column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / 4-hydroxynonenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 4-hydroxynonenal Km raw_value=21 raw_unit=uM

row_label: ALDH3I1 / 4-hydroxynonenal


enzyme_display_name: Aldehyde dehydrogenase family 3 member I1, chloroplastic

organism: Arabidopsis thaliana

substrate_name: NAD(+) (in the presence of hexanal as co-substrate)

source_db: uniprot

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.

assay_conditions_summary: cofactor NADP+

data_origin: experimental

source: uniprot


substrate_name: NADP(+) (in the presence of hexanal as co-substrate)

enzyme: Aldehyde dehydrogenase family 3 member I1, chloroplastic


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

substrate_name: NAD(+) with 3-aminopropanal as substrate

verification_status: verified

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Table 4; row NAD +; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.091 mM converted from 91 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / NAD + Km 91 +/- 4 uM

row_label: ZmAMADH1a / NAD +

table_label: Table 4

enzyme: Aminoaldehyde dehydrogenase 1a

status: verified


enzyme_display_name: aldehyde dehydrogenase (NAD(+))

organism: Homo sapiens

substrate_name: propanal

source_db: oed

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E399Q with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.

smiles: CCC=O

mutation_type: substitution

enzyme: aldehyde dehydrogenase (NAD(+))

substrate: propanal

status: unverified

source: oed


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E399D with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.

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 E399H with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


kcat_over_km_origin: calculated

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K192E with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K192Q with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


proof_lines:
E399D
propionaldehyde
aliphatic aldehydes


proof_lines:
E399H/D
aliphatic aldehydes
deacylation


enzyme_display_name: Aminoaldehyde dehydrogenase 1b

column_label: Table 4; row NAD +; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.079 mM converted from 79 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / NAD + Km 79 +/- 6 uM

row_label: ZmAMADH1b / NAD +

enzyme: Aminoaldehyde dehydrogenase 1b

substrate: NAD(+) with 3-aminopropanal as substrate


substrate_name: nonanal

smiles: CCCCCCCCC=O

column_label: Table 1; row Nonanal; Km column

normalized_value_unit_evidence: Km=0.0285 mM converted from 28.5 uM

raw_value_unit_evidence: Table 1 Nonanal Km 28.5 +/- 4.8 uM

row_label: Nonanal

table_label: Table 1

substrate: nonanal


smiles: CCCCCCC=CC=O

column_label: Table 1; row trans-2-Nonenal; Km column

normalized_value_unit_evidence: Km=0.0053 mM converted from 5.3 uM

raw_value_unit_evidence: Table 1 trans-2-Nonenal Km 5.3 +/- 0.7 uM


substrate_name: hexanal

smiles: CCCCCC=O

column_label: Table 1; row Hexanal; Km column

normalized_value_unit_evidence: Km=0.0391 mM converted from 39.1 uM

raw_value_unit_evidence: Table 1 Hexanal Km 39.1 +/- 3.9 uM

row_label: Hexanal

substrate: hexanal


substrate_name: octanal

smiles: CCCCCCCC=O

column_label: Table 1; row Octanal; Km column

normalized_value_unit_evidence: Km=0.0175 mM converted from 17.5 uM

raw_value_unit_evidence: Table 1 Octanal Km 17.5 +/- 2.1 uM

row_label: Octanal

substrate: octanal


substrate_name: betaine aldehyde

column_label: Table 1; row Betaine aldehyde; Km column

normalized_value_unit_evidence: Km=0.0411 mM converted from 41.1 uM

raw_value_unit_evidence: Table 1 Betaine aldehyde Km 41.1 +/- 9.3 uM

row_label: Betaine aldehyde

substrate: betaine aldehyde


substrate_name: L-2-aminoadipate 6-semialdehyde

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

column_label: Table 1; row AASA; Km column

normalized_value_unit_evidence: Km=0.169 mM converted from 169 uM

raw_value_unit_evidence: Table 1 AASA Km 169 +/- 9.5 uM

row_label: AASA

substrate: L-2-aminoadipate 6-semialdehyde


substrate_name: benzaldehyde

column_label: Table 1; row Benzaldehyde; Km column

normalized_value_unit_evidence: Km=0.5302 mM converted from 530.2 uM

raw_value_unit_evidence: Table 1 Benzaldehyde Km 530.2 +/- 86.3 uM

row_label: Benzaldehyde

substrate: benzaldehyde


column_label: Table 1; row Propanal; Km column

normalized_value_unit_evidence: Km=0.6474 mM converted from 647.4 uM

raw_value_unit_evidence: Table 1 Propanal Km 647.4 +/- 38.5 uM

row_label: Propanal


substrate_name: glyceraldehyde

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

column_label: Table 1; row Glyceraldehyde; Km column

normalized_value_unit_evidence: Km=7.3743 mM converted from 7374.3 uM

raw_value_unit_evidence: Table 1 Glyceraldehyde Km 7374.3 +/- 117.2 uM

row_label: Glyceraldehyde

substrate: glyceraldehyde


organism: Bacillus subtilis

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADP+

column_label: Table 3. Kinetic parameters of ycbD protein for aliphatic aldehyde substrates in the presence of NADP+; row Octylaldehyde (C8); columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0352 ± 0.0067 mM | kcat 0.97 ± 0.09 s^-1 | kcat/Km 28.2 ± 3.3 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.97 normalized_unit=s^-1; Km normalized_value=0.035 normalized_unit=mM; kcat/Km normalized_value=27.71428571428571 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.97 ± 0.09 raw_unit=s^-1; Km raw_value=0.0352 ± 0.0067 raw_unit=mM; kcat/Km raw_value=28.2 ± 3.3 raw_unit=s^-1*mM^-1

row_label: Octylaldehyde (C8)


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

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+

column_label: Table 1. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for alphaKGSA; row ycbD / NAD+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0104 ± 0.0009 mM | kcat 2.75 ± 0.15 s^-1 | kcat/Km 265 ± 10 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=2.75 normalized_unit=s^-1; Km normalized_value=0.01 normalized_unit=mM; kcat/Km normalized_value=275 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2.75 ± 0.15 raw_unit=s^-1; Km raw_value=0.0104 ± 0.0009 raw_unit=mM; kcat/Km raw_value=265 ± 10 raw_unit=s^-1*mM^-1

row_label: ycbD / NAD+


substrate_name: Butanal

smiles: CCCC=O

column_label: Table 3. Kinetic parameters of ycbD protein for aliphatic aldehyde substrates in the presence of NADP+; row Butylaldehyde (C4); columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.170 ± 0.036 mM | kcat 1.35 ± 0.18 s^-1 | kcat/Km 8.0 ± 0.6 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.35 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM; kcat/Km normalized_value=7.9411764705882355 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.35 ± 0.18 raw_unit=s^-1; Km raw_value=0.170 ± 0.036 raw_unit=mM; kcat/Km raw_value=8.0 ± 0.6 raw_unit=s^-1*mM^-1

row_label: Butylaldehyde (C4)

substrate: Butanal


substrate_name: Heptanal

smiles: CCCCCCC=O

column_label: Table 3. Kinetic parameters of ycbD protein for aliphatic aldehyde substrates in the presence of NADP+; row Heptalaldehyde (C7); columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0393 ± 0.0052 mM | kcat 0.87 ± 0.04 s^-1 | kcat/Km 22.3 ± 1.9 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.87 normalized_unit=s^-1; Km normalized_value=0.039 normalized_unit=mM; kcat/Km normalized_value=22.307692307692307 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.87 ± 0.04 raw_unit=s^-1; Km raw_value=0.0393 ± 0.0052 raw_unit=mM; kcat/Km raw_value=22.3 ± 1.9 raw_unit=s^-1*mM^-1

row_label: Heptalaldehyde (C7)

substrate: Heptanal


substrate_name: Hexanal

column_label: Table 3. Kinetic parameters of ycbD protein for aliphatic aldehyde substrates in the presence of NADP+; row Hexylaldehyde (C6); columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0814 ± 0.0257 mM | kcat 1.47 ± 0.23 s^-1 | kcat/Km 18.8 ± 2.6 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.47 normalized_unit=s^-1; Km normalized_value=0.081 normalized_unit=mM; kcat/Km normalized_value=18.14814814814815 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.47 ± 0.23 raw_unit=s^-1; Km raw_value=0.0814 ± 0.0257 raw_unit=mM; kcat/Km raw_value=18.8 ± 2.6 raw_unit=s^-1*mM^-1

row_label: Hexylaldehyde (C6)

substrate: Hexanal


column_label: Table 2. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for NAD+ and NADP+; row ycbD / NAD+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.5569 ± 0.0437 mM | kcat 0.74 ± 0.06 s^-1 | kcat/Km 1.44 ± 0.01 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.74 normalized_unit=s^-1; Km normalized_value=0.557 normalized_unit=mM; kcat/Km normalized_value=1.3285457809694792 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.74 ± 0.06 raw_unit=s^-1; Km raw_value=0.5569 ± 0.0437 raw_unit=mM; kcat/Km raw_value=1.44 ± 0.01 raw_unit=s^-1*mM^-1


substrate_name: NADP+

column_label: Table 2. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for NAD+ and NADP+; row ycbD / NADP+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0940 ± 0.0026 mM | kcat 1.08 ± 0.02 s^-1 | kcat/Km 11.5 ± 0.1 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.08 normalized_unit=s^-1; Km normalized_value=0.094 normalized_unit=mM; kcat/Km normalized_value=11.48936170212766 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.08 ± 0.02 raw_unit=s^-1; Km raw_value=0.0940 ± 0.0026 raw_unit=mM; kcat/Km raw_value=11.5 ± 0.1 raw_unit=s^-1*mM^-1

row_label: ycbD / NADP+

substrate: NADP+


substrate_name: Pentanal

smiles: CCCCC=O

column_label: Table 3. Kinetic parameters of ycbD protein for aliphatic aldehyde substrates in the presence of NADP+; row Valeraldehyde (C5); columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.145 ± 0.012 mM | kcat 2.10 ± 0.13 s^-1 | kcat/Km 14.5 ± 0.3 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=2.1 normalized_unit=s^-1; Km normalized_value=0.145 normalized_unit=mM; kcat/Km normalized_value=14.482758620689657 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2.10 ± 0.13 raw_unit=s^-1; Km raw_value=0.145 ± 0.012 raw_unit=mM; kcat/Km raw_value=14.5 ± 0.3 raw_unit=s^-1*mM^-1

row_label: Valeraldehyde (C5)

substrate: Pentanal


column_label: Table 3. Kinetic parameters of ycbD protein for aliphatic aldehyde substrates in the presence of NADP+; row Propionaldehyde (C3); columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 1.46 ± 0.25 mM | kcat 1.29 ± 0.13 s^-1 | kcat/Km 0.89 ± 0.08 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.29 normalized_unit=s^-1; Km normalized_value=1.46 normalized_unit=mM; kcat/Km normalized_value=0.8835616438356165 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.29 ± 0.13 raw_unit=s^-1; Km raw_value=1.46 ± 0.25 raw_unit=mM; kcat/Km raw_value=0.89 ± 0.08 raw_unit=s^-1*mM^-1

row_label: Propionaldehyde (C3)


enzyme_display_name: UniProt P49189

source_db: skid

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

sequence_source: multiple

source_databases_merged: skid uniprot

enzyme: UniProt P49189

source: skid


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: butyraldehyde

substrate: butyraldehyde


substrate_name: hexanaldehyde

substrate: hexanaldehyde


substrate_name: propanal

substrate: propanal


substrate_name: nonanal

column_label: Table 1; row Nonanal; Km column

normalized_value_unit_evidence: Km=0.0285 mM converted from 28.5 uM

raw_value_unit_evidence: Table 1 Nonanal Km 28.5 +/- 4.8 uM

substrate: nonanal


column_label: Table 1; row trans-2-Nonenal; Km column

normalized_value_unit_evidence: Km=0.0053 mM converted from 5.3 uM

raw_value_unit_evidence: Table 1 trans-2-Nonenal Km 5.3 +/- 0.7 uM


substrate_name: hexanal

column_label: Table 1; row Hexanal; Km column

normalized_value_unit_evidence: Km=0.0391 mM converted from 39.1 uM

raw_value_unit_evidence: Table 1 Hexanal Km 39.1 +/- 3.9 uM

substrate: hexanal


substrate_name: octanal

column_label: Table 1; row Octanal; Km column

normalized_value_unit_evidence: Km=0.0175 mM converted from 17.5 uM

raw_value_unit_evidence: Table 1 Octanal Km 17.5 +/- 2.1 uM

substrate: octanal


substrate_name: betaine aldehyde

column_label: Table 1; row Betaine aldehyde; Km column

normalized_value_unit_evidence: Km=0.0411 mM converted from 41.1 uM

raw_value_unit_evidence: Table 1 Betaine aldehyde Km 41.1 +/- 9.3 uM

substrate: betaine aldehyde


substrate_name: L-2-aminoadipate 6-semialdehyde

column_label: Table 1; row AASA; Km column

normalized_value_unit_evidence: Km=0.169 mM converted from 169 uM

raw_value_unit_evidence: Table 1 AASA Km 169 +/- 9.5 uM

substrate: L-2-aminoadipate 6-semialdehyde


substrate_name: benzaldehyde

column_label: Table 1; row Benzaldehyde; Km column

normalized_value_unit_evidence: Km=0.5302 mM converted from 530.2 uM

raw_value_unit_evidence: Table 1 Benzaldehyde Km 530.2 +/- 86.3 uM

substrate: benzaldehyde


column_label: Table 1; row Propanal; Km column

normalized_value_unit_evidence: Km=0.6474 mM converted from 647.4 uM

raw_value_unit_evidence: Table 1 Propanal Km 647.4 +/- 38.5 uM


substrate_name: glyceraldehyde

column_label: Table 1; row Glyceraldehyde; Km column

normalized_value_unit_evidence: Km=7.3743 mM converted from 7374.3 uM

raw_value_unit_evidence: Table 1 Glyceraldehyde Km 7374.3 +/- 117.2 uM

substrate: glyceraldehyde


enzyme_display_name: alcohol dehydrogenase

organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

substrate_name: acetaldehyde (with NADH as cosubstrate)

assay_conditions_summary: cofactor NADPH

enzyme: alcohol dehydrogenase

substrate: acetaldehyde (with NADH as cosubstrate)


substrate_name: acetoin (with NADH as cosubstrate)

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

substrate: acetoin (with NADH as cosubstrate)


substrate_name: diacetyl (with NADH as cosubstrate)

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

substrate: diacetyl (with NADH as cosubstrate)


substrate_name: erythro-2,3-butanediol (with NAD as cosubstrate)

smiles: CC(C(C)O)O


substrate_name: ethanol (with NAD as cosubstrate)

smiles: CCO

substrate: ethanol (with NAD as cosubstrate)


substrate_name: NADH (with acetaldehyde as cosubstrate)

assay_conditions_summary: cofactor NADH

substrate: NADH (with acetaldehyde as cosubstrate)


substrate_name: NAD (with ethanol as cosubstrate)

substrate: NAD (with ethanol as cosubstrate)


substrate_name: NADPH (with acetaldehyde as cosubstrate)


smiles: C(CC=O)CN

assay_conditions_summary: pH 9; buffer 0.15 M Tris-HCl; cofactor NAD+

column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row ABAL, column ZmAMADH1a Km; Km, cell 28 +/- 3 uM, normalized 0.028 mM

raw_value_unit_evidence: Km raw 28 +/- 3 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row ABAL, column ZmAMADH1a Km

row_label: ZmAMADH1a / ABAL


smiles: C(CN)C=O

column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row APAL, column ZmAMADH1a Km; Km, cell 9 +/- 2 uM, normalized 0.009 mM

raw_value_unit_evidence: Km raw 9 +/- 2 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row APAL, column ZmAMADH1a Km

row_label: ZmAMADH1a / APAL


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

column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row TMABAL, column ZmAMADH1a Km; Km, cell 6 +/- 0.8 uM, normalized 0.006 mM

raw_value_unit_evidence: Km raw 6 +/- 0.8 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row TMABAL, column ZmAMADH1a Km

row_label: ZmAMADH1a / TMABAL


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

column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row GBAL, column ZmAMADH1a Km; Km, cell 3 +/- 0.7 uM, normalized 0.003 mM

raw_value_unit_evidence: Km raw 3 +/- 0.7 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row GBAL, column ZmAMADH1a Km

row_label: ZmAMADH1a / GBAL


substrate_name: NAD(+) with 3-aminopropanal as substrate

column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row NAD+, column ZmAMADH1a Km; Km, cell 91 +/- 4 uM, normalized 0.091 mM

raw_value_unit_evidence: Km raw 91 +/- 4 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row NAD+, column ZmAMADH1a Km

row_label: ZmAMADH1a / NAD+


column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row ABAL, column ZmAMADH1b Km; Km, cell 26 +/- 4 uM, normalized 0.026 mM

raw_value_unit_evidence: Km raw 26 +/- 4 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row ABAL, column ZmAMADH1b Km

row_label: ZmAMADH1b / ABAL


column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row APAL, column ZmAMADH1b Km; Km, cell 11 +/- 2 uM, normalized 0.011 mM

raw_value_unit_evidence: Km raw 11 +/- 2 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row APAL, column ZmAMADH1b Km

row_label: ZmAMADH1b / APAL


column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row TMABAL, column ZmAMADH1b Km; Km, cell 10 +/- 2 uM, normalized 0.01 mM

normalized_value_unit_evidence: Km 0.01 mM

raw_value_unit_evidence: Km raw 10 +/- 2 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row TMABAL, column ZmAMADH1b Km

row_label: ZmAMADH1b / TMABAL


column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row GBAL, column ZmAMADH1b Km; Km, cell 5 +/- 1 uM, normalized 0.005 mM

raw_value_unit_evidence: Km raw 5 +/- 1 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row GBAL, column ZmAMADH1b Km

row_label: ZmAMADH1b / GBAL


column_label: Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row BAL, column ZmAMADH1b Km; Km, cell 29 +/- 4 uM, normalized 0.029 mM

raw_value_unit_evidence: Km raw 29 +/- 4 uM from Table 4. Kinetic parameters of ALDH10 family from maize for selected substrates and the coenzyme NAD+, row BAL, column ZmAMADH1b Km

row_label: ZmAMADH1b / BAL


enzyme_display_name: aldehyde dehydrogenase (NADP(+))

organism: Arthrobacter nicotinovorans

substrate_name: Acetaldehyde

assay_conditions_summary: pH 8.4; 301.15 K; cofactor NADP+

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

normalized_value_unit_evidence: kcat paper=0.75 s^-1; Km paper=2.5 mM; kcat/Km paper=0.3 s^-1 mM^-1

row_label: Acetaldehyde footnote b

table_label: Table 2. Kinetic parameters of ALDH

enzyme: aldehyde dehydrogenase (NADP(+))

substrate: Acetaldehyde


substrate_name: Benzaldehyde

verification_status: corrected

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

normalized_value_unit_evidence: kcat paper=4.52 s^-1; Km paper=2.1 mM; kcat/Km paper=2.1 s^-1 mM^-1

row_label: Benzaldehyde footnote b

substrate: Benzaldehyde

status: corrected


substrate_name: Butanal

column_label: ScienceDirect HTML Table 2 row Butyraldehyde has columns Km (mM)=0.15 +/- 0.02, kcat (s^-1)=0.65 +/- 0.08, and kcat/Km (s^-1 M^-1)=4.3 x 10^3.

row_label: Butyraldehyde

table_label: Table 2. Aldehyde dehydrogenase kinetic parameters

substrate: Butanal


substrate_name: Glutaral

smiles: O=CCCCC=O

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

normalized_value_unit_evidence: kcat paper=3.92 s^-1; Km paper=0.11 mM; kcat/Km paper=35 s^-1 mM^-1

row_label: Glutaraldehyde footnote b

substrate: Glutaral


substrate_name: Glyceraldehyde

smiles: O=CC(O)CO

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

normalized_value_unit_evidence: kcat paper=1.35 s^-1; Km paper=0.65 mM; kcat/Km paper=2 s^-1 mM^-1

row_label: Glyceraldehyde footnote b

substrate: Glyceraldehyde


substrate_name: formaldehyde

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

normalized_value_unit_evidence: kcat paper=0.38 s^-1; Km paper=4.2 mM; kcat/Km paper=0.09 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row Formaldehyde: Km 4.2 +/- 1.1 mM; kcat 0.38 +/- 0.03 s^-1; kcat/Km 9 x 10 s^-1 M^-1.

row_label: Formaldehyde footnote b

substrate: formaldehyde


substrate_name: NADP+

column_label: Table 2; row NADP+ 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=1.02 s^-1; Km paper=0.022 mM; kcat/Km paper=46 s^-1 mM^-1

row_label: NADP+ footnote a

substrate: NADP+


substrate_name: propanal

smiles: CCC=O

column_label: ScienceDirect HTML Table 2 row Propionaldehyde has columns Km (mM)=1.5 +/- 0.1, kcat (s^-1)=1.2 +/- 0.11, and kcat/Km (s^-1 M^-1)=8 x 10^2.

raw_value_unit_evidence: Propionaldehyde row reports Km=1.5 +/- 0.1 mM, kcat=1.2 +/- 0.11 s^-1, kcat/Km=8 x 10^2 s^-1 M^-1.

row_label: Propionaldehyde

substrate: propanal


enzyme_display_name: Magnesium-activated aldehyde dehydrogenase, cytosolic

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADP (with acetaldehyde as cosubstrate)

assay_conditions_summary: pH 7.4; buffer 100 mM sodium phosphate; cofactor NADP+

column_label: PMC Table 3 row ALDH1, group Acetaldehyde-NADP, column Km for NADP (uM) lists 40 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=0.04 normalized_unit=mM from 40 uM.

raw_value_unit_evidence: Table 3 cell: ALDH1 / Acetaldehyde-NADP / Km for NADP (uM) = 40 uM.

row_label: ALDH1 / Acetaldehyde-NADP / NADP

table_label: PMC106960 Table 3, kinetic constants for recombinantly expressed S. cerevisiae ALDHs

substrate: NADP (with acetaldehyde as cosubstrate)


substrate_name: NAD (with propanal as cosubstrate)

assay_conditions_summary: pH 7.4; buffer 100 mM sodium phosphate; cofactor NAD+

column_label: PMC Table 3 row ALDH1, group Propionaldehyde-NAD, column Km for NAD (uM) lists 17,400 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=17.4 normalized_unit=mM from 17,400 uM.

raw_value_unit_evidence: Table 3 cell: ALDH1 / Propionaldehyde-NAD / Km for NAD (uM) = 17,400 uM.

row_label: ALDH1 / Propionaldehyde-NAD / NAD

enzyme: Magnesium-activated aldehyde dehydrogenase, cytosolic

substrate: NAD (with propanal as cosubstrate)


substrate_name: acetaldehyde (with NADP as cosubstrate)

column_label: PMC Table 3 row ALDH1, group Acetaldehyde-NADP, column Km for aldehyde (uM) lists 24 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=0.024 normalized_unit=mM from 24 uM.

raw_value_unit_evidence: Table 3 cell: ALDH1 / Acetaldehyde-NADP / Km for aldehyde (uM) = 24 uM.

row_label: ALDH1 / Acetaldehyde-NADP / aldehyde

substrate: acetaldehyde (with NADP as cosubstrate)


substrate_name: propanal (with NADP as cosubstrate)

column_label: PMC Table 3 row ALDH1, group Propionaldehyde-NADP, column Km for aldehyde (uM) lists 30 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=0.03 normalized_unit=mM from 30 uM.

raw_value_unit_evidence: Table 3 cell: ALDH1 / Propionaldehyde-NADP / Km for aldehyde (uM) = 30 uM.

row_label: ALDH1 / Propionaldehyde-NADP / aldehyde

substrate: propanal (with NADP as cosubstrate)


enzyme_display_name: Aldehyde dehydrogenase 5, mitochondrial

column_label: PMC Table 3 row ALDH5, group Acetaldehyde-NADP, column Km for NADP (uM) lists 640 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=0.64 normalized_unit=mM from 640 uM.

raw_value_unit_evidence: Table 3 cell: ALDH5 / Acetaldehyde-NADP / Km for NADP (uM) = 640 uM.

row_label: ALDH5 / Acetaldehyde-NADP / NADP

enzyme: Aldehyde dehydrogenase 5, mitochondrial


column_label: PMC Table 3 row ALDH5, group Propionaldehyde-NAD, column Km for NAD (uM) lists 6,430 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=6.43 normalized_unit=mM from 6,430 uM.

raw_value_unit_evidence: Table 3 cell: ALDH5 / Propionaldehyde-NAD / Km for NAD (uM) = 6,430 uM.

row_label: ALDH5 / Propionaldehyde-NAD / NAD


column_label: PMC Table 3 row ALDH5, group Acetaldehyde-NADP, column Km for aldehyde (uM) lists 58 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=0.058 normalized_unit=mM from 58 uM.

raw_value_unit_evidence: Table 3 cell: ALDH5 / Acetaldehyde-NADP / Km for aldehyde (uM) = 58 uM.

row_label: ALDH5 / Acetaldehyde-NADP / aldehyde


column_label: PMC Table 3 row ALDH5, group Propionaldehyde-NADP, column Km for aldehyde (uM) lists 390 uM; this matches the package Km after uM to mM conversion.

normalized_value_unit_evidence: Km normalized_value=0.39 normalized_unit=mM from 390 uM.

raw_value_unit_evidence: Table 3 cell: ALDH5 / Propionaldehyde-NADP / Km for aldehyde (uM) = 390 uM.

row_label: ALDH5 / Propionaldehyde-NADP / aldehyde


enzyme_display_name: aldehyde dehydrogenase (NADP+)

organism: Acinetobacter calcoaceticus

substrate_name: decanal

source_db: brenda

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

smiles: CCCCCCCCCC=O

column_label: Abstract reports aldehyde Km values decreasing with chain length, including decanal: 1.5 X 10(-6) M.

raw_value_unit_evidence: Km raw_value=1.5 X 10(-6) M raw_unit=M

row_label: Acinetobacter aldehyde dehydrogenase / decanal

table_label: PubMed XML abstract PMID 3566912

enzyme: aldehyde dehydrogenase (NADP+)

substrate: decanal

source: brenda


substrate_name: Nonanal

smiles: CCCCCCCCC=O

proof_lines:
Acinetobacter calcoaceticus
aldehyde dehydrogenase (NADP(+))
butanal

substrate: Nonanal


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


substrate_name: Heptanal

smiles: CCCCCCC=O

substrate: Heptanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


smiles: CCCC=O

column_label: Abstract reports aldehyde Km values decreasing with chain length, including butanal: 1.6 X 10(-3) M.

raw_value_unit_evidence: Km raw_value=1.6 X 10(-3) M raw_unit=M

row_label: Acinetobacter aldehyde dehydrogenase / butanal


enzyme_display_name: betaine-aldehyde dehydrogenase

organism: Spinacia oleracea

substrate_name: Betaine aldehyde

assay_conditions_summary: pH 8; 303.15 K; buffer 50 mM HEPES-KOH; cofactor NAD+

column_label: Official EuropePMC PDF text extraction lines 337-360: Table 1; row Wild type under variable substrate BAL; columns kcat, Km, kcat/Km; cells 3.36 s^-1, 98 uM, 35 mM^-1 s^-1.

raw_value_unit_evidence: Table 1 wild type BAL row cells report kcat 3.36 s^-1, Km 98 uM, and kcat/Km 35 mM^-1 s^-1.

row_label: Wild type; variable substrate BAL

table_label: Table 1 SoBADH steady-state kinetic parameters in BAL oxidation

enzyme: betaine-aldehyde dehydrogenase

substrate: Betaine aldehyde


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17202 and applied mutation signature A441C to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-state kinetic parameters of wild-type and mutant SoBADH enzymes in the oxidation of BAL), NAD+ block, row 'A441C'; column 'kcat (s-1)' = 2.20; column 'Km (uM)' = 14; column 'kcat/Km (mM-1s-1)' = 179.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.20 s^-1; the cell is already in s^-1, so no unit conversion applies and the value is 2.2 s^-1. Km: printed Table 1 cell 14 uM; 14 / 1000 = 0.014 mM. kcat/Km: printed Table 1 cell 179 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the printed cell is 179.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, NAD+ block, row A441C: kcat = 2.20 s^-1; Km = 14 uM; printed kcat/Km = 179 mM^-1 s^-1.

row_label: Table 1, NAD+ block, row A441C (the kcat, Km and kcat/Km cells of that printed row)

table_label: Table 1: Steady-state kinetic parameters of wild-type and mutant SoBADH enzymes in the oxidation of BAL (BMC Plant Biology 2014, 14:149)

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17202 and applied mutation signature A441F to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-state kinetic parameters of wild-type and mutant SoBADH enzymes in the oxidation of BAL), NAD+ block, row 'A441F'; column 'kcat (s-1)' = 0.39; column 'Km (uM)' = 18; column 'kcat/Km (mM-1s-1)' = 22.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.39 s^-1; the cell is already in s^-1, so no unit conversion applies and the value is 0.39 s^-1. Km: printed Table 1 cell 18 uM; 18 / 1000 = 0.018 mM. kcat/Km: printed Table 1 cell 22 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the printed cell is 22.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, NAD+ block, row A441F: kcat = 0.39 s^-1; Km = 18 uM; printed kcat/Km = 22 mM^-1 s^-1.

row_label: Table 1, NAD+ block, row A441F (the kcat, Km and kcat/Km cells of that printed row)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17202 and applied mutation signature A441I to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-state kinetic parameters of wild-type and mutant SoBADH enzymes in the oxidation of BAL), NAD+ block, row 'A441I'; column 'kcat (s-1)' = 0.68; column 'Km (uM)' = 2.8; column 'kcat/Km (mM-1s-1)' = 243.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.68 s^-1; the cell is already in s^-1, so no unit conversion applies and the value is 0.68 s^-1. Km: printed Table 1 cell 2.8 uM; 2.8 / 1000 = 0.0028 mM. kcat/Km: printed Table 1 cell 243 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the printed cell is 243.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, NAD+ block, row A441I: kcat = 0.68 s^-1; Km = 2.8 uM; printed kcat/Km = 243 mM^-1 s^-1.

row_label: Table 1, NAD+ block, row A441I (the kcat, Km and kcat/Km cells of that printed row)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17202 and applied mutation signature A441S to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-state kinetic parameters of wild-type and mutant SoBADH enzymes in the oxidation of BAL), NAD+ block, row 'A441S'; column 'kcat (s-1)' = 3.27; column 'Km (uM)' = 29; column 'kcat/Km (mM-1s-1)' = 114.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.27 s^-1; the cell is already in s^-1, so no unit conversion applies and the value is 3.27 s^-1. Km: printed Table 1 cell 29 uM; 29 / 1000 = 0.029 mM. kcat/Km: printed Table 1 cell 114 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the printed cell is 114.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, NAD+ block, row A441S: kcat = 3.27 s^-1; Km = 29 uM; printed kcat/Km = 114 mM^-1 s^-1.

row_label: Table 1, NAD+ block, row A441S (the kcat, Km and kcat/Km cells of that printed row)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A441T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A441V to reconstruct the assayed variant sequence.


column_label: Official EuropePMC PDF text extraction lines 337-360: Table 1; row Wild type under variable substrate NAD+; columns kcat, Km, kcat/Km; cells 4.25 s^-1, 22 uM, 195 mM^-1 s^-1.

raw_value_unit_evidence: Table 1 wild type NAD+ row cells report kcat 4.25 s^-1, Km 22 uM, and kcat/Km 195 mM^-1 s^-1.

row_label: Wild type; variable substrate NAD+


organism: Escherichia coli

substrate_name: acetaldehyde

smiles: CC=O

column_label: Primary PMC HTML table extract table_id=t3, Table 3 row Acetaldehyde, column Km (uM).

normalized_value_unit_evidence: Normalized paper Km: 2.5 uM = 0.0025 mM, matching export Km 0.0025 mM.

raw_value_unit_evidence: Table 3 row Acetaldehyde reports Vmax 2 U/mg, Km 2.5 uM, and Kcat/Km 225 mM^-1 min^-1.

row_label: Acetaldehyde

table_label: Table 3. Kinetic properties of AldB

source_databases_merged: brenda uniprot

substrate: acetaldehyde


substrate_name: Chloroacetaldehyde

smiles: C(C=O)Cl

column_label: Primary PMC HTML table extract table_id=t3, Table 3 row Chloroacetaldehyde, column Km (uM).

normalized_value_unit_evidence: Normalized paper Km: 3.6 uM = 0.0036 mM, matching export Km 0.0036 mM.

raw_value_unit_evidence: Table 3 row Chloroacetaldehyde reports Vmax 3.3 U/mg, Km 3.6 uM, and Kcat/Km 206 mM^-1 min^-1.

row_label: Chloroacetaldehyde

substrate: Chloroacetaldehyde


column_label: Primary PMC HTML table extract table_id=t3, Table 3 row Propionaldehyde, column Km (uM).

normalized_value_unit_evidence: Normalized paper Km: 5.8 uM = 0.0058 mM, matching export Km 0.0058 mM.

raw_value_unit_evidence: Table 3 row Propionaldehyde reports Vmax 1 U/mg, Km 5.8 uM, and Kcat/Km 39 mM^-1 min^-1.

row_label: Propionaldehyde


substrate_name: benzaldehyde

column_label: Table 3 row Benzaldehyde lists Km 56.8 microM.

raw_value_unit_evidence: Km raw_value=56.8 raw_unit=microM

row_label: Benzaldehyde

table_label: Table 3. Kinetic properties of AldB.

substrate: benzaldehyde


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

substrate: NADP+


column_label: Primary PMC HTML table extract table_id=t3, Table 3 row 4-Hydroperoxycyclophosphamide, column Km (uM).

normalized_value_unit_evidence: Normalized paper Km: 900 uM = 0.9 mM, matching export Km 0.9 mM.

raw_value_unit_evidence: Table 3 row 4-Hydroperoxycyclophosphamide reports Vmax 0.2 U/mg, Km 900 uM, and Kcat/Km 0.05 mM^-1 min^-1.


assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7


substrate_name: NADP

substrate: NADP


substrate_name: gamma-trimethylaminobutyraldehyde

column_label: Table II, enzyme column MBP-ALDH9, row gamma-trimethylaminobutyraldehyde, column Km (uM).

normalized_value_unit_evidence: Km=0.0048 mM converted from 4.8 uM.

raw_value_unit_evidence: Table II reports MBP-ALDH9 gamma-trimethylaminobutyraldehyde Km=4.8 uM.

table_label: Table II: Substrate specificity of purified TMABA-DH and heterologously expressed enzymes

substrate: gamma-trimethylaminobutyraldehyde


assay_conditions_summary: pH 9; buffer pH 9; cofactor NAD+

column_label: Table II, enzyme column MBP-ALDH9, row gamma-aminobutyraldehyde, column Km (microM).

normalized_value_unit_evidence: Km normalized_value=0.028 normalized_unit=mM converted from 28 microM.

raw_value_unit_evidence: Table II reports MBP-ALDH9 / gamma-aminobutyraldehyde Km=28 microM.

row_label: MBP-ALDH9 / gamma-aminobutyraldehyde


substrate_name: heptanal

substrate: heptanal


organism: Rattus norvegicus

substrate_name: NAD

column_label: Table II, enzyme column Rat liver TMABA-DH, row NAD+, column Km (uM).

normalized_value_unit_evidence: Km=0.028 mM converted from 28 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH NAD+ Km=28 uM.

row_label: Rat liver TMABA-DH / NAD+

substrate: NAD


assay_conditions_summary: pH 9; cofactor NADP+

column_label: Table II, enzyme column Rat liver TMABA-DH, row NADP+, column Km (uM).

normalized_value_unit_evidence: Km=1.63 mM converted from 1630 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH NADP+ Km=1630 uM.

row_label: Rat liver TMABA-DH / NADP+


column_label: Table II, enzyme column Rat liver TMABA-DH, row gamma-trimethylaminobutyraldehyde, column Km (uM).

normalized_value_unit_evidence: Km=0.0014 mM converted from 1.4 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH gamma-trimethylaminobutyraldehyde Km=1.4 uM.

row_label: Rat liver TMABA-DH / gamma-trimethylaminobutyraldehyde


column_label: Table II, enzyme column Rat liver TMABA-DH, row gamma-aminobutyraldehyde, column Km (uM).

normalized_value_unit_evidence: Km=0.024 mM converted from 24 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH gamma-aminobutyraldehyde Km=24 uM.

row_label: Rat liver TMABA-DH / gamma-aminobutyraldehyde


column_label: Table II, enzyme column Rat liver TMABA-DH, row Heptanal (C7), column Km (uM).

normalized_value_unit_evidence: Km=0.007 mM converted from 7 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH Heptanal (C7) Km=7 uM.

row_label: Rat liver TMABA-DH / Heptanal (C7)


column_label: Table II, enzyme column Rat liver TMABA-DH, row Octanal (C8), column Km (uM).

normalized_value_unit_evidence: Km=0.006 mM converted from 6 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH Octanal (C8) Km=6 uM.

row_label: Rat liver TMABA-DH / Octanal (C8)


enzyme_display_name: Aminoaldehyde dehydrogenase 1

organism: Solanum lycopersicum

column_label: Table 3; row ABAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.278 mM converted from 278 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / ABAL Km 278 +/- 19 uM

row_label: SlAMADH1 / ABAL

table_label: Table 3

enzyme: Aminoaldehyde dehydrogenase 1


column_label: Table 3; row APAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.041 mM converted from 41 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / APAL Km 41 +/- 5 uM

row_label: SlAMADH1 / APAL


column_label: Table 3; row TMABAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.017 mM converted from 17 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / TMABAL Km 17 +/- 1.4 uM

row_label: SlAMADH1 / TMABAL


column_label: Table 3; row GBAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.085 mM converted from 85 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / GBAL Km 85 +/- 13 uM

row_label: SlAMADH1 / GBAL


substrate_name: betaine aldehyde

column_label: TABLE 3; row BAL; enzyme column group SlAMADH1; metric column Km; raw cell 2051 +/- 83 uM; SlAMADH2 BAL cells are not determined.

normalized_value_unit_evidence: 2051 uM = 2.051 mM; reported uncertainty 83 uM = 0.083 mM; exported row value is 2.1 mM from source rounding.

raw_value_unit_evidence: Table 3 BAL row under SlAMADH1 reports Km 2051 +/- 83 uM.

row_label: Ligand BAL (betaine aldehyde); enzyme SlAMADH1 / Aminoaldehyde dehydrogenase 1

table_label: PMCID PMC3611018 TABLE 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and the coenzyme NAD+

substrate: betaine aldehyde


substrate_name: NAD(+) with 3-aminopropanal as substrate

column_label: Table 3; row NAD +; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.072 mM converted from 72 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / NAD + Km 72 +/- 7 uM

row_label: SlAMADH1 / NAD +


organism: Lachnoclostridium phytofermentans

column_label: Primary paper Table 1 row Acetaldehyde reports kcat (s^-1) = 1.62 +/- 0.02, KM (mM) = 5.16 +/- 0.10, and kcat/KM (s^-1 mM^-1) = 0.31.

normalized_value_unit_evidence: kcat normalized_value=1.62 normalized_unit=s^-1; KM normalized_value=5.16 normalized_unit=mM; kcat/KM table_normalized_value=0.31 normalized_unit=s^-1 mM^-1; CatLog computed ratio=1.62/5.16=0.313953488372093.

raw_value_unit_evidence: Table 1 row Acetaldehyde: kcat raw_value=1.62 +/- 0.02 raw_unit=s^-1; KM raw_value=5.16 +/- 0.10 raw_unit=mM; kcat/KM raw_value=0.31 raw_unit=s^-1 mM^-1; Ki raw_value=n/a raw_unit=mM.

row_label: Acetaldehyde

table_label: Table 1: The catalytic activity of Cphy1178 against aldehyde substrates


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: hexanaldehyde

column_label: Primary paper Table 1 row Hexanaldehyde reports kcat (s^-1) = 5.61 +/- 0.12, KM (mM) = 2.90 +/- 0.10, and kcat/KM (s^-1 mM^-1) = 1.93.

normalized_value_unit_evidence: kcat normalized_value=5.61 normalized_unit=s^-1; KM normalized_value=2.9 normalized_unit=mM; kcat/KM table_normalized_value=1.93 normalized_unit=s^-1 mM^-1; CatLog computed ratio=5.61/2.9=1.9344827586206899.

raw_value_unit_evidence: Table 1 row Hexanaldehyde: kcat raw_value=5.61 +/- 0.12 raw_unit=s^-1; KM raw_value=2.90 +/- 0.10 raw_unit=mM; kcat/KM raw_value=1.93 raw_unit=s^-1 mM^-1; Ki raw_value=23.52 +/- 1.28 raw_unit=mM.

row_label: Hexanaldehyde

substrate: hexanaldehyde


substrate_name: pentanaldehyde

substrate: pentanaldehyde


substrate_name: propionaldehyde

column_label: Primary paper Table 1 row Propionaldehyde reports kcat (s^-1) = 3.45 +/- 0.03, KM (mM) = 0.82 +/- 0.02, and kcat/KM (s^-1 mM^-1) = 4.21.

normalized_value_unit_evidence: kcat normalized_value=3.45 normalized_unit=s^-1; KM normalized_value=0.82 normalized_unit=mM; kcat/KM table_normalized_value=4.21 normalized_unit=s^-1 mM^-1; CatLog computed ratio=3.45/0.82=4.207317073170732.

raw_value_unit_evidence: Table 1 row Propionaldehyde: kcat raw_value=3.45 +/- 0.03 raw_unit=s^-1; KM raw_value=0.82 +/- 0.02 raw_unit=mM; kcat/KM raw_value=4.21 raw_unit=s^-1 mM^-1; Ki raw_value=17.31 +/- 0.46 raw_unit=mM.

row_label: Propionaldehyde

substrate: propionaldehyde


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A8 / Km column / ABAL row = 19+/-5 uM.

normalized_value_unit_evidence: Km=0.019 mM converted from 19+/-5 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for ABAL reports 19+/-5 uM.

row_label: AtALDH10A8 / Km column / ABAL row


column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A8 / Km column / APAL row = 2+/-0.3 uM.

normalized_value_unit_evidence: Km=0.002 mM converted from 2+/-0.3 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for APAL reports 2+/-0.3 uM.

row_label: AtALDH10A8 / Km column / APAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic


substrate_name: NAD(+) with 4-aminobutanal as substrate

assay_conditions_summary: cofactor NAD+

substrate: NAD(+) with 4-aminobutanal as substrate


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A9 / Km column / ABAL row = 31+/-4 uM.

normalized_value_unit_evidence: Km=0.031 mM converted from 31+/-4 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for ABAL reports 31+/-4 uM.

row_label: AtALDH10A9 / Km column / ABAL row


assay_conditions_summary: pH 9.5; cofactor NAD+

column_label: Table 1 / Kinetic parameters for AtALDH10A8 and AtALDH10A9 AtALDH10A9 / Km column / APAL row = 17.3+/-4.1 uM.

normalized_value_unit_evidence: Km=0.0173 mM converted from 17.3+/-4.1 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for APAL reports 17.3+/-4.1 uM.

row_label: AtALDH10A9 / Km column / APAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Aldehyde dehydrogenase 1A1

substrate_name: NAD (at pH 8.0)

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 1, row NAD, column Km (uM).

raw_value_unit_evidence: Table 1 row NAD: Km 59.4 +/- 2.4 uM; assay condition pH 8.0.

row_label: NAD

table_label: Table 1: Kinetic Parameters of Human Lens ALDH1A1 Using Various Substrates

enzyme: Aldehyde dehydrogenase 1A1

substrate: NAD (at pH 8.0)


substrate_name: (E)-4-hydroxynon-2-enal (at pH 8.0)

smiles: CCCCCC(C=CC=O)O

substrate: (E)-4-hydroxynon-2-enal (at pH 8.0)


substrate_name: acetaldehyde (at pH 8.0)

column_label: Table 1, row Acetaldehyde, column Km (uM).

raw_value_unit_evidence: Table 1 row Acetaldehyde: Km 238.2 +/- 12.9 uM; assay condition pH 8.0.

substrate: acetaldehyde (at pH 8.0)


substrate_name: propanal (at pH 8.0)

assay_conditions_summary: pH 8

substrate: propanal (at pH 8.0)


substrate_name: trans-2-heptenal (at pH 8.0)

smiles: CCCCC=CC=O

column_label: Table 1, row trans-2-Heptenal, column Km (uM).

raw_value_unit_evidence: Table 1 row trans-2-Heptenal: Km 177.1 +/- 11.7 uM; assay condition pH 8.0.

substrate: trans-2-heptenal (at pH 8.0)


substrate_name: Acetaldehyde

substrate: Acetaldehyde


column_label: Table 1 columns enzyme, substrate, Km, kcat (s^-1), kcat/Km (M^-1 s^-1); ALDH1 / acetaldehyde cells 41 uM, 0.16, 3900.

normalized_value_unit_evidence: Km 41 uM = 0.041 mM; kcat 0.16 s^-1; kcat/Km 3900 M^-1 s^-1 = 3.9 s^-1*mM^-1; exported 3.902439 is the kcat/Km computed from rounded kcat/Km table values.

raw_value_unit_evidence: ALDH1 / acetaldehyde row: Km 41 uM; kcat 0.16 s^-1; kcat/Km 3900 M^-1 s^-1.

row_label: ALDH1 / acetaldehyde

table_label: ACS institutional HTML Table 1, Kinetic Constants of Recombinant Rat Liver Class 1 Aldehyde Dehydrogenase Isozymes


substrate_name: all-trans-Retinal

column_label: Table 1 columns enzyme, substrate, Km, kcat (s^-1), kcat/Km (M^-1 s^-1); ALDH1 / all-trans-retinal cells 0.6 uM, 0.03, 50000.

raw_value_unit_evidence: ALDH1 / all-trans-retinal row: Km 0.6 uM; kcat 0.03 s^-1; kcat/Km 50000 M^-1 s^-1.

row_label: ALDH1 / all-trans-retinal

substrate: all-trans-Retinal


substrate_name: Benzaldehyde

substrate: Benzaldehyde


column_label: Table 1 columns enzyme, substrate, Km, kcat (s^-1), kcat/Km (M^-1 s^-1); ALDH1 / benzaldehyde cells 0.12 uM, 0.12, 1.0 x 10^6.

raw_value_unit_evidence: ALDH1 / benzaldehyde row: Km 0.12 uM; kcat 0.12 s^-1; kcat/Km 1.0 x 10^6 M^-1 s^-1.

row_label: ALDH1 / benzaldehyde


substrate_name: propanal

substrate: propanal


enzyme_display_name: aldehyde dehydrogenase [NAD(P)(+)]

organism: Sulfurisphaera tokodaii

substrate_name: acetaldehyde

column_label: Supplemental Table 4 columns Km (mM), kcat (s^-1), and kcat/Km x10^3 (s^-1 M^-1); Native row cells 6.38+/-0.52, 1.14+/-0.08, 0.18.

normalized_value_unit_evidence: kcat=1.14 s^-1; Km=6.38 mM; kcat/Km=0.18 s^-1 mM^-1 printed, matching expected computed ratio 0.1786833855799373 within table precision.

row_label: Native

table_label: Springer supplementary material 8, Supplemental Table 4

enzyme: aldehyde dehydrogenase [NAD(P)(+)]

substrate: acetaldehyde


substrate_name: D-glyceraldehyde

proof_lines: acetaldehyde NAD NADP

substrate: D-glyceraldehyde


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


substrate_name: NAD+

assay_conditions_summary: pH 8; 353.15 K; cofactor NAD+

column_label: Supplemental Table 3 columns Km (mM), kcat (s^-1), and kcat/Km x10^3 (s^-1 M^-1); Native row cells 0.84+/-0.07, 2.05+/-0.20, 2.45.

normalized_value_unit_evidence: kcat=2.05 s^-1; Km=0.84 mM; kcat/Km=2.45 s^-1 mM^-1 printed, matching expected computed ratio 2.4404761904761902 within table precision.

table_label: Springer supplementary material 7, Supplemental Table 3

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8; 353.15 K; cofactor NADP+

column_label: Table 3; row NADP; Acetaldehyde columns Km, kcat, and kcat/Km; cells 3.81 +/- 0.40, 3.71 +/- 0.10, and 0.98 +/- 0.11.

normalized_value_unit_evidence: Km 3.81 mM; kcat 3.71 s^-1; printed kcat/Km 0.98 s^-1 mM^-1. The current derived ratio 0.973753280839895 agrees at the printed table precision.

row_label: NADP / Acetaldehyde

table_label: Table 3. Kinetics parameters of stALDH toward NAD and NADP

substrate: NADP+


enzyme_display_name: Betaine aldehyde dehydrogenase 1

organism: Oryza sativa subsp. japonica

smiles: CC(=O)NCCCC=O

column_label: PDF Table 1 row N-acetyl-gamma-aminobutyraldehyde/N-acetyl-pyrroline has BAD1 Km=420 uM and BAD2 Km=10,608 uM; BAD1 maps to 0.42 mM.

raw_value_unit_evidence: Km raw_value=420 raw_unit=uM

table_label: Table 1 Km and kcat/Km values of BAD1 and BAD2 at optimum pH towards various substrates

enzyme: Betaine aldehyde dehydrogenase 1


substrate_name: gamma-aminobutyraldehyde

smiles: C(CC=O)CN

substrate: gamma-aminobutyraldehyde


enzyme_display_name: Betaine aldehyde dehydrogenase 2

enzyme: Betaine aldehyde dehydrogenase 2


substrate_name: betaine aldehyde

assay_conditions_summary: pH 10

column_label: PDF Table 1 row Betaine aldehyde has BAD2 Km=63 uM, which normalizes to 0.063 mM.

raw_value_unit_evidence: Km raw_value=63 raw_unit=uM

row_label: Betaine aldehyde; enzyme BAD2

substrate: betaine aldehyde


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.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+


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


enzyme_display_name: UniProt P17202

substrate_name: Betaine aldehyde

proof_lines:
SoBADH
BAL
Table II

enzyme: UniProt P17202

substrate: Betaine aldehyde


enzyme_display_name: Aminoaldehyde dehydrogenase BADH

proof_lines: APAL 3-aminopropionaldehyde SoBADH

enzyme: Aminoaldehyde dehydrogenase BADH


smiles: C(CN)C=O

proof_lines: ABAL 4-aminobutyraldehyde SoBADH


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

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

column_label: PMID 22345508 / DOI 10.1104/pp.112.194514, Table I, section TMABAL, row Wild type, K_m (uM) column = 3.6 +/- 0.2 uM; normalized K_m = 0.0036 mM.

raw_value_unit_evidence: Table I section TMABAL, row Wild type, K_m column: 3.6 +/- 0.2 uM; adjacent Vmax column: 1.2 +/- 0.0 units/mg protein; adjacent Vmax/Km column: 3.4 +/- 0.1 (x10^-1). Table I footnote states Vmax and Km values are given as units/mg protein and uM, respectively.

row_label: TMABAL / Wild type

table_label: Table I. Kinetic parameters of wild-type and mutant SoBADH enzymes using different omega-aminoaldehydes as substrates


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+


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

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


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_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)

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


enzyme_display_name: Potassium-activated aldehyde dehydrogenase, mitochondrial

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)

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

substrate_name: octanal

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

enzyme: aldehyde dehydrogenase (NAD(+))

substrate: Acetaldehyde


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.


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.


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


substrate_name: propanal

substrate: propanal


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_name: NAD(+)

substrate: NAD(+)


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


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+


substrate_name: 3-aminopropionaldehyde (AP-ald)

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


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

substrate: NAD+


organism: Homo sapiens

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

smiles: C(C=O)C=O


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

smiles: CCCCCC=O

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.

assay_conditions_summary: cofactor NADP+

proof_lines:
Pseudomonas strain K172
anaerobic toluene metabolism
benzyl alcohol dehydrogenase

enzyme: benzaldehyde dehydrogenase (NADP+)


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.

smiles: CCCCCCCC=O

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+


organism: Lycium ruthenicum

proof_lines:
LrAMADH1
betaine aldehyde
BRENDA literature summary 763552


substrate_name: acetaldehyde (at 30 degrees Celsius)

smiles: CC=O

substrate: acetaldehyde (at 30 degrees Celsius)


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

substrate_name: betaine aldehyde

assay_conditions_summary: pH 9; cofactor NAD+

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

substrate: propanal


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate: NAD+


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+

assay_conditions_summary: cofactor NAD+

substrate: deamino-NAD+


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_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

smiles: CCC=O

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: NAD+


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_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


organism: Arabidopsis thaliana

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

substrate: NAD+


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


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


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


organism: Pseudomonas aeruginosa


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


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


substrate: NAD+


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


smiles: CCC=O


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


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)

organism: Escherichia coli

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


organism: Homo sapiens

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

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-]


smiles: CCC=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


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


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)

assay_conditions_summary: cofactor NAD+

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


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

assay_conditions_summary: cofactor NAD+

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

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

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

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

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

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