025 mM.

raw_value_unit_evidence: Figure 3 kinetic-parameter prose reports Vmax (pmol/min/ng protein) and Km (uM) for 3xFLAG-ALDH3B1-catalyzed oxidation: 9.7 and 45.6 for hexadecanal, 4.8 and 4.9 for trans-2-hexadecenal, and 5.0 and 25.0 for octanal. Matched row substrate: octanal; Km 25.0 uM.

row_label: 3xFLAG-ALDH3B1 oxidation of octanal

table_label: Figure 3 / ALDH3B1 exhibits activity toward C16 aldehydes

substrate: octanal


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

column_label: Figure 3 kinetic-parameter prose / ALDH3B1-catalyzed oxidation of hexadecanal: Km 45.6 uM; normalized Km 0.0456 mM.

raw_value_unit_evidence: Figure 3 kinetic-parameter prose reports Vmax (pmol/min/ng protein) and Km (uM) for 3xFLAG-ALDH3B1-catalyzed oxidation: 9.7 and 45.6 for hexadecanal, 4.8 and 4.9 for trans-2-hexadecenal, and 5.0 and 25.0 for octanal. Matched row substrate: hexadecanal; Km 45.6 uM.

row_label: 3xFLAG-ALDH3B1 oxidation of hexadecanal

enzyme: Aldehyde dehydrogenase family 3 member B1

substrate: hexadecanal


smiles: CCCCCCCCCCCCCC=CC=O

column_label: Figure 3 kinetic-parameter prose / ALDH3B1-catalyzed oxidation of trans-2-hexadecenal: Km 4.9 uM; normalized Km 0.0049 mM.

raw_value_unit_evidence: Figure 3 kinetic-parameter prose reports Vmax (pmol/min/ng protein) and Km (uM) for 3xFLAG-ALDH3B1-catalyzed oxidation: 9.7 and 45.6 for hexadecanal, 4.8 and 4.9 for trans-2-hexadecenal, and 5.0 and 25.0 for octanal. Matched row substrate: trans-2-hexadecenal; Km 4.9 uM.

row_label: 3xFLAG-ALDH3B1 oxidation of trans-2-hexadecenal


enzyme_display_name: aldehyde dehydrogenase (NAD(+))

substrate_name: Acetaldehyde

source_db: oed

kcat_over_km_origin: calculated

enzyme: aldehyde dehydrogenase (NAD(+))

substrate: Acetaldehyde

source: oed


substrate_name: citral

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

substrate: citral


substrate_name: NAD+

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E487Q with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


substrate_name: propanal

substrate: propanal


organism: Rattus norvegicus

sequence_variant_note: Mutation signature S74A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Betaine aldehyde dehydrogenase

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

proof_lines:
NAD
NADP
betaine aldehyde dehydrogenase

enzyme: Betaine aldehyde dehydrogenase

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


substrate_name: betaine aldehyde (at pH 7.5 and 25 degrees Celsius)

proof_lines:
betaine aldehyde
betaine aldehyde dehydrogenase
0.13 mM


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

proof_lines:
NADP
betaine aldehyde dehydrogenase
0.13 mM

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


organism: Bacillus subtilis (strain 168)

substrate_name: betaine aldehyde

substrate: betaine aldehyde


substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

substrate: NAD(+)


enzyme_display_name: Aldehyde dehydrogenase 1A1

substrate_name: benzaldehyde (at pH 7.1 and 30 degrees Celsius)

enzyme: Aldehyde dehydrogenase 1A1


substrate_name: 3-deoxyglucosone (at pH 7.1 and 30 degrees Celsius)

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


enzyme_display_name: aldehyde dehydrogenase (NADP(+))

organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

enzyme: aldehyde dehydrogenase (NADP(+))


substrate_name: NADP+

substrate: NADP+


enzyme_display_name: Betaine aldehyde dehydrogenase 2

organism: Oryza sativa subsp. japonica

substrate_name: 3-aminopropionaldehyde (AP-ald)

smiles: C(CN)C=O

enzyme: Betaine aldehyde dehydrogenase 2

substrate: 3-aminopropionaldehyde (AP-ald)


organism: Equus caballus

substrate_name: p-Nitrophenyl acetate

proof_lines:
horse liver aldehyde dehydrogenase
esterase reaction
NAD(H)

substrate: p-Nitrophenyl acetate


organism: Arthrobacter nicotinovorans

verification_status: corrected

assay_conditions_summary: pH 8.4; 301.15 K; cofactor NAD+

column_label: Table 2; row NAD+ footnote a; columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); footnote a determined with butyraldehyde.

normalized_value_unit_evidence: kcat paper=3.1 s^-1; Km paper=1.26 mM; kcat/Km paper=2.4 s^-1 mM^-1

row_label: NAD+ footnote a

table_label: Table 2. Kinetic parameters of ALDH

status: corrected


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

smiles: C(C=O)C=O

assay_conditions_summary: pH 8


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

smiles: CCCCCC=O

assay_conditions_summary: pH 8; buffer pH 8; cofactor NAD+

column_label: PDF Table 4 row Hexanal has recombinant human ALDH1A1 Km=13.4 +/- 2.3 uM; 13.4 uM normalizes to 0.0134 mM.

raw_value_unit_evidence: Km raw_value=13.4 raw_unit=uM; SE=2.3 uM

row_label: Hexanal; recombinant human ALDH1A1

table_label: Table 4. Kinetic properties of recombinant human ALDH1A1


enzyme_display_name: benzaldehyde dehydrogenase (NADP+)

organism: Pseudomonas sp.

source_db: brenda

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

assay_conditions_summary: cofactor NADP+

proof_lines:
Pseudomonas strain K172
anaerobic toluene metabolism
benzyl alcohol dehydrogenase

enzyme: benzaldehyde dehydrogenase (NADP+)

source: brenda


smiles: CCCCCC(C=CC=O)O

assay_conditions_summary: pH 8; cofactor NAD+

column_label: PMC full-text paragraph P24 states a Km of 119.5 +/- 16.8 uM was determined for 4HNE; method paragraph P16 gives the assay conditions.

raw_value_unit_evidence: Km raw_value=119.5 raw_unit=uM uncertainty=+/-16.8 uM

row_label: Paragraph P24 4HNE metric sentence

table_label: PMC full-text prose section 3.5


enzyme_display_name: aldehyde dehydrogenase (NAD+)

substrate_name: octanal

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

proof_lines: pH and temperature not specified in the publication

enzyme: aldehyde dehydrogenase (NAD+)


substrate_name: Heptanal

smiles: CCCCCCC=O

proof_lines:
enzyme form ALDH-1, pH 9.5
enzyme form ALDH-2, pH 9.5

substrate: Heptanal


proof_lines:
enzyme ALDH-1
enzyme ALDH-2


substrate_name: m-methylbenzaldehyde

substrate: m-methylbenzaldehyde


substrate_name: benzaldehyde

assay_conditions_summary: pH 8.5; 298.15 K; buffer 0.1 M sodium diphosphate

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

substrate: benzaldehyde


substrate_name: m-methoxybenzaldehyde

substrate: m-methoxybenzaldehyde


substrate_name: p-nitrobenzaldehyde

substrate: p-nitrobenzaldehyde


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


substrate_name: hydrocinnamaldehyde

substrate: hydrocinnamaldehyde


substrate_name: alpha-phenylpropanal

substrate: alpha-phenylpropanal


substrate_name: phenylacetaldehyde

proof_lines:
enzyme ALDH-2
enzyme ALDH-1

substrate: phenylacetaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: betaine-aldehyde dehydrogenase

organism: Staphylococcus aureus

substrate_name: Betaine aldehyde

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

enzyme: betaine-aldehyde dehydrogenase

substrate: Betaine aldehyde


proof_lines: mutant enzyme H448F/Y450L, at pH 8.0 and 30°C


proof_lines: mutant enzyme H448F/P449M/Y450L, at pH 8.0 and 30°C


proof_lines: mutant enzyme P449M/Y450L, at pH 8.0 and 30°C


proof_lines: mutant enzyme H448F/P449M, at pH 8.0 and 30°C


proof_lines: mutant enzyme L161M7Q162M, at pH 8.0 and 30°C


substrate_name: NAD+

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

substrate: NAD+


organism: Lycium ruthenicum

proof_lines:
LrAMADH1
betaine aldehyde
BRENDA literature summary 763552


substrate_name: acetaldehyde (at 30 degrees Celsius)

substrate: acetaldehyde (at 30 degrees Celsius)


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

substrate_name: betaine aldehyde

column_label: Wiley prose reports recombinant maize ZmAMADH1 oxidizes betaine aldehyde with Km 14 uM; UniProt C0P9J6 maps to EMBL GQ184593, matching the Zea mays AMADH1a accession context.

raw_value_unit_evidence: Km raw_value=14 uM raw_unit=uM

row_label: recombinant ZmAMADH1 / GenBank GQ184593

table_label: PMID 21740525 Wiley prose: Analysis of betaine aldehyde dehydrogenase activity of PsAMADH2

enzyme: Aminoaldehyde dehydrogenase 1a

substrate: betaine aldehyde


organism: Bos taurus


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: glyceraldehyde 3-phosphate

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

substrate: glyceraldehyde 3-phosphate


substrate_name: Succinic semialdehyde

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

substrate: Succinic semialdehyde


substrate_name: malondialdehyde

substrate: malondialdehyde


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


substrate_name: glyceraldehyde

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

substrate: glyceraldehyde


substrate_name: propanal

smiles: CCC=O

substrate: propanal


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: pentanal

substrate: pentanal


substrate_name: Heptanal

substrate: Heptanal


substrate_name: Pyruvic aldehyde

smiles: CC(=O)C=O

substrate: Pyruvic aldehyde


substrate_name: p-Carboxybenzaldehyde

substrate: p-Carboxybenzaldehyde


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: formaldehyde

substrate: formaldehyde


substrate_name: crotonaldehyde

smiles: CC=CC=O

substrate: crotonaldehyde


substrate_name: Monochloroacetaldehyde

smiles: C(C=O)Cl

substrate: Monochloroacetaldehyde


substrate_name: Glyoxal

smiles: C(=O)C=O

substrate: Glyoxal


substrate_name: deamino-NAD+

substrate: deamino-NAD+


organism: Escherichia coli

substrate_name: NAD+

assay_conditions_summary: pH 7.7; cofactor NAD+

proof_lines:
pH 7.7, reaction with benzaldehyde
pH 7.7, reaction with isovaleraldehyde
pH 7.7, reaction with undecanal

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 7.7; cofactor NADP+

proof_lines:
pH 7.7, reaction with undecanal
pH 7.7, reaction with valeraldehyde
pH 7.7, reaction with isovaleraldehyde

substrate: NADP+


substrate_name: benzaldehyde

proof_lines:
pH 7.7, coenzyme NAD+
pH 7.7, coenzyme NADP+

substrate: benzaldehyde


substrate_name: Valeraldehyde

substrate: Valeraldehyde


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


substrate_name: p-nitrobenzaldehyde

substrate: p-nitrobenzaldehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: Undecanal

smiles: CCCCCCCCCCC=O

proof_lines:
pH 7.7, coenzyme NADP+
pH 7.7, coenzyme NAD+

substrate: Undecanal


substrate_name: methylglyoxal

substrate: methylglyoxal


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: glycolaldehyde

substrate: glycolaldehyde


substrate_name: D,L-glyceraldehyde

substrate: D,L-glyceraldehyde


substrate_name: phenyl acetaldehyde

substrate: phenyl acetaldehyde


enzyme_display_name: aldehyde dehydrogenase [NAD(P)+]

assay_conditions_summary: pH 7.4; buffer 25 mM Na-HEPES; cofactor NAD+

proof_lines: mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication

enzyme: aldehyde dehydrogenase [NAD(P)+]


substrate_name: Chloroacetaldehyde

assay_conditions_summary: pH 7.4; buffer 25 mM Na-HEPES

substrate: Chloroacetaldehyde


proof_lines: mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication


proof_lines: mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication


proof_lines: mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication


proof_lines: wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication


proof_lines:
native enzyme
phenobarbital-inducible enzyme
enzyme I from mitochondria


substrate_name: p-Methoxybenzaldehyde

substrate: p-Methoxybenzaldehyde


substrate_name: Butanal

substrate: Butanal


substrate_name: propanal

proof_lines:
native enzyme and mutant enzyme S74A
mutant enzyme S74A

substrate: propanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: Glutaraldehyde

smiles: C(CC=O)CC=O

substrate: Glutaraldehyde


substrate_name: formaldehyde

substrate: formaldehyde


substrate_name: NAD+

proof_lines: mutant enzyme S74A, reaction with propanal

substrate: NAD+


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


proof_lines:
enzyme ALDH-1
enzyme ALDH-2


substrate_name: o-methoxybenzaldehyde

substrate: o-methoxybenzaldehyde


substrate_name: p-nitrocinnamaldehyde

substrate: p-nitrocinnamaldehyde


assay_conditions_summary: pH 8.1; cofactor NAD+

proof_lines: apparent Km value, pyrophosphate buffer, pH 8.1, cofactor NAD+


substrate_name: m-hydroxybenzaldehyde

substrate: m-hydroxybenzaldehyde


substrate_name: o-nitrobenzaldehyde

substrate: o-nitrobenzaldehyde


substrate_name: p-(dimethylamino)cinnamaldehyde

proof_lines:
enzyme ALDH-2
enzyme ALDH-1

substrate: p-(dimethylamino)cinnamaldehyde


substrate_name: p-(dimethylamino)benzaldehyde

substrate: p-(dimethylamino)benzaldehyde


substrate_name: trans-cinnamaldehyde

substrate: trans-cinnamaldehyde


substrate_name: o-methylbenzaldehyde

substrate: o-methylbenzaldehyde


substrate_name: p-methylbenzaldehyde

substrate: p-methylbenzaldehyde


substrate_name: decanal

smiles: CCCCCCCCCC=O

proof_lines:
enzyme form ALDH-1, pH 9.5
enzyme form ALDH-2, pH 9.5

substrate: decanal


proof_lines:
enzyme ALDH-2
salivary ALDH


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


substrate_name: cinnamic aldehyde

substrate: cinnamic aldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


smiles: CCCC=CC=O


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: mutant enzyme E149T/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C

proof_lines: mutant enzyme E149T/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C

proof_lines: mutant enzyme E149T/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C


smiles: CCCCCCC=CC=O


substrate_name: hexanal

substrate: hexanal


proof_lines: mutant enzyme E149Q/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C


proof_lines: mutant enzyme E149D/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C


proof_lines: mutant enzyme E149N/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C


proof_lines: mutant enzyme I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C

proof_lines: mutant enzyme I200G, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C


proof_lines: wild type enzyme, with hexanal as cosubstrate, at pH 8.0 and 25°C

proof_lines: wild type enzyme, with nonanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C

proof_lines: wild type enzyme, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C


substrate_name: Nonanal

smiles: CCCCCCCCC=O

substrate: Nonanal


proof_lines: mutant enzyme I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C

proof_lines: mutant enzyme I200V, with hexanal as cosubstrate, in 100 mM sodium diphosphate, at pH 8.0 and 22°C


proof_lines: mutant enzyme E149Q/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C


proof_lines: mutant enzyme E149D/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C


proof_lines: mutant enzyme E149N/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C


proof_lines: mutant enzyme E149T/I200G, with hexanal as cosubstrate, at pH 8.0 and 25°C


organism: Sinorhizobium meliloti

substrate_name: phosphonoacetaldehyde

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: mutant enzyme R108A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C

substrate: phosphonoacetaldehyde


proof_lines: mutant enzyme R447A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C


proof_lines: mutant enzyme R290A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C


proof_lines: wild type enzyme, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C


substrate_name: NAD+

proof_lines: mutant enzyme R108A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C

substrate: NAD+


proof_lines: mutant enzyme R447A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C


proof_lines: wild type enzyme, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C

proof_lines: wild type enzyme, with glyceraldehyde-3-phosphate as cosubstrate, at pH 7.5 and 30°C


proof_lines: mutant enzyme R290A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


substrate_name: propionaldehyde

substrate: propionaldehyde


proof_lines: pH 7.5, 25°C, mutant enzyme ALDH1-H3tail


organism: Rhodococcus erythropolis

substrate_name: octanal

smiles: CCCCCCCC=O

assay_conditions_summary: pH 10; 310.15 K; buffer pH 10; cofactor NAD+

proof_lines: 1 mM NAD+, 0,05 mM substrate, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C

substrate: octanal


substrate_name: Butanal

substrate: Butanal


substrate_name: propanal

substrate: propanal


proof_lines: 0,05 mM propanal, 250 mM sodium bicarbonate-NaOH buffer pH 10.0, 37°C


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


organism: Arabidopsis thaliana

proof_lines: in 100 mM sodium diphosphate, at pH 8.0 and 22°C


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

substrate: dodecanal


smiles: CCCCCC(C=CC=O)O


smiles: CCC=O


organism: Pseudomonas aeruginosa


assay_conditions_summary: cofactor NAD+


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Homo sapiens

assay_conditions_summary: pH 8.5; buffer 0.1 M sodium diphosphate

proof_lines: in 0.1 M sodium diphosphate buffer (pH 8.5), at ambient temperature


proof_lines:
ALDH3A1, at pH 7.5 and 37°C
ALDH3A1,at pH 7.5 and 37°C


substrate_name: 3,4-dihydroxyphenyl acetaldehyde

substrate: 3,4-dihydroxyphenyl acetaldehyde


substrate_name: NADP+

substrate: NADP+


organism: Oryctolagus cuniculus


substrate_name: malondialdehyde

smiles: C(C=O)C=O

substrate: malondialdehyde


proof_lines:
pH 8.0, 25°C
microsomal enzyme


smiles: C(CC=O)CN


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


substrate_name: Unknown

substrate: Unknown


organism: Nocardia sp.


substrate_name: benzaldehyde

substrate: benzaldehyde


proof_lines: reaction with NAD+ or NADP+, enzyme from breast adenocarcinoma cell line

proof_lines: reaction with NADP+, enzyme from stomach mucosa

proof_lines: reaction with NAD+, enzyme from stomach mucosa


proof_lines: reaction with NAD+ or NADP+, enzyme from stomach mucosa


substrate_name: aldophosphamide

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

substrate: aldophosphamide


substrate_name: hexanal

substrate: hexanal


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


proof_lines: pH and temperature not specified in the publication


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


substrate_name: alpha-aminoadipate semialdehyde

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

substrate: alpha-aminoadipate semialdehyde


organism: Rattus norvegicus

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


proof_lines:
mitochondrial enzyme
cytoplasmic enzyme


substrate_name: NAD+

proof_lines:
cytoplasmic enzyme
mitochondrial enzyme

substrate: NAD+


assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


proof_lines: in 100 mM sodium diphosphate pH 8.0, at 22°C


smiles: C(CN)C=O


enzyme_display_name: glucose 1-dehydrogenase (PQQ, quinone)

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

proof_lines: recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C

enzyme: glucose 1-dehydrogenase (PQQ, quinone)


substrate_name: D-xylose

substrate: D-xylose


enzyme_display_name: glycerol-3-phosphate dehydrogenase

organism: Sus scrofa

substrate_name: coenzyme Q1

enzyme: glycerol-3-phosphate dehydrogenase

substrate: coenzyme Q1


organism: Acinetobacter calcoaceticus

substrate_name: lactose

proof_lines: recombinant cytochrome c-fusion protein, pH 7.0

substrate: lactose


substrate_name: melibiose

substrate: melibiose


proof_lines:
30°C, pH 8.0, cosubstrate NADP+
30°C, pH 8.0, cosubstrate NAD+


proof_lines:
30°C, pH 8.0
30°C, pH 8.0, cosubstrate NADP+
30°C, pH 8.0, cosubstrate NAD+


enzyme_display_name: malate dehydrogenase (quinone)

organism: Pseudomonas putida

substrate_name: ubiquinone 9

enzyme: malate dehydrogenase (quinone)

substrate: ubiquinone 9


substrate_name: (S)-malate

substrate: (S)-malate


substrate_name: 3-hydroxypropionic acid

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

assay_conditions_summary: pH 8; 310.15 K; buffer 50 mM potassium phosphate; cofactor NADH

proof_lines: with NADH as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C

substrate: 3-hydroxypropionic acid


smiles: C(CO)C=O

assay_conditions_summary: pH 8; 310.15 K; buffer 50 mM potassium phosphate; cofactor NADP+

proof_lines: with NADP+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C

proof_lines: with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C


substrate_name: acetaldehyde

assay_conditions_summary: pH 8; 310.15 K; buffer 50 mM potassium phosphate; cofactor NAD+

substrate: acetaldehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


enzyme_display_name: hydroxyacid-oxoacid transhydrogenase

enzyme: hydroxyacid-oxoacid transhydrogenase


enzyme_display_name: gluconate 2-dehydrogenase (acceptor)

organism: Klebsiella pneumoniae

substrate_name: D-gluconate

assay_conditions_summary: pH 6

proof_lines:
pH 6
pH 4

enzyme: gluconate 2-dehydrogenase (acceptor)

substrate: D-gluconate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: glycolate dehydrogenase

substrate_name: glycolate

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

enzyme: glycolate dehydrogenase

substrate: glycolate


substrate_name: D(-)-lactate

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

substrate: D(-)-lactate


organism: Saccharomyces cerevisiae

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


substrate_name: pyruvate

substrate: pyruvate


smiles: CCCCCC(C=CC=O)O

assay_conditions_summary: pH 7.4; 310.15 K; buffer 40 mM sodium phosphate

proof_lines: ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C


smiles: CC=O

proof_lines: ALDH5A, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C


substrate_name: alpha-aminoadipate semialdehyde

proof_lines: pH 8.0, 26°C, recombinant wild-type enzyme

substrate: alpha-aminoadipate semialdehyde


organism: Ovis aries

substrate_name: Butanal

substrate: Butanal


substrate_name: propanal

smiles: CCC=O

substrate: propanal


organism: Acetivibrio thermocellus


substrate_name: NADH

assay_conditions_summary: pH 7; 328.15 K; cofactor NADH

substrate: NADH


substrate_name: glyceraldehyde 3-phosphate

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

substrate: glyceraldehyde 3-phosphate


substrate_name: 3-oxopropyl phosphonate

substrate: 3-oxopropyl phosphonate


organism: Danio rerio

proof_lines: 0.1 M sodium diphosphate pH 8.0, 1 mM NAD+, 50 mM 2-mercaptoethanol, 1 mM pyrazole, 30 min, 25°C


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

proof_lines:
enzyme from liver
enzyme from brain
minor component of enzyme E3, pH 7.4


smiles: CC(=O)NCCCC(=O)[O-]


proof_lines:
mutant enzyme E487K, pH 7.4
mutant enzyme E487K, pH 9.0


substrate_name: NAD+

assay_conditions_summary: pH 7.4; cofactor NAD+

substrate: NAD+


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


substrate_name: malondialdehyde

smiles: C(C=O)C=O

substrate: malondialdehyde


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

substrate: dodecanal


substrate_name: Heptanal

smiles: CCCCCCC=O

substrate: Heptanal


organism: Escherichia coli

substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


assay_conditions_summary: pH 7.7; 298.15 K; cofactor NAD+


substrate_name: Isobutanal

smiles: CC(C)C=O

substrate: Isobutanal


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


organism: Sinorhizobium meliloti

substrate_name: phosphonoacetaldehyde

substrate: phosphonoacetaldehyde


substrate_name: Unknown

proof_lines:
at 22°C and pH 7.8
pH 8.5, 37°C

substrate: Unknown


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: H2O; NAD+; Betaine aldehyde

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

substrate: H2O; NAD+; Betaine aldehyde


substrate_name: glycine betaine aldehyde

assay_conditions_summary: pH 7.5; 293.15 K; cofactor NADP+

proof_lines: pH 7.5, 20°C, native betaine-aldehyde dehydrogenase or betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein

substrate: glycine betaine aldehyde


assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

proof_lines: mutant S82A/D80G of isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


substrate_name: Succinic semialdehyde

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

substrate: Succinic semialdehyde


substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


organism: Streptococcus pneumoniae

substrate_name: D-ribulose 5-phosphate

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

substrate: D-ribulose 5-phosphate


enzyme_display_name: L-galactonate 5-dehydrogenase

substrate_name: L-galactonate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication, recombinant enzyme

enzyme: L-galactonate 5-dehydrogenase

substrate: L-galactonate


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

substrate_name: L-lactate

proof_lines: H373Q mutant enzyme with 2,6-dichloroindophenol as electron acceptor

enzyme: L-lactate dehydrogenase (cytochrome)

substrate: L-lactate


proof_lines: mutant Y254L with R289 distal, pH 7.0, 30°C


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: D-lactate dehydrogenase (cytochrome)

organism: Stutzerimonas stutzeri

substrate_name: (R)-lactate

enzyme: D-lactate dehydrogenase (cytochrome)

substrate: (R)-lactate


organism: Nitratidesulfovibrio vulgaris

substrate_name: D-lactate

substrate: D-lactate


organism: Bradyrhizobium sp.

substrate_name: methanol

smiles: CO

proof_lines: pH and temperature not specified in the publication, lanthanide: Ce3+

substrate: methanol


enzyme_display_name: L-threonate 2-dehydrogenase

organism: Cupriavidus necator

substrate_name: L-threonate

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines:
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NAD+, pH 8.0, 25°C

enzyme: L-threonate 2-dehydrogenase

substrate: L-threonate


substrate_name: ferricytochrome c

proof_lines: pH 7.5, 25°C, recombinantly expressed flavocytochrome b2 flavin-binding domain

substrate: ferricytochrome c


substrate_name: cytochrome c

substrate: cytochrome c


enzyme_display_name: glucose oxidase

organism: Aspergillus niger

proof_lines:
pH 7.3, 30°C
native enzyme, pH 6.5, 70°C

enzyme: glucose oxidase


substrate_name: beta-D-glucose

proof_lines: mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication

proof_lines: mutant H447C, pH and temperature not specified in the publication

substrate: beta-D-glucose


organism: Aspergillus tubingensis


proof_lines: recombinant enzyme mutant B11 in fusion with Aga2, pH 5.5, 25°C

proof_lines: recombinant enzyme mutant B11, pH 5.5, 25°C

proof_lines: recombinant mutant M12 enzyme expressed in Saccharomyces cerevisiae, pH 5.5, 25°C


smiles: O=O

proof_lines:
periodate-oxidized enzyme
native enzyme


organism: Eggerthella lenta


assay_conditions_summary: pH 5; 323.15 K; buffer pH 7


organism: Penicillium chrysogenum

assay_conditions_summary: pH 5.4; 318.15 K; buffer 50 mM sodium acetate

proof_lines: in 50 mM sodium acetate buffer (pH 5.4). at 45°C


enzyme_display_name: cholesterol oxidase

organism: Rhodococcus erythropolis

substrate_name: cholesterol

proof_lines: pH and temperature not specified in the publication

enzyme: cholesterol oxidase

substrate: cholesterol


proof_lines: wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication

proof_lines: recombinant wild-type enzyme in fusion with Aga2, pH 5.5, 25°C


organism: Streptomyces sp. SA-COO


organism: Nocardia sp.

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


organism: Chromobacterium sp. DS-1


organism: Pseudomonas sp.


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


organism: Chromobacterium sp. DS1


organism: Streptomyces rimosus


organism: Pseudomonas fluorescens

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

proof_lines: apparent value, free enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30°C

proof_lines: apparent value, silk mat-immobilized enzyme, in 50 mM potassium phosphate buffer, pH 7.5, 30°C


organism: Streptomyces sp. AKHSS


organism: Streptomyces sp.


organism: Chromobacterium sp.


enzyme_display_name: galactose oxidase

organism: Fusarium sp.

substrate_name: Unknown

enzyme: galactose oxidase

substrate: Unknown


enzyme_display_name: L-gulonolactone oxidase

organism: Arabidopsis thaliana

proof_lines:
at pH 8.0 and 25°C
at pH and 25°C

enzyme: L-gulonolactone oxidase


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

organism: Ricinus communis

substrate_name: glycolate

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

proof_lines: pH 7.5, temperature not specified in the publication

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

substrate: glycolate


organism: Glycine max


organism: Gallus gallus


substrate_name: L-2-hydroxy-4-methylthiobutanoic acid

proof_lines: decreasing values as the number of carbons in the alkyl side chain increases from 1 to 2 and to 5

substrate: L-2-hydroxy-4-methylthiobutanoic acid


organism: Zea mays

proof_lines:
mesophyll cell enzyme
bundle sheath cell enzyme


organism: Sus scrofa

substrate_name: dichlorophenolindophenol

proof_lines:
cosubstrate: glycolate
long chain oxidase
non-competitive, glycolate oxidation

substrate: dichlorophenolindophenol


enzyme_display_name: glycerol-3-phosphate oxidase

organism: Enterococcus faecalis

substrate_name: sn-glycerol 3-phosphate

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

enzyme: glycerol-3-phosphate oxidase

substrate: sn-glycerol 3-phosphate


organism: Enterococcus faecium


organism: Gluconobacter oxydans

substrate_name: D-glucose

proof_lines: recombinant Strep-tagged enzyme, pH 6.0, 25°C

substrate: D-glucose


organism: Acinetobacter calcoaceticus

proof_lines: recombinant cytochrome c-fusion protein, pH 7.0

proof_lines: pH 8.5, reaction with 2,6-dichlorophenolindophenol as electron acceptor


substrate_name: maltose

proof_lines: recombinant triple mutant enzyme, pH 7.0, 25°C

proof_lines: recombinant Arg-tagged enzyme, and recombinant chimeric mutant enzyme, pH 7.0

substrate: maltose


organism: Escherichia coli

substrate_name: glycerol 3-phosphate

assay_conditions_summary: cofactor FMN

proof_lines: with phenazine methosulfate coupled with 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide as electron acceptor

substrate: glycerol 3-phosphate


organism: Rattus norvegicus

proof_lines: enzyme from testis and pancreatic islets, in presence of saturating concentrations of free Ca2+

proof_lines: enzyme from pancreatic islets, in absence of free calcium

proof_lines: enzyme from testis in absence of free calcium


organism: Pseudomonas putida

substrate_name: vitamin K3

substrate: vitamin K3


enzyme_display_name: D-lactate dehydrogenase (quinone)

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

proof_lines:
presence of Triton X-100, pH 7.8, 25°C
pH 7.8, 25°C

enzyme: D-lactate dehydrogenase (quinone)


substrate_name: (R)-lactate

proof_lines:
pH 8.0, 23°C
presence of Triton X-100, pH 8.0, 23°C
presence of cyanide, pH 8.0, 23°C

substrate: (R)-lactate


enzyme_display_name: glucose 1-dehydrogenase (PQQ, quinone)

substrate_name: pyrroloquinoline quinone

enzyme: glucose 1-dehydrogenase (PQQ, quinone)

substrate: pyrroloquinoline quinone


enzyme_display_name: choline dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: phenazine methosulfate

enzyme: choline dehydrogenase

substrate: phenazine methosulfate


enzyme_display_name: L-2-hydroxyglutarate dehydrogenase

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

enzyme: L-2-hydroxyglutarate dehydrogenase


substrate_name: choline

smiles: C[N+](C)(C)CCO

proof_lines: in the presence of 0.05 mM phenazine methosulfate

substrate: choline


organism: Homo sapiens

substrate_name: NAD+

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+

substrate: NAD+


organism: Pseudomonas fluorescens

substrate_name: D-gluconate

substrate: D-gluconate


enzyme_display_name: aldehyde dehydrogenase (NAD+)

substrate_name: benzaldehyde

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADP+

proof_lines: at 25°C and pH 8.5, with NADP+ as the electron acceptor

proof_lines: at 25°C and pH 8.5, with NAD+ as the electron acceptor

enzyme: aldehyde dehydrogenase (NAD+)

substrate: benzaldehyde


enzyme_display_name: D-2-hydroxyglutarate dehydrogenase

enzyme: D-2-hydroxyglutarate dehydrogenase


organism: Stutzerimonas stutzeri


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


enzyme_display_name: (S)-2-hydroxyglutarate dehydrogenase

enzyme: (S)-2-hydroxyglutarate dehydrogenase


enzyme_display_name: gluconate 2-dehydrogenase (acceptor)

organism: Serratia marcescens

enzyme: gluconate 2-dehydrogenase (acceptor)


organism: Bos taurus

assay_conditions_summary: cofactor NAD+


substrate_name: decanal

substrate: decanal


substrate_name: propanal

smiles: CCC=O

substrate: propanal


organism: Arabidopsis thaliana

proof_lines: 25°C, pH 8.75, cofactor oxidized 2,6-dichlorophenolindophenol


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines: reaction with benzaldehyde, enzyme II from microsomes

proof_lines: reaction with benzaldehyde, enzyme II from mitochondria

proof_lines: reaction with benzaldehyde, enzyme I from microsomes

substrate: NADP+


substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

proof_lines: in the absence of Alda-1, at pH 7.4 and 25°C

proof_lines: in the presence of 0.01 mM Alda-1, at pH 7.4 and 25°C

substrate: NADH


substrate_name: cytochrome c

substrate: cytochrome c


substrate_name: all-trans-retinal

substrate: all-trans-retinal


assay_conditions_summary: pH 6

proof_lines:
pH 6
pH 5.0


substrate_name: glyceraldehyde

proof_lines: pH and temperature not specified in the publication

substrate: glyceraldehyde


enzyme_display_name: betaine-aldehyde dehydrogenase

substrate_name: Betaine aldehyde

proof_lines:
mitochondrial enzyme
cytoplasmic enzyme

enzyme: betaine-aldehyde dehydrogenase

substrate: Betaine aldehyde


substrate_name: Unknown

proof_lines:
versus betaine aldehyde
versus NAD+

substrate: Unknown


enzyme_display_name: GDP-L-fucose synthase

substrate_name: NADH; GDP-4-dehydro-D-rhamnose; H+

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

assay_conditions_summary: cofactor NADH

enzyme: GDP-L-fucose synthase

substrate: NADH; GDP-4-dehydro-D-rhamnose; H+


organism: Staphylococcus aureus

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

assay_conditions_summary: cofactor NADPH

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


organism: Brassica rapa subsp. chinensis

substrate_name: O2; Glycolate

substrate: O2; Glycolate


organism: Zea mays


organism: Enterococcus faecalis

substrate_name: sn-Glycerol 3-phosphate; O2

substrate: sn-Glycerol 3-phosphate; O2


substrate_name: O2; Choline

substrate: O2; Choline


organism: Mus musculus

substrate_name: NAD+; H2O; Acetaldehyde

substrate: NAD+; H2O; Acetaldehyde


organism: Oryctolagus cuniculus

substrate_name: Propanal; NAD+; H2O

substrate: Propanal; NAD+; H2O


organism: Ovis aries

substrate_name: Propanal; H2O; NAD+

substrate: Propanal; H2O; NAD+


substrate_name: H2O; Acetaldehyde; NAD+

substrate: H2O; Acetaldehyde; NAD+


organism: Capra hircus

substrate_name: H2O; NAD+; D-Lactaldehyde

substrate: H2O; NAD+; D-Lactaldehyde


organism: Rattus norvegicus

substrate_name: H2O; NAD+; Betaine aldehyde

substrate: H2O; NAD+; Betaine aldehyde


substrate_name: n-nonanal

smiles: CCCCCCCCC=O

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

substrate: n-nonanal


enzyme_display_name: sn-glycerol-1-phosphate dehydrogenase

organism: Sulfolobus tokodaii

substrate_name: Glycerone phosphate; H+; NADPH

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

enzyme: sn-glycerol-1-phosphate dehydrogenase

substrate: Glycerone phosphate; H+; NADPH


organism: Aeropyrum pernix

substrate_name: NADH; Glycerone phosphate; H+

substrate: NADH; Glycerone phosphate; H+


organism: Methanothermobacter thermautotrophicus

substrate_name: Glycerone phosphate; H+; NADH

sequence_source: multiple

substrate: Glycerone phosphate; H+; NADH


organism: Bacillus subtilis

substrate_name: H+; Glycerone phosphate; NADH

substrate: H+; Glycerone phosphate; NADH


organism: Escherichia coli (strain K12)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 1,5-anhydro-D-fructose reductase

substrate_name: NADPH; 1,5-Anhydro-D-fructose

enzyme: 1,5-anhydro-D-fructose reductase

substrate: NADPH; 1,5-Anhydro-D-fructose


organism: Homo sapiens

substrate_name: NADPH; 9,10-Phenanthroquinone; H+

substrate: NADPH; 9,10-Phenanthroquinone; H+


organism: Escherichia coli

substrate_name: 1-Deoxy-D-xylulose 5-phosphate; H+; NADPH

proof_lines: Measured in the presence of manganese ions.


organism: Synechocystis sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W204F to reconstruct the assayed variant sequence.


organism: Yersinia pestis


proof_lines: pH 7.8, 37°C, recombinant wild-type enzyme


organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)


enzyme_display_name: 2-(R)-hydroxypropyl-CoM dehydrogenase

organism: Xanthobacter autotrophicus

proof_lines: competitive inhibition with respect to 2-(R)-hydroxypropyl-CoM

proof_lines: pH and temperature not specified in the publication, versus (2R)-2-hydroxypropyl-CoM

source_databases_merged: brenda uniprot

enzyme: 2-(R)-hydroxypropyl-CoM dehydrogenase


enzyme_display_name: 2-(S)-hydroxypropyl-CoM dehydrogenase 3

organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)

substrate_name: S-HPC

proof_lines: kcat is 5.5 sec(-1) with R-HPC as substrate. kcat is 25 sec(-1) with S-HPC as substrate. kcat is 11 sec(-1) with 2-KPC as substrate. kcat is 0.044 sec(-1) with 2-butanone as substrate. kcat is 2.0 sec(-1) with 2-propanol as substrate. kcat

enzyme: 2-(S)-hydroxypropyl-CoM dehydrogenase 3

substrate: S-HPC


enzyme_display_name: 2-(S)-hydroxypropyl-CoM dehydrogenase 1

proof_lines: kcat is 28 sec(-1) with S-HPC as substrate. kcat is 20 sec(-1) with 2-KPC as substrate. kcat is 2.4 sec(-1) with R-HPC as substrate.

enzyme: 2-(S)-hydroxypropyl-CoM dehydrogenase 1


enzyme_display_name: 3beta-hydroxysteroid 3-dehydrogenase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M304S with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

enzyme: 3beta-hydroxysteroid 3-dehydrogenase


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

substrate_name: 5-alpha-androstan-3-beta-ol-17-one (at 37 degrees Celsius)


enzyme_display_name: Aldo-keto reductase family 1 member C1

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

enzyme: Aldo-keto reductase family 1 member C1


enzyme_display_name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1

substrate_name: dehydroepiandrosterone (in the presence of NAD(+))


enzyme_display_name: 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7

organism: Mus musculus


substrate_name: H+; NADPH; GDP-4-dehydro-D-rhamnose

substrate: H+; NADPH; GDP-4-dehydro-D-rhamnose


enzyme_display_name: (R)-2-hydroxyacid dehydrogenase

organism: Methanocaldococcus jannaschii

substrate_name: NADH; 3-Sulfopyruvate

enzyme: (R)-2-hydroxyacid dehydrogenase

substrate: NADH; 3-Sulfopyruvate


substrate_name: 3-Sulfopyruvate; NADH

substrate: 3-Sulfopyruvate; NADH


organism: Methanothermus fervidus


organism: Halobacterium mediterranei

substrate_name: 3-Methyl-2-oxopentanoate; NADPH; H+

substrate: 3-Methyl-2-oxopentanoate; NADPH; H+


organism: Corynebacterium sp.


enzyme_display_name: xanthoxin dehydrogenase

organism: Arabidopsis thaliana

substrate_name: Xanthoxin; NAD+

proof_lines: no activity with xanthoxic acid, ethanol, isopropanol, butanol, cyclohexanol and 2,6-dimethylcyclohexanol.

enzyme: xanthoxin dehydrogenase

substrate: Xanthoxin; NAD+


enzyme_display_name: Sorbose reductase SOU1

organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

enzyme: Sorbose reductase SOU1


enzyme_display_name: 2-hydroxymethylglutarate dehydrogenase

organism: Eubacterium barkeri

substrate_name: NAD+; (S)-2-(Hydroxymethyl)glutarate

enzyme: 2-hydroxymethylglutarate dehydrogenase

substrate: NAD+; (S)-2-(Hydroxymethyl)glutarate


organism: Ensifer adhaerens


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase YdfG

organism: Escherichia coli (strain K12)

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

assay_conditions_summary: pH 9

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


enzyme_display_name: malate dehydrogenase [NAD(P)+]

organism: Methanothermobacter thermautotrophicus

substrate_name: NAD+; L-Malate

enzyme: malate dehydrogenase [NAD(P)+]

substrate: NAD+; L-Malate


enzyme_display_name: Malate dehydrogenase

organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

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

proof_lines: kcat is 2.6 sec(-1) for NAD-dependent malate oxidation. kcat is 1.4 sec(-1) for NADP-dependent malate oxidation.

enzyme: Malate dehydrogenase

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


enzyme_display_name: Aldo-keto reductase family 1 member B15

organism: Homo sapiens

substrate_name: 3-alpha,17-beta-androstandiol (tested with isoform 1 in the oxidative reaction)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 min(-1) using isoform 1 for the reduction of androsterone. kcat is 1.1 min(-1) using isoform 1 for the reduction of delta-4-androstenedione. kcat is 1.0 min(-1) using isoform 1 for the reduction of estrone. kcat is 0.5 min(-1) u

enzyme: Aldo-keto reductase family 1 member B15


enzyme_display_name: Retinol dehydrogenase 14

substrate_name: Unknown

proof_lines: Vmax is measured per mg microsomal protein.

enzyme: Retinol dehydrogenase 14


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

substrate_name: GS-acrolein

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


enzyme_display_name: Retinol dehydrogenase 13

enzyme: Retinol dehydrogenase 13


enzyme_display_name: Retinol dehydrogenase 11

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+

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

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


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

substrate: D-xylose


organism: Scheffersomyces stipitis

substrate_name: NAD(P)+

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

substrate: NAD(P)+


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

substrate: Unknown


substrate_name: cyclohexanecarboxaldehyde

substrate: cyclohexanecarboxaldehyde


substrate_name: NADH

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

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADPH

substrate: NADPH


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

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

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


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

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q7NQL0

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.


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+

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

substrate: Unknown


enzyme_display_name: D-chiro-inositol 1-dehydrogenase

organism: Bacillus subtilis

substrate_name: D-chiro-Inositol; NAD+

assay_conditions_summary: cofactor 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

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)


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.


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+

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.

substrate: Unknown


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


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

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

enzyme: methanol dehydrogenase (cytochrome c)

substrate: Methanol; Phenazine ethosulfate


enzyme_display_name: alcohol dehydrogenase (cytochrome c)

substrate_name: Methanol; PQQ

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

substrate: Unknown


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


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


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

substrate: Unknown


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

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

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


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)

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