substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: mutant enzyme E149T/V178R/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C

proof_lines: mutant enzyme E149T/V178R/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C

proof_lines: mutant enzyme E149T/V178R/I200V, with hexanal as cosubstrate, at pH 8.0 and 25°C

substrate: NAD+


enzyme_display_name: aldehyde dehydrogenase (NAD+)

organism: Arabidopsis thaliana

source_db: brenda

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149T/V178R/I200V to reconstruct the assayed variant sequence.

smiles: CCCCCCC=CC=O

assay_conditions_summary: pH 8

proof_lines: mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C

data_origin: experimental

enzyme: aldehyde dehydrogenase (NAD+)

status: unverified

source: brenda


substrate_name: hexanal

sequence_source: multiple

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature E149T/V178R/I200V to reconstruct the assayed variant sequence.

smiles: CCCCCC=O

source_databases_merged: brenda oed

source_db: oed

substrate: hexanal


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149T with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

mutation_type: substitution

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149D with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149Q with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

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


substrate_name: Nonanal

smiles: CCCCCCCCC=O

substrate: Nonanal


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149N with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

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


organism: Rattus norvegicus

substrate_name: acetaldehyde

kcat_over_km_display: Not reported

mutation_signature: Unknown

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

smiles: CC=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

substrate: acetaldehyde


enzyme_display_name: Aldehyde dehydrogenase

organism: Paenarthrobacter nicotinovorans

substrate_name: NADP(+)

source_db: uniprot

kcat_display: Not reported

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

proof_lines: kcat is 0.38 sec(-1) with formaldehyde as substrate. kcat is 0.75 sec(-1) with acetaldehyde as substrate. kcat is 1.2 sec(-1) with propionaldehyde as substrate. kcat is 1.35 sec(-1) with glyceraldehyde as substrate. kcat is 0.65 sec(-1) wit

enzyme: Aldehyde dehydrogenase

substrate: NADP(+)

source: uniprot


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: glyceraldehyde

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

substrate: glyceraldehyde


substrate_name: butyraldehyde

smiles: CCCC=O

substrate: butyraldehyde


substrate_name: glutaraldehyde

smiles: C(CC=O)CC=O

substrate: glutaraldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


enzyme_display_name: betaine-aldehyde dehydrogenase

organism: Spinacia oleracea

substrate_name: Betaine aldehyde

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

enzyme: betaine-aldehyde dehydrogenase

substrate: Betaine aldehyde


enzyme_display_name: Aldehyde dehydrogenase family 3 member A2

organism: Homo sapiens

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


substrate_name: octanal

smiles: CCCCCCCC=O

enzyme: Aldehyde dehydrogenase family 3 member A2

substrate: octanal


substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

substrate: dodecanal


substrate_name: tetradecanal

smiles: CCCCCCCCCCCCCC=O

substrate: tetradecanal


substrate_name: octadecanal

smiles: CCCCCCCCCCCCCCCCCC=O

substrate: octadecanal


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


organism: Oryza sativa

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

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

source_databases_merged: brenda uniprot


smiles: C(CN)C=O


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Antirrhinum majus

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


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


organism: Sinorhizobium meliloti

substrate_name: phosphonoacetaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N158A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: mutant enzyme N158A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C

substrate: phosphonoacetaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E385A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E385A, 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 N158A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C

substrate: NAD+


proof_lines: mutant enzyme E385A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C


organism: Ovis aries

assay_conditions_summary: cofactor NAD+

proof_lines:
reaction with propanal
reaction with butanal
cytoplasmic isoenzyme


substrate_name: propionaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D80G with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

substrate: propionaldehyde


assay_conditions_summary: pH 7.5; cofactor NAD+


km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R475E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R475Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

substrate: hexadecanal


substrate_name: farnesal

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

substrate: farnesal


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E103Q to reconstruct the assayed variant sequence.

smiles: C(CC=O)CN


proof_lines: mutant enzyme E103Q, reaction with betaine aldehyde

proof_lines: mutant enzyme E103Q, reaction with 4-aminobutyraldehyde


enzyme_display_name: Aldehyde dehydrogenase 1A1

organism: Oryctolagus cuniculus

smiles: CCCCCC(C=CC=O)O

enzyme: Aldehyde dehydrogenase 1A1


substrate_name: malonaldehyde

smiles: C(C=O)C=O

substrate: malonaldehyde


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: propanal

smiles: CCC=O

substrate: propanal


enzyme_display_name: aldehyde dehydrogenase [NAD(P)+]

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H1A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines:
isozyme ALDH1A1
isozyme ALDH1A1 from brain

enzyme: aldehyde dehydrogenase [NAD(P)+]


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H9A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


organism: Bos taurus

substrate_name: all-trans retinal

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

substrate: all-trans retinal


organism: Craterostigma plantagineum

substrate_name: nonanal

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

smiles: CCCCCCCCC=O

substrate: nonanal


smiles: CC=O


organism: Loktanella sp.

proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


enzyme_display_name: Aldehyde dehydrogenase 1

organism: Tanacetum cinerariifolium

substrate_name: NAD(+)

assay_conditions_summary: cofactor NADP+

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

enzyme: Aldehyde dehydrogenase 1

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: 9-cis retinal (at pH 7.5 and 25 degrees Celsius)

proof_lines: Has more than 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans retinal and 11-cis retinal.


enzyme_display_name: Aldehyde dehydrogenase, cytosolic 1

proof_lines: The highest catalytic efficiency is observed with benzaldehyde as substrate. No activity with retinal.

enzyme: Aldehyde dehydrogenase, cytosolic 1


substrate_name: benzaldehyde

substrate: benzaldehyde


enzyme_display_name: aldehyde dehydrogenase (NADP+)

organism: Acetobacter pasteurianus

substrate_name: NADP+

enzyme: aldehyde dehydrogenase (NADP+)

substrate: NADP+


enzyme_display_name: NAD/NADP-dependent betaine aldehyde dehydrogenase

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

substrate_name: NADP(+) (at pH 8.0 and 30 degrees Celsius)

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


substrate_name: NAD(+) (at pH 8.0 and 30 degrees Celsius)

enzyme: NAD/NADP-dependent betaine aldehyde dehydrogenase


enzyme_display_name: aldehyde dehydrogenase (NAD(+))

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

enzyme: aldehyde dehydrogenase (NAD(+))

source: oed


verification_status: verified

column_label: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / o-methoxy- (o-methoxybenzaldehyde), columns kcat (min-1) and Km (nM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / o-methoxy- (o-methoxybenzaldehyde): kcat 22 min^-1 and Km 800 nM; the table prints no kcat/Km column, so kcat/Km is derived from those same-row same-column cells.

status: verified


column_label: Table 2 (Continued): Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Naphthaldehydes / 2-naphthaldehyde, columns kcat (min-1) and Km (nM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2 (Continued): Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Naphthaldehydes / 2-naphthaldehyde: kcat 240 min^-1 and Km 8 nM; the table prints no kcat/Km column, so kcat/Km is derived from those same-row same-column cells.

row_label: Naphthaldehydes / 2-naphthaldehyde


column_label: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / m-methoxy- (m-methoxybenzaldehyde), columns kcat (min-1) and Km (nM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / m-methoxy- (m-methoxybenzaldehyde): kcat 350 min^-1 and Km 90 nM; the table prints no kcat/Km column, so kcat/Km is derived from those same-row same-column cells.


organism: Acinetobacter calcoaceticus

proof_lines:
reaction with heptanal
reaction with nonanal
reaction with pentanal


enzyme_display_name: benzaldehyde dehydrogenase (NADP+)

organism: Pseudomonas sp.

proof_lines: kcat is 8240 min(-1) with benzaldehyde and NAD as substrate. kcat is 2550 min(-1) with benzaldehyde and NADP as substrate.

enzyme: benzaldehyde dehydrogenase (NADP+)


organism: Macaca fascicularis

substrate_name: all-trans retinal (at pH 7.5 and 25 degrees Celsius)

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


substrate_name: Pentanal

verification_status: corrected

smiles: CCCCC=O

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 pentanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 155: pentanal kcat 1370 min^-1 and Km 34 nM.

row_label: ALDH-2 pentanal

substrate: Pentanal

status: corrected


substrate_name: Phenylacetaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 phenylacetaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 233: phenylacetaldehyde kcat 1800 min^-1 and Km 29 nM.

row_label: ALDH-2 phenylacetaldehyde

substrate: Phenylacetaldehyde


substrate_name: p-Nitrobenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 p-nitrobenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 245: p-nitrobenzaldehyde kcat 430 min^-1 and Km 7 nM.

row_label: ALDH-2 p-nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


substrate_name: p-Tolualdehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 p-methylbenzaldehyde / p-tolualdehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 251: p-methylbenzaldehyde kcat 180 min^-1 and Km 17 nM.

substrate: p-Tolualdehyde


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 quinoline-3-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 383: quinoline-3-carboxaldehyde kcat 670 min^-1 and Km 330 nM.

row_label: ALDH-2 quinoline-3-carboxaldehyde


substrate_name: Salicylaldehyde

column_label: Table 2 row o-hydroxy- under Benzaldehydes gives columns K_m (nM) and kcat (min^-1); source salicylaldehyde is o-hydroxybenzaldehyde; kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 50 plus/minus 5; K_m 320000 plus/minus 40000 nM; kcat 590 plus/minus 70 min^-1

row_label: o-hydroxybenzaldehyde (salicylaldehyde)

table_label: ACS PDF Table 2 Continued - human liver ALDH-2 substrate specificity

substrate: Salicylaldehyde


substrate_name: trans-Cinnamaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 trans-cinnamaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 224: trans-cinnamaldehyde kcat 150 min^-1 and Km 35 nM.

row_label: ALDH-2 trans-cinnamaldehyde

substrate: trans-Cinnamaldehyde


substrate_name: Veratraldehyde

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

column_label: Table 2  Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; journal page 4460, Table 2, Benzaldehydes block; row `3,4-dimethoxy- (veratraldehyde)`; column `Vm,rel (%)`; column `Km (nM)`; column `kcat (min-1)`; the row reads | 3,4-dimethoxy- (veratraldehyde) | Vm,rel (%) 7.2 +/- 0.4 | Km (nM) 330 +/- 60 | kcat (min-1) 85 +/- 7 |

normalized_value_unit_evidence: kcat: printed cell 85 min-1; 85.0 min-1 / 60 = 1.4166666666666667 s^-1, and the catalog kcat is 1.41666666666667 s^(-1), the same value at the catalog's own printed precision. Km: printed cell 330 nM; 330.0 nM / 1000000 = 0.00033 mM, which equals the catalog km exactly. kcat/Km: Table 1, Table 2 and Table 3 have no kcat/Km column and the paper prints no kcat/Km cell for this row, so the catalog kcat_over_km 4292.92929292929 s^(-1)*mM^(-1) can only be the full-precision quotient of this same row's own printed kcat and Km, 1.4166666666666667 / 0.00033 = 4292.929292929293.

raw_value_unit_evidence: journal page 4460, Table 2, Benzaldehydes block, row `3,4-dimethoxy- (veratraldehyde)`: Vm,rel and the two kinetic cells read | 3,4-dimethoxy- (veratraldehyde) | Vm,rel (%) 7.2 +/- 0.4 | Km (nM) 330 +/- 60 | kcat (min-1) 85 +/- 7 |. No kcat/Km cell is printed.

row_label: Table 2, Benzaldehydes block, row `3,4-dimethoxy-`

substrate: Veratraldehyde


substrate_name: decanal

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 decanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 159: decanal kcat 700 min^-1 and Km 22 nM.

row_label: ALDH-2 decanal

substrate: decanal


table_label: Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes

row_label: ALDH-2 quinoline-4-carboxaldehyde

column_label: kcat (min^-1), Km (nM), same-row ratio lock

raw_value_unit_evidence: Table 2 line 392: quinoline-4-carboxaldehyde kcat 280 min^-1 and Km 2800 nM.


column_label: Table 2 row phenanthrene-9-carboxaldehyde under Others gives columns K_m (nM) and kcat (min^-1); kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 1.5 plus/minus 0.4; K_m 4 plus/minus 3 nM; kcat 18 plus/minus 6 min^-1


substrate_name: Heptanal

smiles: CCCCCCC=O

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 heptanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 157: heptanal kcat 1360 min^-1 and Km 27 nM.

row_label: ALDH-2 heptanal

substrate: Heptanal


substrate_name: Hexanal

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 hexanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 156: hexanal kcat 1710 min^-1 and Km 30 nM.

row_label: ALDH-2 hexanal

substrate: Hexanal


substrate_name: Hydrocinnamaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 hydrocinnamaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 227: hydrocinnamaldehyde kcat 740 min^-1 and Km 500 nM.

row_label: ALDH-2 hydrocinnamaldehyde

substrate: Hydrocinnamaldehyde


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 indole-3-acetaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 lines 424-425: indole-3-acetaldehyde kcat 560 min^-1 and Km 150 nM.

row_label: ALDH-2 indole-3-acetaldehyde


substrate_name: m-Methylbenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 m-methylbenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 254: m-methylbenzaldehyde kcat 270 min^-1 and Km 18 nM.

row_label: ALDH-2 m-methylbenzaldehyde

substrate: m-Methylbenzaldehyde


substrate_name: formaldehyde

smiles: C=O

column_label: PMID 8605195 Table 1; row ALDH-2 formaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 152: formaldehyde kcat 4050 min^-1 and Km 320000 nM.

row_label: ALDH-2 formaldehyde

table_label: Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5)

substrate: formaldehyde


substrate_name: o-Methylbenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 o-methylbenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 278: o-methylbenzaldehyde kcat 165 min^-1 and Km 1300 nM.

row_label: ALDH-2 o-methylbenzaldehyde

substrate: o-Methylbenzaldehyde


substrate_name: o-Nitrobenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 o-nitrobenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 242: o-nitrobenzaldehyde kcat 74 min^-1 and Km 6.3 nM.

row_label: ALDH-2 o-nitrobenzaldehyde

substrate: o-Nitrobenzaldehyde


substrate_name: p-(dimethylamino)benzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 p-(dimethylamino)benzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 261: p-(dimethylamino)benzaldehyde kcat 140 min^-1 and Km 20 nM.

row_label: ALDH-2 p-(dimethylamino)benzaldehyde

substrate: p-(dimethylamino)benzaldehyde


substrate_name: p-(dimethylamino)cinnamaldehyde

column_label: PMID 8605195 Table 2; row ALDH-2 p-(dimethylamino)cinnamaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 221: p-(dimethylamino)cinnamaldehyde kcat 90 min^-1 and Km 5 nM.

row_label: ALDH-2 p-(dimethylamino)cinnamaldehyde

substrate: p-(dimethylamino)cinnamaldehyde


column_label: Table 2  Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; journal page 4461, Table 2 (Continued), Coumarin-4-carboxaldehydes block; row `6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde)`; column `Vm,rel (%)`; column `Km (nM)`; column `kcat (min-1)`; the row reads | 6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde) | Vm,rel (%) 5.0 +/- 0.5 | Km (nM) 690 +/- 100 | kcat (min-1) 59 +/- 7 |

normalized_value_unit_evidence: kcat: printed cell 59 min-1; 59.0 min-1 / 60 = 0.9833333333333333 s^-1, and the catalog kcat is 0.983333333333333 s^(-1), the same value at the catalog's own printed precision. Km: printed cell 690 nM; 690.0 nM / 1000000 = 0.00069 mM, which equals the catalog km exactly. kcat/Km: Table 1, Table 2 and Table 3 have no kcat/Km column and the paper prints no kcat/Km cell for this row, so the catalog kcat_over_km 1425.12077294686 s^(-1)*mM^(-1) can only be the full-precision quotient of this same row's own printed kcat and Km, 0.9833333333333333 / 0.00069 = 1425.1207729468594.

raw_value_unit_evidence: journal page 4461, Table 2 (Continued), Coumarin-4-carboxaldehydes block, row `6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde)`: Vm,rel and the two kinetic cells read | 6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde) | Vm,rel (%) 5.0 +/- 0.5 | Km (nM) 690 +/- 100 | kcat (min-1) 59 +/- 7 |. No kcat/Km cell is printed.

row_label: Table 2 (Continued), Coumarin-4-carboxaldehydes block, row `6,7-dimethoxy-`


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 6-(dimethylamino)-2-naphthaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 lines 321-322: 6-(dimethylamino)-2-naphthaldehyde kcat 37 min^-1 and Km 2.3 nM.


raw_value_unit_evidence: Table 2 line 396: 6-methoxy-2-quinolinone-4-carboxaldehyde kcat 59 min^-1 and Km 5400 nM.


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 7-acetoxycoumarin-4-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 355: 7-acetoxy coumarin-4-carboxaldehyde kcat 65 min^-1 and Km 60 nM.


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 7-(dimethylamino)coumarin-4-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 360: 7-(dimethylamino)coumarin-4-carboxaldehyde kcat 78 min^-1 and Km 62 nM.


column_label: Table 2 row 7-hydroxy- under Coumarin-4-carboxaldehydes gives columns K_m (nM) and kcat (min^-1); kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 42 plus/minus 3; K_m 150000 plus/minus 20000 nM; kcat 500 plus/minus 40 min^-1


column_label: Table 2 row 7-methoxy-2-quinolinone-4- under Quinoline- and Quinolinonecarboxaldehydes gives columns K_m (nM) and kcat (min^-1); kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 27 plus/minus 3; K_m 50000 plus/minus 10000 nM; kcat 320 plus/minus 40 min^-1


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 7-methoxycoumarin-4-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 365: 7-methoxycoumarin-4-carboxaldehyde kcat 190 min^-1 and Km 280 nM.


substrate_name: alpha-Phenylpropionaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 alpha-phenylpropionaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 230: R-phenylpropionaldehyde kcat 910 min^-1 and Km 930 nM.

row_label: ALDH-2 alpha-phenylpropionaldehyde

substrate: alpha-Phenylpropionaldehyde


substrate_name: Benzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 benzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 248: benzaldehyde kcat 350 min^-1 and Km 18 nM.

row_label: ALDH-2 benzaldehyde

substrate: Benzaldehyde


organism: Thermus thermophilus

substrate_name: propanal

column_label: The primary article states that ALDHTt530 has a KM of 2.76 mM when propanal was used.

raw_value_unit_evidence: Km raw_value=2.76 raw_unit=mM

row_label: ALDHTt530 with propanal

table_label: Discussion prose comparing ALDHTt530 propanal kinetic parameters

substrate: propanal


organism: Arabidopsis thaliana

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149T with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149T; kcat column raw 10.2 +/- 0.4; kcat/Km column raw 8.1 +/- 0.2; Km column raw 1262 +/- 38

normalized_value_unit_evidence: kcat normalized_value=10.2 normalized_unit=s^-1; kcat/Km normalized_value=8.0824088748019 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=8.1 +/- 0.2 s^-1 mM^-1; Km normalized_value=1.262 normalized_unit=mM from 1262 +/- 38 uM / 1000

raw_value_unit_evidence: kcat raw_value=10.2 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=8.1 +/- 0.2 raw_unit=s^-1 mM^-1; Km raw_value=1262 +/- 38 raw_unit=uM

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149T/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149T/I200G; kcat column raw 33.9 +/- 0.8; kcat/Km column raw 9.9 +/- 0.6; Km column raw 3418 +/- 187

normalized_value_unit_evidence: kcat normalized_value=33.9 normalized_unit=s^-1; kcat/Km normalized_value=9.91808074897601 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=9.9 +/- 0.6 s^-1 mM^-1; Km normalized_value=3.418 normalized_unit=mM from 3418 +/- 187 uM / 1000

raw_value_unit_evidence: kcat raw_value=33.9 +/- 0.8 raw_unit=s^-1; kcat/Km raw_value=9.9 +/- 0.6 raw_unit=s^-1 mM^-1; Km raw_value=3418 +/- 187 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149T/I200V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149T/V178R/I200V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1I200G; kcat column raw 16.3 +/- 1.7; kcat/Km column raw 5.1 +/- 0.3; Km column raw 3218 +/- 54

normalized_value_unit_evidence: kcat normalized_value=16.3 normalized_unit=s^-1; kcat/Km normalized_value=5.06525792417651 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=5.1 +/- 0.3 s^-1 mM^-1; Km normalized_value=3.218 normalized_unit=mM from 3218 +/- 54 uM / 1000

raw_value_unit_evidence: kcat raw_value=16.3 +/- 1.7 raw_unit=s^-1; kcat/Km raw_value=5.1 +/- 0.3 raw_unit=s^-1 mM^-1; Km raw_value=3218 +/- 54 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1I200V; kcat column raw 18.5 +/- 1.7; kcat/Km column raw 37.3 +/- 1.1; Km column raw 496 +/- 4

normalized_value_unit_evidence: kcat normalized_value=18.5 normalized_unit=s^-1; kcat/Km normalized_value=37.2983870967742 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=37.3 +/- 1.1 s^-1 mM^-1; Km normalized_value=0.496 normalized_unit=mM from 496 +/- 4 uM / 1000

raw_value_unit_evidence: kcat raw_value=18.5 +/- 1.7 raw_unit=s^-1; kcat/Km raw_value=37.3 +/- 1.1 raw_unit=s^-1 mM^-1; Km raw_value=496 +/- 4 raw_unit=uM


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

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1; kcat column raw 17.2 +/- 1.6; kcat/Km column raw 40.9 +/- 1.2; Km column raw 421 +/- 23.5

normalized_value_unit_evidence: kcat normalized_value=17.2 normalized_unit=s^-1; kcat/Km normalized_value=40.855106888361 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=40.9 +/- 1.2 s^-1 mM^-1; Km normalized_value=0.421 normalized_unit=mM from 421 +/- 23.5 uM / 1000

raw_value_unit_evidence: kcat raw_value=17.2 +/- 1.6 raw_unit=s^-1; kcat/Km raw_value=40.9 +/- 1.2 raw_unit=s^-1 mM^-1; Km raw_value=421 +/- 23.5 raw_unit=uM


substrate_name: Nonanal

column_label: Table 3, ALDH3H1 wild-type column. Kinetic properties related to substrate specificity.; row ALDH3H1 / Nonanal; kcat column raw 17.9 +/- 3.8; kcat/Km column raw 2166 +/- 37; Km column raw 8 +/- 2

normalized_value_unit_evidence: kcat normalized_value=17.9 normalized_unit=s^-1; kcat/Km normalized_value=2237.5 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=2166 +/- 37 s^-1 mM^-1; Km normalized_value=0.008 normalized_unit=mM from 8 +/- 2 uM / 1000

raw_value_unit_evidence: kcat raw_value=17.9 +/- 3.8 raw_unit=s^-1; kcat/Km raw_value=2166 +/- 37 raw_unit=s^-1 mM^-1; Km raw_value=8 +/- 2 raw_unit=uM

row_label: ALDH3H1 / Nonanal

substrate: Nonanal


smiles: CCC/C=C/C=O

column_label: Table 3. Kinetic properties related to substrate specificity of wild-type enzyme ALDH3H1 and triple mutant enzyme ALDH3H1E149T/V178R/I200V.; row ALDH3H1E149T/V178R/I200V / trans-2-Hexenal; kcat column raw 1.1 +/- 0.04; kcat/Km column raw 5.3 +/- 0.2; Km column raw 199 +/- 6

normalized_value_unit_evidence: kcat normalized_value=1.1 normalized_unit=s^-1; kcat/Km normalized_value=5.52763819095477 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=5.3 +/- 0.2 s^-1 mM^-1; Km normalized_value=0.199 normalized_unit=mM from 199 +/- 6 uM / 1000

raw_value_unit_evidence: kcat raw_value=1.1 +/- 0.04 raw_unit=s^-1; kcat/Km raw_value=5.3 +/- 0.2 raw_unit=s^-1 mM^-1; Km raw_value=199 +/- 6 raw_unit=uM


column_label: Table 3, ALDH3H1 wild-type column. Kinetic properties related to substrate specificity.; row ALDH3H1 / trans-2-Hexenal; kcat column raw 2.2 +/- 0.1; kcat/Km column raw 12.4 +/- 0.8; Km column raw 180 +/- 24

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; kcat/Km normalized_value=12.2222222222222 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=12.4 +/- 0.8 s^-1 mM^-1; Km normalized_value=0.18 normalized_unit=mM from 180 +/- 24 uM / 1000

raw_value_unit_evidence: kcat raw_value=2.2 +/- 0.1 raw_unit=s^-1; kcat/Km raw_value=12.4 +/- 0.8 raw_unit=s^-1 mM^-1; Km raw_value=180 +/- 24 raw_unit=uM

row_label: ALDH3H1 / trans-2-Hexenal


substrate_name: hexanal

column_label: Table 3, ALDH3H1 wild-type column. Kinetic properties related to substrate specificity.; row ALDH3H1 / Hexanal; kcat column raw 11.2 +/- 0.5; kcat/Km column raw 154 +/- 3; Km column raw 71 +/- 12

normalized_value_unit_evidence: kcat normalized_value=11.2 normalized_unit=s^-1; kcat/Km normalized_value=157.746478873239 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=154 +/- 3 s^-1 mM^-1; Km normalized_value=0.071 normalized_unit=mM from 71 +/- 12 uM / 1000

raw_value_unit_evidence: kcat raw_value=11.2 +/- 0.5 raw_unit=s^-1; kcat/Km raw_value=154 +/- 3 raw_unit=s^-1 mM^-1; Km raw_value=71 +/- 12 raw_unit=uM

row_label: ALDH3H1 / Hexanal

substrate: hexanal


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149D with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149D; kcat column raw 10.7 +/- 0.8; kcat/Km column raw 24.3 +/- 1.1; Km column raw 441 +/- 40

normalized_value_unit_evidence: kcat normalized_value=10.7 normalized_unit=s^-1; kcat/Km normalized_value=24.2630385487528 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=24.3 +/- 1.1 s^-1 mM^-1; Km normalized_value=0.441 normalized_unit=mM from 441 +/- 40 uM / 1000

raw_value_unit_evidence: kcat raw_value=10.7 +/- 0.8 raw_unit=s^-1; kcat/Km raw_value=24.3 +/- 1.1 raw_unit=s^-1 mM^-1; Km raw_value=441 +/- 40 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149D/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149D/I200G; kcat column raw 23.2 +/- 0.6; kcat/Km column raw 6.4 +/- 0.3; Km column raw 3651 +/- 125

normalized_value_unit_evidence: kcat normalized_value=23.2 normalized_unit=s^-1; kcat/Km normalized_value=6.35442344563133 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=6.4 +/- 0.3 s^-1 mM^-1; Km normalized_value=3.651 normalized_unit=mM from 3651 +/- 125 uM / 1000

raw_value_unit_evidence: kcat raw_value=23.2 +/- 0.6 raw_unit=s^-1; kcat/Km raw_value=6.4 +/- 0.3 raw_unit=s^-1 mM^-1; Km raw_value=3651 +/- 125 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149D/I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149D/I200V; kcat column raw 12.4 +/- 0.4; kcat/Km column raw 12.5 +/- 0.6; Km column raw 991 +/- 82

normalized_value_unit_evidence: kcat normalized_value=12.4 normalized_unit=s^-1; kcat/Km normalized_value=12.5126135216953 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=12.5 +/- 0.6 s^-1 mM^-1; Km normalized_value=0.991 normalized_unit=mM from 991 +/- 82 uM / 1000

raw_value_unit_evidence: kcat raw_value=12.4 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=12.5 +/- 0.6 raw_unit=s^-1 mM^-1; Km raw_value=991 +/- 82 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149N with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149N; kcat column raw 16.6 +/- 0.7; kcat/Km column raw 26.3 +/- 0.9; Km column raw 630 +/- 33.1

normalized_value_unit_evidence: kcat normalized_value=16.6 normalized_unit=s^-1; kcat/Km normalized_value=26.3492063492064 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=26.3 +/- 0.9 s^-1 mM^-1; Km normalized_value=0.63 normalized_unit=mM from 630 +/- 33.1 uM / 1000

raw_value_unit_evidence: kcat raw_value=16.6 +/- 0.7 raw_unit=s^-1; kcat/Km raw_value=26.3 +/- 0.9 raw_unit=s^-1 mM^-1; Km raw_value=630 +/- 33.1 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149N/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149N/I200G; kcat column raw 26.9 +/- 2.1; kcat/Km column raw 6.5 +/- 0.2; Km column raw 4136 +/- 124

normalized_value_unit_evidence: kcat normalized_value=26.9 normalized_unit=s^-1; kcat/Km normalized_value=6.50386847195358 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=6.5 +/- 0.2 s^-1 mM^-1; Km normalized_value=4.136 normalized_unit=mM from 4136 +/- 124 uM / 1000

raw_value_unit_evidence: kcat raw_value=26.9 +/- 2.1 raw_unit=s^-1; kcat/Km raw_value=6.5 +/- 0.2 raw_unit=s^-1 mM^-1; Km raw_value=4136 +/- 124 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149N/I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149N/I200V; kcat column raw 13.1 +/- 0.6; kcat/Km column raw 13.2 +/- 0.5; Km column raw 992 +/- 54.4

normalized_value_unit_evidence: kcat normalized_value=13.1 normalized_unit=s^-1; kcat/Km normalized_value=13.2056451612903 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=13.2 +/- 0.5 s^-1 mM^-1; Km normalized_value=0.992 normalized_unit=mM from 992 +/- 54.4 uM / 1000

raw_value_unit_evidence: kcat raw_value=13.1 +/- 0.6 raw_unit=s^-1; kcat/Km raw_value=13.2 +/- 0.5 raw_unit=s^-1 mM^-1; Km raw_value=992 +/- 54.4 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149Q with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149Q; kcat column raw 12.7 +/- 0.8; kcat/Km column raw 14.3 +/- 0.7; Km column raw 886 +/- 110

normalized_value_unit_evidence: kcat normalized_value=12.7 normalized_unit=s^-1; kcat/Km normalized_value=14.334085778781 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=14.3 +/- 0.7 s^-1 mM^-1; Km normalized_value=0.886 normalized_unit=mM from 886 +/- 110 uM / 1000

raw_value_unit_evidence: kcat raw_value=12.7 +/- 0.8 raw_unit=s^-1; kcat/Km raw_value=14.3 +/- 0.7 raw_unit=s^-1 mM^-1; Km raw_value=886 +/- 110 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149Q/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149Q/I200G; kcat column raw 20.1 +/- 1.9; kcat/Km column raw 5 +/- 0.4; Km column raw 4059 +/- 130

normalized_value_unit_evidence: kcat normalized_value=20.1 normalized_unit=s^-1; kcat/Km normalized_value=4.9519586104952 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=5 +/- 0.4 s^-1 mM^-1; Km normalized_value=4.059 normalized_unit=mM from 4059 +/- 130 uM / 1000

raw_value_unit_evidence: kcat raw_value=20.1 +/- 1.9 raw_unit=s^-1; kcat/Km raw_value=5 +/- 0.4 raw_unit=s^-1 mM^-1; Km raw_value=4059 +/- 130 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149Q/I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149Q/I200V; kcat column raw 11.4 +/- 0.6; kcat/Km column raw 6.1 +/- 0.1; Km column raw 1856 +/- 43

normalized_value_unit_evidence: kcat normalized_value=11.4 normalized_unit=s^-1; kcat/Km normalized_value=6.14224137931034 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=6.1 +/- 0.1 s^-1 mM^-1; Km normalized_value=1.856 normalized_unit=mM from 1856 +/- 43 uM / 1000

raw_value_unit_evidence: kcat raw_value=11.4 +/- 0.6 raw_unit=s^-1; kcat/Km raw_value=6.1 +/- 0.1 raw_unit=s^-1 mM^-1; Km raw_value=1856 +/- 43 raw_unit=uM


smiles: CCCCCC/C=C/C=O


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


enzyme_display_name: Aldehyde dehydrogenase family 3 member H1

substrate_name: propionaldehyde

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

raw_value_unit_evidence: Table 1 ALDH3H1 propionaldehyde Km raw_value=510 raw_unit=uM

row_label: ALDH3H1 / propionaldehyde

substrate: propionaldehyde


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

raw_value_unit_evidence: Table 1 ALDH3H1 hexanal Km raw_value=71 raw_unit=uM

row_label: ALDH3H1 / hexanal

enzyme: Aldehyde dehydrogenase family 3 member H1


substrate_name: octanal

smiles: CCCCCCCC=O

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

raw_value_unit_evidence: Table 1 ALDH3H1 octanal Km raw_value=29 raw_unit=uM

row_label: ALDH3H1 / octanal

substrate: octanal


substrate_name: nonanal

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

raw_value_unit_evidence: Table 1 ALDH3H1 nonanal Km raw_value=8 raw_unit=uM

row_label: ALDH3H1 / nonanal

substrate: nonanal


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

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

raw_value_unit_evidence: Table 1 ALDH3H1 dodecanal Km raw_value=5 raw_unit=uM

row_label: ALDH3H1 / dodecanal

substrate: dodecanal


smiles: CCCC=CC=O

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / trans-2-hexenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 trans-2-hexenal Km raw_value=180 raw_unit=uM

row_label: ALDH3H1 / trans-2-hexenal


smiles: CCCCCCC=CC=O

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / trans-2-nonenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 trans-2-nonenal Km raw_value=3 raw_unit=uM

row_label: ALDH3H1 / trans-2-nonenal


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

raw_value_unit_evidence: Table 1 ALDH3H1 4-hydroxynonenal Km raw_value=40.3 raw_unit=uM

row_label: ALDH3H1 / 4-hydroxynonenal


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


enzyme_display_name: Aldehyde dehydrogenase family 3 member I1, chloroplastic

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

raw_value_unit_evidence: Table 1 ALDH3I1 propionaldehyde Km raw_value=8053 raw_unit=uM

row_label: ALDH3I1 / propionaldehyde


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

raw_value_unit_evidence: Table 1 ALDH3I1 hexanal Km raw_value=111 raw_unit=uM

row_label: ALDH3I1 / hexanal

enzyme: Aldehyde dehydrogenase family 3 member I1, chloroplastic


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

raw_value_unit_evidence: Table 1 ALDH3I1 octanal Km raw_value=24 raw_unit=uM

row_label: ALDH3I1 / octanal


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

raw_value_unit_evidence: Table 1 ALDH3I1 nonanal Km raw_value=7 raw_unit=uM

row_label: ALDH3I1 / nonanal


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

raw_value_unit_evidence: Table 1 ALDH3I1 dodecanal Km raw_value=1.3 raw_unit=uM

row_label: ALDH3I1 / dodecanal


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / trans-2-hexenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 trans-2-hexenal Km raw_value=151 raw_unit=uM

row_label: ALDH3I1 / trans-2-hexenal


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / trans-2-nonenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 trans-2-nonenal Km raw_value=5.5 raw_unit=uM

row_label: ALDH3I1 / trans-2-nonenal


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


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


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


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

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

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


organism: Homo sapiens

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.


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+


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.


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.


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


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


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


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


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


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_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

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

smiles: CCCCCC=O

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


substrate_name: NAD+

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

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


substrate_name: propanal

smiles: CCC=O

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)

substrate: propanal


enzyme_display_name: UniProt P49189

source_db: skid

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

source_databases_merged: skid uniprot

enzyme: UniProt P49189

source: skid


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: formaldehyde

substrate: formaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: butyraldehyde

substrate: butyraldehyde


substrate_name: hexanaldehyde

substrate: hexanaldehyde


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

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

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


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

smiles: C=O

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

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


substrate_name: decanal

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

substrate: decanal


substrate_name: Nonanal

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

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


smiles: CCC=O

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

assay_conditions_summary: cofactor 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+


assay_conditions_summary: pH 9; cofactor NAD+

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

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


enzyme_display_name: aldehyde dehydrogenase (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.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

enzyme: aldehyde dehydrogenase (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