organism: Paraburkholderia xenovorans

substrate_name: pentaldehyde

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

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

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

substrate: pentaldehyde


organism: Pseudomonas putida

substrate_name: benzaldehyde

source_db: brenda

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor NAD+

column_label: Abstract reports the apparent K(m) value of benzaldehyde dehydrogenase for benzaldehyde was 460 microM.

raw_value_unit_evidence: Km raw_value=460 microM raw_unit=microM

row_label: Pseudomonas putida TOL plasmid benzaldehyde dehydrogenase / benzaldehyde

table_label: PubMed XML abstract PMID 2202600

data_origin: experimental

substrate: benzaldehyde

status: verified

source: brenda


substrate_name: picolinaldehyde

verification_status: unverified

substrate: picolinaldehyde

status: unverified


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

mutation_type: substitution

proof_lines: mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)


substrate_name: propionaldehyde

km_display: Not reported

smiles: CCC=O

proof_lines: mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)

substrate: propionaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


proof_lines: mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0)


proof_lines: mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


organism: Oryza sativa

substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines: mutant enzyme F37L, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

substrate: 3-phospho-D-glyceroyl phosphate


proof_lines: mutant enzyme F37T, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C


substrate_name: D-glyceraldehyde 3-phosphate

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

proof_lines: mutant enzyme F37L, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C

substrate: D-glyceraldehyde 3-phosphate


proof_lines: mutant enzyme F37T, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C


proof_lines: mutant enzyme F37G, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C


proof_lines: mutant enzyme F37G, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C


proof_lines: wild type enzyme, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C


proof_lines: wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C


substrate_name: NAD+

assay_conditions_summary: pH 8.8; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: aspartate-semialdehyde dehydrogenase

organism: Haemophilus influenzae

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

enzyme: aspartate-semialdehyde dehydrogenase


proof_lines: recombinant mutant R103K and mutant K246L


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: phosphate

substrate: phosphate


organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADH


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: succinate semialdehyde

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

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C

substrate: succinate semialdehyde


proof_lines: mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines: mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C

proof_lines: wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


organism: Bacillus subtilis

assay_conditions_summary: pH 8.2; 303.15 K; cofactor NAD+

proof_lines: V229G/H226P/G225 insertion, pH 8.2 and 30°C


proof_lines: V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C


proof_lines:
V229G/G225 insertion, pH 8.2 and 30°C
V229G, pH 8.2 and 30°C


mutation_signature: G225 insertion

mutation_type: insertion


proof_lines: wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C

proof_lines: wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C


substrate_name: methylmalonate semialdehyde

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

substrate: methylmalonate semialdehyde


proof_lines: wild type MSDH, steady-state conditions, pH 8.2 and 30°C


substrate_name: CoA

assay_conditions_summary: pH 8.2; 303.15 K; cofactor CoA

substrate: CoA


organism: Triticum aestivum

proof_lines: pH 8.5, 30°C, recombinant wild-type enzyme


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+


proof_lines: R124L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C

proof_lines: R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C


proof_lines: R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C


proof_lines: R124L mutant enzyme, steady-state conditions, pH 8.2 and 30°C


proof_lines: R301L mutant enzyme, steady-state conditions, pH 8.2 and 30°C


proof_lines: R301L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+


proof_lines: recombinant wild-type enzyme, pH 9.0, 30°C

proof_lines: recombinant wild-type enzyme and mutant E243D


substrate_name: cacodylate

substrate: cacodylate


enzyme_display_name: UniProt P00352

organism: Homo sapiens

substrate_name: decanal

source_db: skid

source_license: CC BY-NC-ND 4.0

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

smiles: CCCCCCCCCC=O

enzyme: UniProt P00352

substrate: decanal

source: skid


substrate_name: all-trans-retinal

substrate: all-trans-retinal


enzyme_display_name: UniProt P47895

substrate_name: hexanal

smiles: CCCCCC=O

enzyme: UniProt P47895

substrate: hexanal


proof_lines: glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C

proof_lines: pH 7.3, enzyme isolated of sarcoma tissue


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


mutation_signature: highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus / highly soluble form of sperm-specific glyceraldehyd

mutation_type: truncation

proof_lines: recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25?


mutation_signature: N-terminally truncated mutant

proof_lines: N-terminally truncated mutant, pH 8.5, 25°C


proof_lines: recombinant wild-type enzyme, pH 8.9, 20°C


organism: Escherichia coli

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+


proof_lines: recombinant mutant Q350N/H171A, pH 9.0, 30°C


proof_lines:
mutant N313T/Y317G
mutant N313T and Y317G


enzyme_display_name: retinal dehydrogenase

source_db: oed

enzyme: retinal dehydrogenase

source: oed


assay_conditions_summary: pH 8.5; 303.15 K; buffer TAPS; cofactor NADP+

proof_lines: native wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C

proof_lines: recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C


proof_lines: His-tagged BADH, cosubstrate benzaldehyde


assay_conditions_summary: pH 8.5; 303.15 K; buffer TAPS; cofactor NAD+


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


substrate_name: benzaldehyde

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

proof_lines: recombinant wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C

proof_lines: native wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C

substrate: benzaldehyde


proof_lines:
His-tagged BADH, cosubstrate NADP+
His-tagged BADH, cosubstrate NAD+


enzyme_display_name: (R)-dehydropantoate dehydrogenase

organism: Pseudomonas sp.

assay_conditions_summary: cofactor NAD+

enzyme: (R)-dehydropantoate dehydrogenase


enzyme_display_name: phenylacetaldehyde dehydrogenase

organism: Rhodococcus opacus

substrate_name: phenylacetaldehyde

assay_conditions_summary: pH 7.7; cofactor NAD+

proof_lines: with NAD+ as cosubstrate, at pH 7.7, temperature not specified in the publication

enzyme: phenylacetaldehyde dehydrogenase

substrate: phenylacetaldehyde


proof_lines: with phenylacetaldehyde as cosubstrate, at pH 7.7, temperature not specified in the publication


organism: Mus musculus

assay_conditions_summary: pH 9; 298.15 K; buffer 100 mM HEPES

proof_lines: recombinant isozyme type-2, pH 9.0, 25°C

proof_lines: isoform RALDH4, in 100 mM HEPES buffer, pH 8.5, at 37°C

proof_lines: recombinant isozyme type-1, pH 7.5, 25°C


organism: Gordonia rubripertincta


organism: Achromobacter eurydice


substrate_name: Unknown

ki_unit: mM

assay_conditions_summary: pH 8.5; 310.15 K; buffer 100 mM HEPES

proof_lines: isoform RALDH4, using 13-cis retinal as substrate, in 100 mM HEPES buffer, pH 8.5, at 37°C

proof_lines: isoform RALDH4, using 9-cis retinal as substrate, in 100 mM HEPES buffer, pH 8.5, at 37°C

proof_lines: recombinant isozyme type-1, pH 7.5, 25°C, with substrate all-trans-retinal

substrate: Unknown


organism: Aromatoleum aromaticum

verification_status: corrected

sequence_source: UniProt:Q5P171 (ebA4954)

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: PMC3911259 Table 4 columns K0.5 (uM), kcat (s^-1), and kcat/K0.5 (uM^-1 s^-1): NAD Michaelis-Menten row reports 18, 53, and 3.0.

row_label: NAD (1 mM), Michaelis-Menten

table_label: PMC3911259 Table 4

status: corrected


assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: PMC3911259 Table 4 columns K0.5 (uM), kcat (s^-1), and kcat/K0.5 (uM^-1 s^-1): NADP Michaelis-Menten row reports 25, 63, and 2.5.

row_label: NADP (1 mM), Michaelis-Menten


substrate_name: acetaldehyde

substrate: acetaldehyde


enzyme_display_name: Aldehyde dehydrogenase 1A1

organism: Oryctolagus cuniculus

source_db: uniprot

smiles: CCCCCC(C=CC=O)O

enzyme: Aldehyde dehydrogenase 1A1

source: uniprot


substrate_name: malonaldehyde

smiles: C(C=O)C=O

substrate: malonaldehyde


substrate_name: propanal

substrate: propanal


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


proof_lines: pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme


organism: Rattus norvegicus

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.


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: octanal

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L459F/N460G with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

smiles: CCCCCCCC=O

proof_lines: recombinant mutant L459F/N460G, pH 8.5, 25°C

substrate: octanal


substrate_name: NAD+

substrate: NAD+


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).


organism: Bos taurus

substrate_name: all-trans retinal

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

substrate: all-trans retinal


enzyme_display_name: Retinaldehyde dehydrogenase 3

column_label: PMC5069622 biochemical characterization prose reports all-trans retinal (KM = 9.3 x 10^-6 M); this normalizes to 0.0093 mM.

raw_value_unit_evidence: Km raw_value=9.3 x 10^-6 M raw_unit=M

row_label: Prose segment: all-trans retinal

table_label: PMC5069622 Results and Discussion, Biochemical characterization prose

enzyme: Retinaldehyde dehydrogenase 3


substrate_name: NAD

column_label: Supplementary Table S1 row Variable substrate NAD+ / Fixed substrate All-trans Retinal, KM column: 4.8x10-6 M, normalized to 0.0048 mM, matching CatLog NAD Km.

normalized_value_unit_evidence: Km normalized_value=0.0048 normalized_unit=mM after M-to-mM conversion; CatLog value=0.0048 mM.

raw_value_unit_evidence: Supplementary Table S1 row Variable substrate NAD+ / Fixed substrate All-trans Retinal reports KM raw_value=4.8x10-6 raw_unit=M.

row_label: Variable substrate NAD+ / fixed substrate All-trans Retinal

table_label: Supplementary Table S1. Steady-state kinetic parameters of hALDH1A3

substrate: NAD


column_label: PMC5069622 biochemical characterization prose reports acetaldehyde (KM = 2.4 x 10^-3 M); this normalizes to 2.4 mM.

raw_value_unit_evidence: Km raw_value=2.4 x 10^-3 M raw_unit=M

row_label: Prose segment: acetaldehyde


organism: Sphingopyxis fribergensis


organism: Pseudomonas putida

substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


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

assay_conditions_summary: pH 8


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

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

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

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

row_label: Hexanal; recombinant human ALDH1A1

table_label: Table 4. Kinetic properties of recombinant human ALDH1A1


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


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

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


kcat_over_km_origin: calculated

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


enzyme_display_name: Retinal dehydrogenase 2

substrate_name: all-trans-retinal

column_label: Table II row All-trans-retinal column Km reports 0.4 +/- 0.1 uM.

raw_value_unit_evidence: Km raw_value=0.4 +/- 0.1 raw_unit=uM

row_label: All-trans-retinal

table_label: Table II. Relative efficiencies of RalDH(II)/rL for aldehyde substrates

enzyme: Retinal dehydrogenase 2


column_label: The RalDH(II)/rL and Retinal paragraph reports NAD Km 70 +/- 0.6 uM.

raw_value_unit_evidence: Km raw_value=70 +/- 0.6 raw_unit=uM

row_label: RalDH(II)/rL

table_label: Main text section RalDH(II)/rL and Retinal


substrate_name: NADP

column_label: The RalDH(II)/rL and Retinal paragraph reports NADP Km 400 +/- 7 uM.

raw_value_unit_evidence: Km raw_value=400 +/- 7 raw_unit=uM

substrate: NADP


organism: Brevibacterium sp.

substrate_name: phenylacetaldehyde

assay_conditions_summary: pH 9; buffer glycine-NaOH; cofactor NAD+

column_label: Table 3 reports Phenylacetaldehyde Km (uM) = 1.24 and Vmax = 4.63 umol min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=1.24 raw_unit=uM

row_label: Phenylacetaldehyde

table_label: Table 3 - Kinetic parameters for PADH


column_label: Table 3 reports NAD+ Km (uM) = 116 and Vmax = 4.40 umol min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=116 raw_unit=uM

row_label: NAD+


organism: Taeniopygia guttata

substrate_name: retinal

substrate: retinal


organism: Homo sapiens

substrate_name: NAD (at pH 8.0)

assay_conditions_summary: pH 7.1; 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

substrate: NAD (at pH 8.0)


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

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


substrate_name: acetaldehyde (at pH 8.0)

assay_conditions_summary: pH 8; cofactor NAD+

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.

row_label: Acetaldehyde

substrate: acetaldehyde (at pH 8.0)


substrate_name: propanal (at pH 8.0)

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)


enzyme_display_name: hexadecanal dehydrogenase (acylating)

organism: Porphyromonas gingivalis

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.15; 303.15 K; cofactor CoA

enzyme: hexadecanal dehydrogenase (acylating)

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Pseudomonas sp.

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


substrate_name: NAD+

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 8.5; 301.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 301.15 K; cofactor NADP+

substrate: NADP+


enzyme_display_name: cinnamoyl-CoA reductase

organism: Petunia x hybrida

assay_conditions_summary: pH 6; cofactor NADPH

column_label: Table 1, column p-Coumaroyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

row_label: p-Coumaroyl-CoA

table_label: Table 1. Kinetic Constants of Ph-CCR1 with Various Hydroxycinnamoyl-CoA Esters.

enzyme: cinnamoyl-CoA reductase


substrate_name: sinapoyl-CoA

column_label: Table 1, column Sinapoyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

row_label: Sinapoyl-CoA

substrate: sinapoyl-CoA


substrate_name: feruloyl-CoA

column_label: Table 1, column Feruloyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

row_label: Feruloyl-CoA

substrate: feruloyl-CoA


organism: Lathyrus oleraceus

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
aldehyde generation
alcohol generation

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Marinobacter nauticus

substrate_name: hexadecanoyl-CoA

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: hexadecanoyl-CoA


smiles: CCCCC=CCCCCCCCCCC=O


organism: Populus tomentosa

assay_conditions_summary: pH 6; 313.15 K; buffer NADPH in 100 mM phosphate; cofactor CoA

column_label: Table 2; PtoCCR7 row; p-Coumaroyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, p-Coumaroyl-CoA columns: Km 15.95 uM; kcat 1.10 min^-1; kcat/Km 0.07 uM^-1 min^-1.

row_label: PtoCCR7 / p-Coumaroyl-CoA

table_label: Table 2. Kinetic parameters of PtoCCR7


substrate_name: caffeoyl-CoA

column_label: Table 2; PtoCCR7 row; Caffeoyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, Caffeoyl-CoA columns: Km 23.76 uM; kcat 2.17 min^-1; kcat/Km 0.09 uM^-1 min^-1.

row_label: PtoCCR7 / Caffeoyl-CoA

substrate: caffeoyl-CoA


column_label: Table 2; PtoCCR7 row; Feruloyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, Feruloyl-CoA columns: Km 14.31 uM; kcat 61.95 min^-1; kcat/Km 4.33 uM^-1 min^-1.

row_label: PtoCCR7 / Feruloyl-CoA


column_label: Table 2; PtoCCR7 row; Sinapoyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, Sinapoyl-CoA columns: Km 41.02 uM; kcat 3.84 min^-1; kcat/Km 0.09 uM^-1 min^-1.

row_label: PtoCCR7 / Sinapoyl-CoA


organism: Arabidopsis thaliana

substrate_name: [hexadecanoyl]-acyl carrier protein

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM phosphate

proof_lines: in 100 mM phosphate buffer, pH 7.0, at 30°C

substrate: [hexadecanoyl]-acyl carrier protein


assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM phosphate; cofactor CoA


organism: Fragaria x ananassa

assay_conditions_summary: pH 6; cofactor CoA

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


organism: Anas platyrhynchos


enzyme_display_name: long-chain-aldehyde dehydrogenase

organism: Simmondsia chinensis

substrate_name: decyl aldehyde

enzyme: long-chain-aldehyde dehydrogenase

substrate: decyl aldehyde


assay_conditions_summary: cofactor NAD+

substrate: NAD+


enzyme_display_name: formaldehyde dehydrogenase

organism: Ogataea angusta

substrate_name: formaldehyde

proof_lines: KM value of the used FdDH in solution from the wild strains

enzyme: formaldehyde dehydrogenase

substrate: formaldehyde


proof_lines: immobilized enzyme in a bioactive layer on the transducer surface, apparent Michaelis-Menten constant derived from the formaldehyde calibration curves is 120 mM with a linear detection range for formaldehyde up to 20 mM


organism: Forsythia suspensa

assay_conditions_summary: cofactor CoA


enzyme_display_name: Cinnamoyl-CoA reductase 1

organism: Medicago truncatula

substrate_name: feruloyl-CoA (at pH 6.25 and 30 degrees Celsius)

assay_conditions_summary: pH 6.25; cofactor CoA

proof_lines: kcat is 60.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 5.5 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 3.1 min(-1) with ca

enzyme: Cinnamoyl-CoA reductase 1


substrate_name: sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate_name: caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate_name: coumaroyl-CoA (at pH 6.25 and 30 degrees Celsius)


enzyme_display_name: Cinnamoyl-CoA reductase 2

proof_lines: kcat is 18.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 12.0 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 9.0 min(-1) with c

enzyme: Cinnamoyl-CoA reductase 2

substrate: feruloyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate: sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate: caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate: coumaroyl-CoA (at pH 6.25 and 30 degrees Celsius)


organism: Solanum lycopersicum


substrate_name: coumaroyl-CoA

substrate: coumaroyl-CoA


organism: Leucaena leucocephala

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S212G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S212G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R51G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R51G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D77G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D77G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V200E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V200E, pH and temperature not specified in the publication


organism: Populus tremuloides

column_label: Table 1 row Caffeoyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.0763 mM; kcat 0.0116667 s^-1; no explicit kcat/Km column; exported kcat and kcat_over_km are not supported in s^-1 units.

row_label: Caffeoyl-CoA

table_label: Table 1 Kinetic properties of CCR catalysis with various cinnamoyl-CoA esters


column_label: Table 1 row 5-Hydroxyferuloyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.099 mM; kcat 0.0816667 s^-1; no explicit kcat/Km column; exported kcat and kcat_over_km are not supported in s^-1 units.

raw_value_unit_evidence: Table 1 row 5-Hydroxyferuloyl-CoA: Km 99.0 +/- 1.0 uM; Vmax 97.0 +/- 3.0 uM min^-1; Kcat 4.9 +/- 0.2 min^-1.


column_label: Table 1 row Sinapoyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.1045 mM; kcat 0.0883333 s^-1; no explicit kcat/Km column; exported kcat and kcat_over_km are not supported in s^-1 units.


column_label: Table 1 row feruloyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.0137 mM; kcat 0.13 s^-1; no explicit kcat/Km column; exported kcat_over_km is not supported as s^-1 mM^-1.

row_label: feruloyl-CoA


organism: Pinus massoniana

proof_lines: at pH 6.0, temperature not specified in the publication


organism: Pinus koraiensis


enzyme_display_name: Cinnamoyl-CoA reductase CAD2

substrate_name: coumaraldehyde (at pH 6.25 and 30 degrees Celsius)

proof_lines: kcat is 0.46 sec(-1) with coumaraldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.10 sec(-1) with coniferaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.24 sec(-1)

enzyme: Cinnamoyl-CoA reductase CAD2


substrate_name: coniferaldehyde (at pH 6.25 and 30 degrees Celsius)


substrate_name: sinapaldehyde (at pH 6.25 and 30 degrees Celsius)


organism: Bacillus subtilis (strain 168)


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

assay_conditions_summary: pH 7; cofactor CoA

substrate: hexadecanal


substrate_name: feruloyl-CoA


substrate_name: sinapoyl-CoA


enzyme_display_name: UniProt A0A059TC02

organism: Petunia x hybrida

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

assay_conditions_summary: pH 6; 298.15 K; cofactor CoA

proof_lines: kcat is 1.2 sec(-1) with p-coumaroyl-CoA as substrate (PubMed:25217505). kcat is 5.8 sec(-1) with feruloyl-CoA as substrate (PubMed:25217505). kcat is 3.4 sec(-1) with sinapoyl-CoA as substrate (PubMed:25217505).

source_databases_merged: skid uniprot

enzyme: UniProt A0A059TC02


enzyme_display_name: Aminoaldehyde dehydrogenase 1

smiles: C(CC=O)CN

assay_conditions_summary: pH 9; cofactor NAD+

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


smiles: C(CN)C=O

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


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

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

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

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 +


enzyme_display_name: Aminoaldehyde dehydrogenase 2

column_label: Table 3; row ABAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.054 mM converted from 54 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / ABAL Km 54 +/- 5 uM

row_label: SlAMADH2 / ABAL

enzyme: Aminoaldehyde dehydrogenase 2


column_label: Table 3; row APAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.009 mM converted from 9 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / APAL Km 9 +/- 1.4 uM

row_label: SlAMADH2 / APAL


column_label: Table 3; row TMABAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.141 mM converted from 141 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / TMABAL Km 141 +/- 17 uM

row_label: SlAMADH2 / TMABAL


column_label: Table 3; row GBAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.022 mM converted from 22 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / GBAL Km 22 +/- 3 uM

row_label: SlAMADH2 / GBAL


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

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

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


column_label: Table 4; row ABAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.059 mM converted from 59 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / ABAL Km 59 +/- 2 uM

row_label: ZmAMADH2 / ABAL


column_label: Table 4; row APAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.098 mM converted from 98 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / APAL Km 98 +/- 8 uM

row_label: ZmAMADH2 / APAL


column_label: Table 4; row TMABAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.016 mM converted from 16 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / TMABAL Km 16 +/- 1.1 uM

row_label: ZmAMADH2 / TMABAL


column_label: Table 4; row GBAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / GBAL Km 11 +/- 1.2 uM

row_label: ZmAMADH2 / GBAL


column_label: Table 4; row NAD +; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.086 mM converted from 86 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / NAD + Km 86 +/- 3 uM

row_label: ZmAMADH2 / NAD +


enzyme_display_name: Aminoaldehyde dehydrogenase 1b

column_label: Table 4; row ABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.026 mM converted from 26 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / ABAL Km 26 +/- 4 uM

row_label: ZmAMADH1b / ABAL

enzyme: Aminoaldehyde dehydrogenase 1b


column_label: Table 4; row APAL; ZmAMADH1b Km column

raw_value_unit_evidence: Table 4 ZmAMADH1b / APAL Km 11 +/- 2 uM

row_label: ZmAMADH1b / APAL


column_label: Table 4; row TMABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.01 mM converted from 10 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / TMABAL Km 10 +/- 2 uM

row_label: ZmAMADH1b / TMABAL


column_label: Table 4; row GBAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.005 mM converted from 5 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / GBAL Km 5 +/- 1 uM

row_label: ZmAMADH1b / GBAL


column_label: Table 4; row BAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.029 mM converted from 29 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / BAL Km 29 +/- 4 uM

row_label: ZmAMADH1b / BAL


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 +


column_label: Table 4; row ABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.028 mM converted from 28 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / ABAL Km 28 +/- 3 uM

row_label: ZmAMADH1a / ABAL


column_label: Table 4; row APAL; ZmAMADH1a Km column

raw_value_unit_evidence: Table 4 ZmAMADH1a / APAL Km 9 +/- 2 uM

row_label: ZmAMADH1a / APAL


column_label: Table 4; row TMABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.006 mM converted from 6 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / TMABAL Km 6 +/- 0.8 uM

row_label: ZmAMADH1a / TMABAL


column_label: Table 4; row GBAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.003 mM converted from 3 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / GBAL Km 3 +/- 0.7 uM

row_label: ZmAMADH1a / GBAL


column_label: Table 3; row NAD +; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.089 mM converted from 89 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / NAD + Km 89 +/- 3 uM

row_label: SlAMADH2 / NAD +


substrate_name: Feruloyl-CoA

assay_conditions_summary: pH 6.25; 303.15 K; cofactor CoA

substrate: Feruloyl-CoA


substrate_name: caffeoyl-CoA


substrate: sinapoyl-CoA


column_label: ScienceDirect PMID 11430991 Table 1 row Feruloyl-CoA under Km (uM) AtCCR1 reports 0.96.

raw_value_unit_evidence: Feruloyl-CoA Km AtCCR1 0.96 uM

row_label: Feruloyl-CoA

table_label: PMID 11430991 Table 1. Kinetic parameters of AtCCR1 and AtCCR2 fusion proteins

substrate: feruloyl-CoA


substrate_name: p-coumaroyl-CoA

column_label: ScienceDirect PMID 16122934 Table 1 row p-Coumaroyl-CoA under Km +/- S.D. (uM) reports 2.27 +/- 0.07.

raw_value_unit_evidence: p-Coumaroyl-CoA Km 2.27 +/- 0.07 uM

row_label: p-Coumaroyl-CoA

table_label: PMID 16122934 Table 1. Kinetic parameters for recombinant AtCCR1

substrate: p-coumaroyl-CoA


column_label: ScienceDirect PMID 11430991 Table 1 row Sinapoyl-CoA under Km (uM) AtCCR1 reports 6.32.

raw_value_unit_evidence: Sinapoyl-CoA Km AtCCR1 6.32 uM

row_label: Sinapoyl-CoA


substrate: caffeoyl-CoA


organism: Homo sapiens


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: formaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: butyraldehyde

smiles: CCCC=O

substrate: butyraldehyde


substrate_name: hexanaldehyde

smiles: CCCCCC=O

substrate: hexanaldehyde


assay_conditions_summary: pH 9


substrate: formaldehyde


assay_conditions_summary: pH 9; cofactor NADPH


organism: Sorghum bicolor

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T154A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA


column_label: PMID 27956488 / PMCID PMC5291045 / DOI 10.1104/pp.16.01671, Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / p-Coumaroyl-CoA (4-coumaroyl-CoA), kcat, Km, and kcat/Km columns for the expected substrate/mutation context.

raw_value_unit_evidence: Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / p-Coumaroyl-CoA (4-coumaroyl-CoA): kcat 0.05 s^-1; Km 100 uM; kcat/Km 0.0005 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProt C5YLL4 plus paper-linked PDB 5TQM and applied mutation signature T154Y to reconstruct the assayed variant sequence.

column_label: PMID 27956488 / PMCID PMC5291045, Table V, row T154Y / p-Coumaroyl-CoA (4-coumaroyl-CoA), columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1), with the Enzyme Kinetic Assays conditions.

normalized_value_unit_evidence: Same-row central values: kcat 8.42 s^-1; Km 0.113 mM; independently printed kcat/Km 74.5 s^-1 mM^-1.

raw_value_unit_evidence: Table V row T154Y / p-Coumaroyl-CoA (4-coumaroyl-CoA): kcat 8.42 s^-1; Km 113 uM; independently printed kcat/Km 0.0745 uM^-1 s^-1.

table_label: Table V


column_label: PMID 27956488 / PMCID PMC5291045, Table IV, row Wild-type SbCCR1 / Caffeoyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1), with the Enzyme Kinetic Assays conditions.

normalized_value_unit_evidence: Same-row central values: kcat 0.01 s^-1; Km 0.014 mM; independently printed kcat/Km 0.8 s^-1 mM^-1.

raw_value_unit_evidence: Table IV row Wild-type SbCCR1 / Caffeoyl-CoA: kcat 0.01 s^-1; Km 14 uM; independently printed kcat/Km 0.0008 uM^-1 s^-1.

row_label: Wild-type SbCCR1 / Caffeoyl-CoA

table_label: Table IV


column_label: PMID 27956488 / PMCID PMC5291045 / DOI 10.1104/pp.16.01671, Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / Feruloyl-CoA, kcat, Km, and kcat/Km columns for the expected substrate/mutation context.

raw_value_unit_evidence: Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / Feruloyl-CoA: kcat 3.96 s^-1; Km 70 uM; kcat/Km 0.0566 uM^-1 s^-1.

row_label: Wild-type SbCCR1 / Feruloyl-CoA


sequence_source: UniProt C5YLL4 plus paper-linked PDB 5TQM

column_label: PMID 27956488 / PMCID PMC5291045, Table V, row T154Y / Feruloyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1), with the Enzyme Kinetic Assays conditions.

normalized_value_unit_evidence: Same-row central values: kcat 17.24 s^-1; Km 0.063 mM; independently printed kcat/Km 273.6 s^-1 mM^-1.

raw_value_unit_evidence: Table V row T154Y / Feruloyl-CoA: kcat 17.24 s^-1; Km 63 uM; independently printed kcat/Km 0.2736 uM^-1 s^-1.

row_label: T154Y / Feruloyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y310F to reconstruct the assayed variant sequence.


enzyme_display_name: Aminoaldehyde dehydrogenase BADH

organism: Spinacia oleracea

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Primary PMC HTML Table I BAL section, Wild type row, Km column = 69 +/- 5 uM.

normalized_value_unit_evidence: Normalized paper Km: 69 uM = 0.069 mM, matching export Km 0.069 mM.

raw_value_unit_evidence: Table I BAL wild-type row reports Km 69 +/- 5 uM.

row_label: BAL section; Wild type row; Km column

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

enzyme: Aminoaldehyde dehydrogenase BADH


column_label: Primary PMC HTML Table I ABAL section, Wild type row, Km column = 5.5 +/- 0.6 uM.

normalized_value_unit_evidence: Normalized paper Km: 5.5 uM = 0.0055 mM, matching export Km 0.0055 mM.

raw_value_unit_evidence: Table I ABAL wild-type row reports Km 5.5 +/- 0.6 uM.

row_label: ABAL section; Wild type row; Km column


column_label: Primary PMC HTML Table I APAL section, Wild type row, Km column = 2.6 +/- 0.3 uM.

normalized_value_unit_evidence: Normalized paper Km: 2.6 uM = 0.0026 mM, matching export Km 0.0026000000000000003 mM.

raw_value_unit_evidence: Table I APAL wild-type row reports Km 2.6 +/- 0.3 uM.

row_label: APAL section; Wild type row; Km column


column_label: Primary PMC HTML Table I TMABAL section, Wild type row, Km column = 3.6 +/- 0.2 uM.

normalized_value_unit_evidence: Normalized paper Km: 3.6 uM = 0.0036 mM, matching export Km 0.0036000000000000003 mM.

raw_value_unit_evidence: Table I TMABAL wild-type row reports Km 3.6 +/- 0.2 uM.

row_label: TMABAL section; Wild type row; Km column


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal

organism: Arabidopsis thaliana

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

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

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

row_label: AtALDH10A9 / Km column / TMABAL row

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


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

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

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

row_label: AtALDH10A9 / Km column / GBAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

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

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

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

row_label: AtALDH10A8 / Km column / TMABAL row


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

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

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

row_label: AtALDH10A8 / Km column / GBAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic


substrate_name: NAD

proof_lines:
ALDH9A1
substrate specificity
NAD

substrate: NAD


substrate_name: NADP

proof_lines:
ALDH9A1
coenzyme specificity
NADP

substrate: NADP


substrate_name: gamma-trimethylaminobutyraldehyde

substrate: gamma-trimethylaminobutyraldehyde


substrate_name: heptanal

smiles: CCCCCCC=O

proof_lines:
ALDH9A1
aldehyde specificity
heptanal

substrate: heptanal


substrate_name: octanal

proof_lines:
ALDH9A1
aldehyde specificity
octanal

substrate: octanal


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

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


column_label: Table 1, column p-Coumaroyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)


substrate_name: feruloyl-CoA

column_label: Table 1, column Feruloyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)


substrate_name: sinapoyl-CoA

column_label: Table 1, column Sinapoyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; cofactor 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+

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


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

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

normalized_value_unit_evidence: Km normalized_value=1.63 normalized_unit=mM converted from 1630 microM.

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

row_label: Rat liver TMABA-DH / NADP+


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

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

normalized_value_unit_evidence: Km normalized_value=0.0014 normalized_unit=mM converted from 1.4 microM.

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


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 (microM).

normalized_value_unit_evidence: Km normalized_value=0.006 normalized_unit=mM converted from 6 microM.

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

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


enzyme_display_name: glutamate-5-semialdehyde dehydrogenase

substrate_name: NADP+

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

enzyme: glutamate-5-semialdehyde dehydrogenase

substrate: NADP+


substrate_name: L-glutamate 5-semialdehyde

assay_conditions_summary: cofactor NADP+

column_label: Abstract prose reports apparent Km values: 1.8 mM for pyrroline 5-carboxylate; this is the radiochemical assay substrate for the gamma-glutamate semialdehyde dehydrogenase paper.

raw_value_unit_evidence: apparent Km = 1.8 mM for pyrroline 5-carboxylate

row_label: pyrroline 5-carboxylate assay substrate for gamma-glutamate semialdehyde dehydrogenase

table_label: PubMed/NCBI abstract prose

substrate: L-glutamate 5-semialdehyde


substrate_name: phosphate

column_label: Abstract prose reports apparent Km values including 11.3 mM for phosphate.

raw_value_unit_evidence: apparent Km = 11.3 mM for phosphate

row_label: phosphate

substrate: phosphate


enzyme_display_name: Aldehyde dehydrogenase family 3 member B1

smiles: CCCCCCCC=O

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

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

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

row_label: 3xFLAG-ALDH3B1 oxidation of octanal

table_label: Figure 3 / ALDH3B1 exhibits activity toward C16 aldehydes


substrate_name: hexadecanal

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

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

row_label: 3xFLAG-ALDH3B1 oxidation of hexadecanal

enzyme: Aldehyde dehydrogenase family 3 member B1

substrate: hexadecanal


smiles: CCCCCCCCCCCCCC=CC=O

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

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

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


organism: Pseudomonas aeruginosa (strain LESB58)

substrate_name: formaldehyde

smiles: C=O

proof_lines:
formaldehyde activity
P. aeruginosa FDH


substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

proof_lines:
NAD+ binding
P. aeruginosa FDH

substrate: NAD(+)


organism: Fragaria x ananassa

column_label: Table 1 row feruloyl-CoA gives Km 16.11 microM, Kcat 2.34 x 10^-3 s^-1, and Kcat/Km 1.45 x 10^-4 s^-1 microM^-1.

normalized_value_unit_evidence: Km normalized_value=0.01611 mM; Kcat normalized_value=0.00234 s^-1; Kcat/Km normalized_value=0.145 s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=16.11 microM; Kcat raw_value=2.34 x 10^-3 s^-1; Kcat/Km raw_value=1.45 x 10^-4 s^-1 microM^-1

row_label: GST-FaCCR / feruloyl-CoA

table_label: Official PMC full-text Table 1: Kinetic parameters for recombinant GST-FaCCR

substrate: feruloyl-CoA


substrate_name: propanal

assay_conditions_summary: pH 9; buffer 0.1 M sodium pyrophosphate

column_label: Table 3; row Km propionaldehyde (0.5 mM NAD); column Cytoplasmic rat liver isozyme.

normalized_value_unit_evidence: Km 0.0075 mM from 7.5 microM.

raw_value_unit_evidence: Table 3 row Km propionaldehyde (0.5 mM NAD), column Cytoplasmic rat liver isozyme: 7.5 +/- 1.3 microM (n=3). Footnote: propionaldehyde Km determined in 0.1 M sodium pyrophosphate buffer, pH 9.0.

row_label: Km propionaldehyde (0.5 mM NAD) / cytoplasmic rat liver isozyme

table_label: Table 3. Kinetic properties of partially purified cytoplasmic rat liver aldehyde dehydrogenase metabolizing gamma-aminobutyraldehyde and comparison with homogeneous E3 isozyme from human liver

substrate: propanal


organism: Populus tomentosa

assay_conditions_summary: pH 6; 313.15 K; cofactor CoA

proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant A132T


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant F155Y


proof_lines: pH 6.0, 40°C, recombinant His-tagged enzyme

proof_lines: pH 6.25, 37°C, recombinant His-tagged enzyme


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant A132S


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate: sinapoyl-CoA


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant A43V


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant F155H


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant L192M


proof_lines: pH 6.0, 40°C, recombinant His-tagged wild-type enzyme


substrate_name: betaine aldehyde

substrate: betaine aldehyde


organism: Pseudomonas putida

substrate_name: n-Hexanol

smiles: CCCCCCO

substrate: n-Hexanol


substrate_name: Isopentanol

smiles: CC(C)CCO

substrate: Isopentanol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


substrate_name: n-Pentanol

smiles: CCCCCO

substrate: n-Pentanol


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


substrate_name: isobutanol

smiles: CC(C)CO

substrate: isobutanol


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


enzyme_display_name: phenylacetaldehyde dehydrogenase

organism: Escherichia coli

substrate_name: benzaldehyde

enzyme: phenylacetaldehyde dehydrogenase

substrate: benzaldehyde


substrate_name: NAD+

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: with phenylacetaldehyde as cosubstrate, at pH 7.7, temperature not specified in the publication

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

substrate: NADP+


substrate_name: hexanal

substrate: hexanal


substrate_name: Heptanal

substrate: Heptanal


substrate_name: phenylacetaldehyde

proof_lines: with NAD+ as cosubstrate, at pH, temperature not specified in the publication

substrate: phenylacetaldehyde


enzyme_display_name: cinnamoyl-CoA reductase

substrate_name: caffeoyl-CoA

enzyme: cinnamoyl-CoA reductase

substrate: caffeoyl-CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


organism: Glycine max

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
cosubstrate feruloyl-CoA
cosubstrate sinapoyl-CoA
cosubstrate p-coumaroyl-CoA

substrate: NADPH


assay_conditions_summary: cofactor CoA


substrate_name: p-Coumaroyl-CoA

substrate: p-Coumaroyl-CoA


substrate_name: sinapoyl-CoA

substrate: sinapoyl-CoA


substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


enzyme_display_name: aspartate-semialdehyde dehydrogenase

enzyme: aspartate-semialdehyde dehydrogenase


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


substrate_name: N-acetyl-L-glumate 5-semialdehyde

substrate: N-acetyl-L-glumate 5-semialdehyde


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: 2-oxoaldehyde dehydrogenase (NADP+)

organism: Capra hircus

substrate_name: NADP+; H2O; Methylglyoxal

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

enzyme: 2-oxoaldehyde dehydrogenase (NADP+)

substrate: NADP+; H2O; Methylglyoxal


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Vicia faba

substrate_name: gamma-guanidinobutyraldehyde

substrate: gamma-guanidinobutyraldehyde


substrate_name: gamma-aminobutyraldehyde

smiles: C(CC=O)CN

substrate: gamma-aminobutyraldehyde


substrate_name: NAD+

substrate: NAD+


organism: Ovis aries

substrate_name: H2O; Methylglyoxal; NADP+

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

substrate: H2O; Methylglyoxal; NADP+


proof_lines: amine as activator in aldehyde oxidation

proof_lines: in the presence of L-2-aminopropan-1-ol (Km 83 mM), at pH 9.3 and 25°C


enzyme_display_name: long-chain acyl-protein thioester reductase

organism: Anas platyrhynchos

substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


enzyme: long-chain acyl-protein thioester reductase


proof_lines: in the presence of L-serine methyl ester (Km 8.0 mM)


substrate_name: NADP+

substrate: NADP+


enzyme_display_name: pyruvate dehydrogenase (NADP+)

organism: Euglena gracilis

substrate_name: CoA

proof_lines:
with NADP+
with methyl viologen

source_databases_merged: brenda uniprot

enzyme: pyruvate dehydrogenase (NADP+)

substrate: CoA


substrate_name: pyruvate

substrate: pyruvate


substrate_name: H2O; NADP+; Methylglyoxal

substrate: H2O; NADP+; Methylglyoxal


organism: Zea mays

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Table 4; row ABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.026 mM converted from 26 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / ABAL Km 26 +/- 4 uM

row_label: ZmAMADH1b / ABAL


smiles: C(CN)C=O

column_label: Table 4; row APAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / APAL Km 11 +/- 2 uM

row_label: ZmAMADH1b / APAL


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

column_label: Table 4; row TMABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.01 mM converted from 10 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / TMABAL Km 10 +/- 2 uM

row_label: ZmAMADH1b / TMABAL


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

column_label: Table 4; row GBAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.005 mM converted from 5 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / GBAL Km 5 +/- 1 uM

row_label: ZmAMADH1b / GBAL


substrate_name: betaine aldehyde

column_label: Table 4; row BAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.029 mM converted from 29 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / BAL Km 29 +/- 4 uM

row_label: ZmAMADH1b / BAL

substrate: betaine aldehyde


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

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 +


column_label: Table 4; row ABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.028 mM converted from 28 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / ABAL Km 28 +/- 3 uM

row_label: ZmAMADH1a / ABAL


column_label: Table 4; row APAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.009 mM converted from 9 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / APAL Km 9 +/- 2 uM

row_label: ZmAMADH1a / APAL


column_label: Table 4; row TMABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.006 mM converted from 6 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / TMABAL Km 6 +/- 0.8 uM

row_label: ZmAMADH1a / TMABAL


column_label: Table 4; row GBAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.003 mM converted from 3 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / GBAL Km 3 +/- 0.7 uM

row_label: ZmAMADH1a / GBAL


organism: Solanum lycopersicum

column_label: Table 3; row NAD +; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.089 mM converted from 89 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / NAD + Km 89 +/- 3 uM

row_label: SlAMADH2 / NAD +

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


enzyme_display_name: butanal dehydrogenase

organism: Clostridium acetobutylicum

substrate_name: Acetyl-CoA; NADH; H+

assay_conditions_summary: cofactor NADH

enzyme: butanal dehydrogenase

substrate: Acetyl-CoA; NADH; H+


substrate_name: NADH

substrate: NADH


substrate_name: NADPH

substrate: NADPH


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


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


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


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

column_label: Table 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and the coenzyme NAD+, row BAL, column SlAMADH1 Km; Km, cell 2051 +/- 83 uM, normalized 2.051 mM

raw_value_unit_evidence: Km raw 2051 +/- 83 uM from Table 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and the coenzyme NAD+, row BAL, column SlAMADH1 Km

row_label: SlAMADH1 / BAL


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 +


column_label: Table 3; row ABAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.054 mM converted from 54 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / ABAL Km 54 +/- 5 uM

row_label: SlAMADH2 / ABAL


column_label: Table 3; row APAL; SlAMADH2 Km column

raw_value_unit_evidence: Table 3 SlAMADH2 / APAL Km 9 +/- 1.4 uM

row_label: SlAMADH2 / APAL


column_label: Table 3; row TMABAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.141 mM converted from 141 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / TMABAL Km 141 +/- 17 uM

row_label: SlAMADH2 / TMABAL


column_label: Table 3; row GBAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.022 mM converted from 22 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / GBAL Km 22 +/- 3 uM

row_label: SlAMADH2 / GBAL


organism: Levilactobacillus brevis

assay_conditions_summary: pH 7.15; 303.15 K; cofactor CoA


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

organism: Corynebacterium glutamicum

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)


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


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


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


organism: Daucus carota


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+


organism: Pyrococcus woesei

sequence_source: multiple

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


organism: Pyrobaculum calidifontis

substrate_name: D-glyceraldehyde 3-phosphate

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

assay_conditions_summary: pH 7; cofactor NADP+

proof_lines: recombinant enzyme, pH 7.0, 80°C, with NAD+

proof_lines: recombinant enzyme, pH 7.0, 80°C, with NADP+

substrate: D-glyceraldehyde 3-phosphate


substrate_name: NADP+

substrate: NADP+


assay_conditions_summary: pH 7; cofactor NAD+


enzyme_display_name: Vanillin dehydrogenase

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

substrate_name: vanillin in the presence of 0.5 mM NAD(+) (at pH 7.0)

assay_conditions_summary: pH 7

proof_lines: kcat is 21.03 sec(-1) with vanillin as substrate in the presence of 0.5 mM NAD(+). kcat is 23.42 sec(-1) with 3,4-dihydroxybenzaldehyde as substrate in the presence of 0.5 mM NAD(+). kcat is 22.92 sec(-1) with 4-hydroxybenzaldehyde as subst

enzyme: Vanillin dehydrogenase


substrate_name: 3,4-dihydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: 4-hydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: NAD(+) in the presence of 1 mM vanillin

assay_conditions_summary: cofactor NAD+

substrate: NAD(+) in the presence of 1 mM vanillin


substrate_name: NADP(+) in the presence of 1 mM vanillin

assay_conditions_summary: cofactor NADP+


organism: Pyrococcus furiosus

assay_conditions_summary: 323.15 K; cofactor NADPH


assay_conditions_summary: 323.15 K; cofactor NADH


organism: Synechocystis sp.


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

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 +


enzyme_display_name: Aminoaldehyde dehydrogenase 2

column_label: Table 4; row ABAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.059 mM converted from 59 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / ABAL Km 59 +/- 2 uM

row_label: ZmAMADH2 / ABAL

enzyme: Aminoaldehyde dehydrogenase 2


column_label: Table 4; row APAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.098 mM converted from 98 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / APAL Km 98 +/- 8 uM

row_label: ZmAMADH2 / APAL


column_label: Table 4; row TMABAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.016 mM converted from 16 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / TMABAL Km 16 +/- 1.1 uM

row_label: ZmAMADH2 / TMABAL


column_label: Table 4; row GBAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / GBAL Km 11 +/- 1.2 uM

row_label: ZmAMADH2 / GBAL


column_label: Table 4; row NAD +; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.086 mM converted from 86 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / NAD + Km 86 +/- 3 uM

row_label: ZmAMADH2 / NAD +


organism: Bacillus subtilis (strain 168)

substrate_name: NADP (at pH 9.2 and 25 degrees Celsius)

proof_lines: kcat is 1 sec(-1) for dehydrogenase activity with NAD (at pH 9.2 and 25 degrees Celsius). kcat is 8 sec(-1) for dehydrogenase activity with NADP (at pH 9.2 and 25 degrees Celsius).

substrate: NADP (at pH 9.2 and 25 degrees Celsius)


substrate_name: NAD (at pH 9.2 and 25 degrees Celsius)

substrate: NAD (at pH 9.2 and 25 degrees Celsius)


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; cofactor NADP+

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


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit beta

organism: Aromatoleum evansii

substrate_name: phenylglyoxylate (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


substrate_name: coenzyme-A (under anaerobic conditions at 37 degrees Celsius and pH 7.8)

enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit beta


substrate_name: NAD (under anaerobic conditions at 37 degrees Celsius and pH 7.8)

assay_conditions_summary: pH 7.8; cofactor NAD+


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit delta

substrate: phenylglyoxylate (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


assay_conditions_summary: cofactor CoA

enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit delta

substrate: coenzyme-A (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


substrate: NAD (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon


enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit gamma


assay_conditions_summary: pH 7.8; cofactor CoA

column_label: Results prose and Table 6 property row Apparent Km values; substrate CoA; metric Km; raw value 55 uM; normalized value 0.055 mM.

raw_value_unit_evidence: Apparent Km value 55 uM CoA.

row_label: Apparent Km values / CoA

table_label: Results prose and Table 6. Properties of the new enzyme phenylglyoxylate:acceptor oxidoreductase from A. evansii

enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit gamma


column_label: Results prose and Table 6 property row Apparent Km values; substrate NAD+; metric Km; raw value 74 uM; normalized value 0.074 mM.

raw_value_unit_evidence: Apparent Km value 74 uM NAD+.

row_label: Apparent Km values / NAD+


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit alpha

column_label: Results prose and Table 6 property row Apparent Km values; substrate phenylglyoxylate; metric Km; raw value 45 uM; normalized value 0.045 mM.

normalized_value_unit_evidence: 45 uM = 0.045 mM phenylglyoxylate.

raw_value_unit_evidence: Apparent Km value 45 uM phenylglyoxylate.

row_label: Apparent Km values / phenylglyoxylate


enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit alpha


organism: Methanothermus fervidus

substrate_name: NADPH


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating)

sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature D35G to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row D35G / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.54+/-0.07, Kcat 382+/-32, Kcat/Km 707+/-82.

normalized_value_unit_evidence: Km normalized_value=0.54 normalized_unit=mM; kcat normalized_value=6.366666666667 normalized_unit=s^-1; kcat/Km normalized_value=11.783333333333 normalized_unit=s^-1 mM^-1.

row_label: D35G / NAD


sequence_variant_note: Mutation signature D35G/L36T/P192S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating)


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature D35G/L36T/T37K to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M1(D35G/L36T/T37K) / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.47+/-0.03, Kcat 252+/-33, Kcat/Km 536+/-48.

normalized_value_unit_evidence: Km normalized_value=0.47 normalized_unit=mM; kcat normalized_value=4.2 normalized_unit=s^-1; kcat/Km normalized_value=8.933333333333 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature D35G/L36T/T37K/P192S to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M3(D35G/L36T/T37K/P192S) / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.10+/-0.014, Kcat 164+/-12, Kcat/Km 1640+/-108.

normalized_value_unit_evidence: Km normalized_value=0.1 normalized_unit=mM; kcat normalized_value=2.733333333333 normalized_unit=s^-1; kcat/Km normalized_value=27.333333333333 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature L36T to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row L36T / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.14+/-0.02, Kcat 87+/-6, Kcat/Km 620+/-132.

normalized_value_unit_evidence: Km normalized_value=0.14 normalized_unit=mM; kcat normalized_value=1.45 normalized_unit=s^-1; kcat/Km normalized_value=10.333333333333 normalized_unit=s^-1 mM^-1.

row_label: L36T / NAD


column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row D35G / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.83+/-0.12, Kcat 178+/-11, Kcat/Km 215+/-22.

normalized_value_unit_evidence: Km normalized_value=0.83 normalized_unit=mM; kcat normalized_value=2.966666666667 normalized_unit=s^-1; kcat/Km normalized_value=3.583333333333 normalized_unit=s^-1 mM^-1.

row_label: D35G / NADP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01651 and applied mutation signature D35G/L36T/T37K to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M1(D35G/L36T/T37K) / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.10+/-0.01, Kcat 480+/-36, Kcat/Km 4800+/-232.

normalized_value_unit_evidence: Km normalized_value=0.1 normalized_unit=mM; kcat normalized_value=8 normalized_unit=s^-1; kcat/Km normalized_value=80 normalized_unit=s^-1 mM^-1.


column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M3(D35G/L36T/T37K/P192S) / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.070+/-0.003, Kcat 428+/-45, Kcat/Km 5868+/-352.

normalized_value_unit_evidence: Km normalized_value=0.07 normalized_unit=mM; kcat normalized_value=7.133333333333 normalized_unit=s^-1; kcat/Km normalized_value=97.8 normalized_unit=s^-1 mM^-1.


column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row L36T / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 1.46+/-0.35, Kcat 95+/-9, Kcat/Km 65+/-9.

normalized_value_unit_evidence: Km normalized_value=1.46 normalized_unit=mM; kcat normalized_value=1.583333333333 normalized_unit=s^-1; kcat/Km normalized_value=1.083333333333 normalized_unit=s^-1 mM^-1.

row_label: L36T / NADP


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

assay_conditions_summary: pH 8; cofactor NADPH

column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Reduction / NADPH, K_m (mM) column = 0.18 +/- 0.07 mM (paper variable substrate NADPH).

raw_value_unit_evidence: Table 4 row Reduction / NADPH, K_m column: 0.18 +/- 0.07 mM; fixed substrate: 10 mM 3-PG; Vmax column: 86.9 +/- 22.1 U/mg; Ki column: 0.035 +/- 0.015 mM (Ki1 Ki2 Ki3). For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Reduction / NADPH

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


column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Oxidation / NADP+, K_m (mM) column = 0.28 +/- 0.08 mM (paper variable substrate NADP+).

raw_value_unit_evidence: Table 4 row Oxidation / NADP+, K_m column: 0.28 +/- 0.08 mM; fixed substrate: 10 mM DL-GAP, 10 mM phosphate; Vmax column: 8.2 +/- 1.5 U/mg; Ki column: 0.75 +/- 0.21 mM. For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Oxidation / NADP+


substrate_name: 3-phospho-D-glyceroyl phosphate

assay_conditions_summary: pH 8

substrate: 3-phospho-D-glyceroyl phosphate


column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Oxidation / NAD+, K_m (mM) column = 16.8 +/- 8.9 mM (paper variable substrate NAD+).

raw_value_unit_evidence: Table 4 row Oxidation / NAD+, K_m column: 16.8 +/- 8.9 mM; fixed substrate: 10 mM DL-GAP, 10 mM phosphate; Vmax column: 14.5 +/- 5.5 U/mg; Ki column: 10.7 +/- 5.3 mM. For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Oxidation / NAD+


substrate_name: phosphate

assay_conditions_summary: pH 8; cofactor NAD+

column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Oxidation / Phosphate, K_m (mM) column = 107 +/- 22 mM (paper variable substrate Phosphate).

normalized_value_unit_evidence: km=107 mM

raw_value_unit_evidence: Table 4 row Oxidation / Phosphate, K_m column: 107 +/- 22 mM; fixed substrate: 10 mM DL-GAP, 1 mM NADP+; Vmax column: 48.4 +/- 7.4 U/mg; Ki column: -. For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Oxidation / Phosphate

substrate: phosphate


enzyme_display_name: Aminoaldehyde dehydrogenase 2, peroxisomal

organism: Pisum sativum

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

column_label: Table 3; row APAL / 3-aminopropanal; column PsAMADH2 Km (uM); raw 10 uM; normalized 0.01 mM.

raw_value_unit_evidence: Table 3 row APAL / 3-aminopropanal gives PsAMADH2 Km 10 uM.

row_label: APAL / 3-aminopropanal (PsAMADH2; UniProt Q93YB2)

table_label: PMID 20026072, Table 3: kinetic parameters of PsAMADHs for the natural substrates and coenzyme NAD+


column_label: Table 3; row ABAL / 4-aminobutanal; column PsAMADH2 Km (uM); raw 29 uM; normalized 0.029 mM.

raw_value_unit_evidence: Table 3 row ABAL / 4-aminobutanal gives PsAMADH2 Km 29 uM.

row_label: ABAL / 4-aminobutanal (PsAMADH2; UniProt Q93YB2)

enzyme: Aminoaldehyde dehydrogenase 2, peroxisomal


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

column_label: Table 3; row GBAL / 4-guanidinobutanal; column PsAMADH2 Km (uM); raw 7 uM; normalized 0.007 mM.

raw_value_unit_evidence: Table 3 row GBAL / 4-guanidinobutanal gives PsAMADH2 Km 7 uM.

row_label: GBAL / 4-guanidinobutanal (PsAMADH2; UniProt Q93YB2)


column_label: Table 3; row NAD+ with APAL substrate; column PsAMADH2 Km (uM); raw 55 uM; normalized 0.055 mM.

raw_value_unit_evidence: Table 3 row NAD+ with APAL substrate gives PsAMADH2 Km 55 uM.

row_label: NAD+ with APAL substrate (PsAMADH2; UniProt Q93YB2)

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


enzyme_display_name: Aminoaldehyde dehydrogenase 1, peroxisomal

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

column_label: Table 3; row APAL / 3-aminopropanal; column PsAMADH1 Km (uM); raw 75 uM; normalized 0.075 mM.

raw_value_unit_evidence: Table 3 row APAL / 3-aminopropanal gives PsAMADH1 Km 75 uM.

row_label: APAL / 3-aminopropanal (PsAMADH1; UniProt Q8VWZ1)


enzyme: Aminoaldehyde dehydrogenase 1, peroxisomal


column_label: Table 3; row GBAL / 4-guanidinobutanal; column PsAMADH1 Km (uM); raw 11 uM; normalized 0.011 mM.

raw_value_unit_evidence: Table 3 row GBAL / 4-guanidinobutanal gives PsAMADH1 Km 11 uM.

row_label: GBAL / 4-guanidinobutanal (PsAMADH1; UniProt Q8VWZ1)


column_label: Table 3; row NAD+ with APAL substrate; column PsAMADH1 Km (uM); raw 40 uM; normalized 0.04 mM.

raw_value_unit_evidence: Table 3 row NAD+ with APAL substrate gives PsAMADH1 Km 40 uM.

row_label: NAD+ with APAL substrate (PsAMADH1; UniProt Q8VWZ1)


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal

organism: Arabidopsis thaliana

assay_conditions_summary: pH 9; cofactor NAD+

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

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

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

row_label: AtALDH10A9 / Km column / ABAL row


assay_conditions_summary: pH 9.5; cofactor NAD+

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

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

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

row_label: AtALDH10A9 / Km column / APAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A9 / Km column / NAD+ row = 33+/-4 uM.

normalized_value_unit_evidence: Km=0.033 mM converted from 33+/-4 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for NAD+ reports 33+/-4 uM.

row_label: AtALDH10A9 / Km column / NAD+ row


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


assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Table 1 / Kinetic parameters for AtALDH10A8 and AtALDH10A9 AtALDH10A8 / Km column / NAD+ row with APAL = 13.2+/-1.5 uM.

normalized_value_unit_evidence: Km=0.0132 mM converted from 13.2+/-1.5 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for NAD+ in the APAL-dependent row reports 13.2+/-1.5 uM.


assay_conditions_summary: cofactor NADPH

column_label: Main text on printed page 4519 reports apparent Km values for NADPH and NADH in the reductive reaction were virtually identical, 10 +/- 1 uM.

raw_value_unit_evidence: Km raw_value=10 +/- 1 raw_unit=uM

row_label: Synechocystis sp. strain PCC 6803 GAPDH2

table_label: Main text, printed page 4519, kinetic paragraph for pyridine nucleotides

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NAD(P)+

column_label: Main text across printed pages 4518-4519 reports apparent Km and Vmax measured for both NAD and NADP in the oxidative reaction, with identical values within experimental errors: Km 30 +/- 5 uM.

raw_value_unit_evidence: Km raw_value=30 +/- 5 raw_unit=uM

table_label: Main text, printed pages 4518-4519, kinetic paragraph for pyridine nucleotides

substrate: NAD(P)+


enzyme_display_name: vanillin dehydrogenase

organism: Sphingobium sp. SYK-6

substrate_name: syringaldehyde

enzyme: vanillin dehydrogenase

substrate: syringaldehyde


substrate_name: Vanillin

substrate: Vanillin


organism: Euglena gracilis

substrate_name: NADP+

column_label: Abstract reports Km values for pyruvate, CoA, and NADP+ were estimated to be 27, 6.6, and 28 microM, respectively.

raw_value_unit_evidence: Km raw_value=28 microM raw_unit=microM

row_label: Euglena gracilis pyruvate:NADP+ oxidoreductase / NADP+

table_label: PubMed XML abstract PMID 2508561


substrate_name: methyl viologen

proof_lines:
methyl viologen
pyruvate:NADP+ oxidoreductase
Euglena gracilis

substrate: methyl viologen


enzyme_display_name: coniferyl-aldehyde dehydrogenase

organism: Zea mays

substrate_name: Unknown

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

proof_lines:
at pH 8.8 and 26°C
at pH 8.0 and 40°C

enzyme: coniferyl-aldehyde dehydrogenase

substrate: Unknown


organism: Micrococcus sp.

assay_conditions_summary: pH 7

proof_lines: pH 7, temperature not specified in the publication


enzyme_display_name: erythrose-4-phosphate dehydrogenase

organism: Escherichia coli

substrate_name: D-erythrose 4-phosphate

sequence_variant_note: Mutation signature H176N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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

enzyme: erythrose-4-phosphate dehydrogenase

substrate: D-erythrose 4-phosphate


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C311Y with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C311A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature M179T with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


enzyme_display_name: salicylaldehyde dehydrogenase

organism: Alteromonas naphthalenivorans

substrate_name: Salicylaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E175A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 35°C, recombinant His-tagged mutant E175A

enzyme: salicylaldehyde dehydrogenase

substrate: Salicylaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N149A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 35°C, recombinant His-tagged mutant N149A


proof_lines: pH 7.5, 35°C, recombinant His-tagged enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V153A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 35°C, recombinant His-tagged mutant V153A


assay_conditions_summary: pH 7.5; cofactor NAD+


substrate_name: vanillin in the presence of 0.5 mM NAD(+) (at pH 7.0)

assay_conditions_summary: pH 7; cofactor NADP+


substrate_name: 3,4-dihydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: 4-hydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: NAD(+) in the presence of 1 mM vanillin

assay_conditions_summary: cofactor NADP+

substrate: NAD(+) in the presence of 1 mM vanillin


substrate_name: NADP(+) in the presence of 1 mM vanillin


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

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

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

row_label: AtALDH10A9 / Km column / TMABAL row


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

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

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

row_label: AtALDH10A9 / Km column / GBAL row


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

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

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

row_label: AtALDH10A8 / Km column / TMABAL row


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

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

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

row_label: AtALDH10A8 / Km column / GBAL row


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M179T with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.9; 298.15 K; cofactor NAD+

column_label: Table II row Wild-type GapB-encoded protein / NAD+ (E4PDH activity): kcat cell 20 s^-1; KM cell 0.8 mM; no kcat/KM column/cell is printed, so kcat_over_km 25.0 s^-1 mM^-1 is the quotient 20 / 0.8 of the two printed cells.

normalized_value_unit_evidence: kcat 20 s^-1; Km 0.8 mM; kcat/Km derived as 20 / 0.8 = 25.0 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type GapB-encoded protein / NAD+ (E4PDH activity): kcat=20 s^-1; km=0.8 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type GapB-encoded protein | NAD+ (E4PDH activity)

table_label: Table II. Kinetic parameters of wild-type and mutants of GapB-encoded protein, and wild-type and mutant of B. stearothermophilus GAPDH


organism: Escherichia coli (strain K12)

substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: NAD (at pH 8.5)

substrate: NAD (at pH 8.5)


substrate_name: succinic semialdehyde (at pH 8.5)

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

substrate: succinic semialdehyde (at pH 8.5)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E175A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+

normalized_value_unit_evidence: Km normalized 0.1056 mM; kcat normalized 157.6 s^-1; kcat/Km normalized from exact kcat/Km columns as 1492.4242424242423 s^-1 mM^-1; printed kcat/Km column rounds to 1500 s^-1 mM^-1.

row_label: E175A; NAD+

table_label: Table 2. Apparent kinetic parameters of the wild-type and mutant SALDan enzymes.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N149A to reconstruct the assayed variant sequence.


column_label: Public PMC HTML Table 2, row WT / NAD+, gives App Km 39.5 +/- 3.2 uM, App kcat 234.3 +/- 24.2 s^-1, and App kcat/Km 5.9 +/- 0.5 s^-1 uM^-1. The catalog value is the exact quotient of the same row's exact central kcat and Km cells; the paper's independently printed efficiency column is rounded and concordant.

normalized_value_unit_evidence: Km=0.0395 mM; kcat=234.3 s^-1; exact same-row kcat/Km=234.3/0.0395=5931.645569620254 s^-1*mM^-1; the independently printed rounded efficiency is 5900 s^-1*mM^-1.

row_label: WT; NAD+


column_label: PMC HTML Table 2 row E175A / SALD has columns App Km (uM)=15.1 +/- 2.6, App kcat (s^-1)=82.2 +/- 10.1, App kcat/Km (s^-1 uM^-1)=5.4 +/- 0.9.

normalized_value_unit_evidence: Km normalized 0.0151 mM; kcat normalized 82.2 s^-1; kcat/Km normalized from exact kcat/Km columns as 5443.7086092715235 s^-1 mM^-1; printed kcat/Km column rounds to 5400 s^-1 mM^-1.

row_label: E175A; SALD


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V153A to reconstruct the assayed variant sequence.


column_label: Public PMC HTML Table 2, row WT / SALD, gives App Km 3.8 +/- 0.5 uM, App kcat 123.6 +/- 13.6 s^-1, and App kcat/Km 32.5 +/- 4.2 s^-1 uM^-1. The catalog value is the exact quotient of the same row's exact central kcat and Km cells; the paper's independently printed efficiency column is rounded and concordant.

normalized_value_unit_evidence: Km=0.0038 mM; kcat=123.6 s^-1; exact same-row kcat/Km=123.6/0.0038=32526.315789473683 s^-1*mM^-1; the independently printed rounded efficiency is 32500 s^-1*mM^-1.

row_label: WT; SALD


enzyme_display_name: fluoroacetaldehyde dehydrogenase

organism: Streptantibioticus cattleyicolor

substrate_name: fluoroacetaldehyde

smiles: C(C=O)F

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Fluoroacetaldehyde, Km (uM) footnote b column = 80; normalized Km = 0.08 mM.

normalized_value_unit_evidence: Km=0.08 mM (converted from 80 uM).

raw_value_unit_evidence: Table 2 row Fluoroacetaldehyde, Km (uM) footnote b column = 80.

row_label: Fluoroacetaldehyde

table_label: Table 2: Substrate specificity of fluoroacetaldehyde dehydrogenase from S. cattleya

enzyme: fluoroacetaldehyde dehydrogenase

substrate: fluoroacetaldehyde


substrate_name: glycoaldehyde

smiles: C(C=O)O

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Glycoaldehyde, Km (uM) footnote b column = 150; normalized Km = 0.15 mM.

normalized_value_unit_evidence: Km=0.15 mM (converted from 150 uM).

raw_value_unit_evidence: Table 2 row Glycoaldehyde, Km (uM) footnote b column = 150.

row_label: Glycoaldehyde

substrate: glycoaldehyde


substrate_name: benzaldehyde

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Benzaldehyde, Km (uM) footnote b column = 320; normalized Km = 0.32 mM.

normalized_value_unit_evidence: Km=0.32 mM (converted from 320 uM).

raw_value_unit_evidence: Table 2 row Benzaldehyde, Km (uM) footnote b column = 320.

row_label: Benzaldehyde

substrate: benzaldehyde


substrate_name: acetaldehyde

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Acetaldehyde, Km (uM) footnote b column = 810; normalized Km = 0.81 mM.

normalized_value_unit_evidence: Km=0.81 mM (converted from 810 uM).

raw_value_unit_evidence: Table 2 row Acetaldehyde, Km (uM) footnote b column = 810.

row_label: Acetaldehyde

substrate: acetaldehyde


organism: Bacillus subtilis

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NADP+

substrate: NADP+


substrate_name: D-Erythrose

assay_conditions_summary: pH 8.9; 298.15 K; cofactor NADH

column_label: Results main text, JBC page 15110, sentence on the catalytic efficiency of the GapB-encoded protein tested with erythrose; Wild-type GapB-encoded protein / erythrose: kcat 0.36 s^-1; KM 90 mM; no kcat/KM value is printed, so kcat_over_km 0.004 s^-1 mM^-1 is the quotient 0.36 / 90 of the two printed prose values.

normalized_value_unit_evidence: kcat 0.36 s^-1; Km 90 mM; kcat/Km derived as 0.36 / 90 = 0.004 s^-1 mM^-1 from the two printed prose values; the paper prints no kcat/KM value.

raw_value_unit_evidence: Results main text, JBC page 15110, sentence on the catalytic efficiency of the GapB-encoded protein tested with erythrose; Wild-type GapB-encoded protein / erythrose: kcat=0.36 s^-1; km=90 mM; kcat_over_km=0.004 s^-1 mM^-1 derived as the quotient 0.36 / 90 s^-1 / mM; no kcat/KM value is printed in the paper.

substrate: D-Erythrose


substrate_name: D-Erythrose 4-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C311A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

substrate: D-Erythrose 4-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C311Y with inferred residue-numbering offset +5 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.

column_label: Table II row Wild-type GapB-encoded protein / D-Erythrose 4-phosphate (E4PDH activity): kcat cell 20 s^-1; KM cell 0.51 mM; no kcat/KM column/cell is printed, so kcat_over_km 39.21568627450981 s^-1 mM^-1 is the quotient 20 / 0.51 of the two printed cells.

normalized_value_unit_evidence: kcat 20 s^-1; Km 0.51 mM; kcat/Km derived as 20 / 0.51 = 39.21568627450981 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type GapB-encoded protein / D-Erythrose 4-phosphate (E4PDH activity): kcat=20 s^-1; km=0.51 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type GapB-encoded protein | D-Erythrose 4-phosphate (E4PDH activity)


substrate_name: NAD+


substrate_name: NAD(+)

column_label: Abstract states apparent Km values for NAD and CHMS were 19.5 +/- 2.7 microM and 9.2 +/- 1.4 microM, respectively, for the E. coli enzyme.

raw_value_unit_evidence: Km raw_value=19.5 microM raw_unit=microM

row_label: E. coli CHMS dehydrogenase / NAD

table_label: PubMed XML abstract

substrate: NAD(+)


raw_value_unit_evidence: Km raw_value=9.2 microM raw_unit=microM

row_label: E. coli CHMS dehydrogenase / CHMS


organism: Pyrococcus woesei

substrate_name: phosphate

column_label: Scanned Table 2 row Phosphate reports Km (mM) of enzyme from P. woesei = 40.

raw_value_unit_evidence: Km raw_value=40 raw_unit=mM

row_label: Phosphate

table_label: PMC213258 scanned Table 2, Kinetic properties of P. woesei glyceraldehyde-3-phosphate dehydrogenase from original organism and transformed E. coli cells

substrate: phosphate


substrate_name: NADP(+)

column_label: Scanned Table 2 row NADP+ reports Km (mM) of enzyme from P. woesei = 0.01.

raw_value_unit_evidence: Km raw_value=0.01 raw_unit=mM

row_label: NADP+

substrate: NADP(+)


substrate_name: D-erythrose 4-phosphate

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

assay_conditions_summary: pH 8.6; cofactor NAD+

column_label: PDF text lines 29-31 and 402-409; page 1 abstract and page 6 Results prose name Kmapp(E4P) and kcatapp for E4P.

raw_value_unit_evidence: Abstract reports Kmapp(E4P) = 0.96 mM and kcatapp(E4P) = 200 s^-1; Results reports Kmapp(E4P) = 0.96 +/- 0.13 mM and kcatapp = 200 s^-1.

row_label: D-erythrose 4-phosphate; purified gapB/epd E4PDH

table_label: Abstract and Results prose: kinetic parameters of purified E4PDH

substrate: D-erythrose 4-phosphate


substrate_name: D-erythrose 4-phosphate (at 25 degrees Celsius and pH 8.9)


enzyme_display_name: Glutamyl-tRNA reductase

substrate_name: NADPH

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

enzyme: Glutamyl-tRNA reductase

substrate: NADPH


enzyme_display_name: Pyruvate dehydrogenase [NADP(+)], mitochondrial

column_label: Results text, NADP+ as third listed substrate/cofactor: 30 uM.

raw_value_unit_evidence: Apparent Km values for pyruvate, CoA, and NADP+ were 210, 8, and 30 uM, respectively.

row_label: Pyruvate:NADP+ oxidoreductase substrate/cofactor profile

table_label: Results text: kinetic profiles

data_origin: curated


enzyme_display_name: glutamyl-tRNA reductase

assay_conditions_summary: pH 8.1; 310.15 K; cofactor NADPH

enzyme: glutamyl-tRNA reductase


organism: Geobacillus stearothermophilus

column_label: Table II row Wild-type B. stearothermophilus GAPDH / D-Erythrose 4-phosphate (E4PDH activity): kcat cell 0.1 s^-1; KM cell 3.3 mM; no kcat/KM column/cell is printed, so kcat_over_km 0.030303030303030307 s^-1 mM^-1 is the quotient 0.1 / 3.3 of the two printed cells.

normalized_value_unit_evidence: kcat 0.1 s^-1; Km 3.3 mM; kcat/Km derived as 0.1 / 3.3 = 0.030303030303030307 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type B. stearothermophilus GAPDH / D-Erythrose 4-phosphate (E4PDH activity): kcat=0.1 s^-1; km=3.3 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type B. stearothermophilus GAPDH | D-Erythrose 4-phosphate (E4PDH activity)


column_label: Table II row Wild-type B. stearothermophilus GAPDH / NAD+ (E4PDH activity): kcat cell 0.1 s^-1; KM cell 0.08 mM; no kcat/KM column/cell is printed, so kcat_over_km 1.25 s^-1 mM^-1 is the quotient 0.1 / 0.08 of the two printed cells.

normalized_value_unit_evidence: kcat 0.1 s^-1; Km 0.08 mM; kcat/Km derived as 0.1 / 0.08 = 1.25 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type B. stearothermophilus GAPDH / NAD+ (E4PDH activity): kcat=0.1 s^-1; km=0.08 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type B. stearothermophilus GAPDH | NAD+ (E4PDH activity)

substrate: NAD+


enzyme_display_name: D-erythrose-4-phosphate dehydrogenase

substrate_name: glyceraldehyde 3-phosphate (at 25 degrees Celsius and pH 8.9)

enzyme: D-erythrose-4-phosphate dehydrogenase


organism: Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NBRC 12016 / NCIMB 10680 / K1)

substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


enzyme_display_name: UniProt Q13WK4

organism: Paraburkholderia xenovorans

enzyme: UniProt Q13WK4


substrate_name: propionaldehyde

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

substrate: propionaldehyde


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


substrate_name: heptaldehyde

smiles: CCCCCCC=O

substrate: heptaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: benzaldehyde