substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


enzyme_display_name: UniProt Q13WK4

organism: Paraburkholderia xenovorans

substrate_name: NAD+

source_db: skid

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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.

data_origin: experimental

enzyme: UniProt Q13WK4

substrate: NAD+

source: skid


enzyme_display_name: UniProt A9SS48

organism: Physcomitrium patens

km_unit: mM

enzyme: UniProt A9SS48


substrate_name: NADP+

substrate: NADP+


substrate_name: succinate semialdehyde

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

substrate: succinate semialdehyde


substrate_name: Glutaric semialdehyde

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

substrate: Glutaric semialdehyde


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

substrate_name: betaine aldehyde

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

source_license: CC BY 4.0

enzyme: Aminoaldehyde dehydrogenase 1a

substrate: betaine aldehyde

status: unverified

source: uniprot


enzyme_display_name: retinal dehydrogenase

organism: Rattus norvegicus

substrate_name: all-trans-retinal

source_db: brenda

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

proof_lines: cellular retinol-binding protein-bound retinal has lower Km of 0.0002 mM

proof_lines: retinal bovine serum albumin, Km is 25 times lower than the Km for acetaldehyde

enzyme: retinal dehydrogenase

substrate: all-trans-retinal

source: brenda


substrate_name: citral

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

substrate: citral


smiles: CCCCCC=CC=CC=O


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: decanal

smiles: CCCCCCCCC=O

substrate: decanal


organism: Homo sapiens

substrate_name: 3-phospho-D-glyceroyl phosphate

assay_conditions_summary: pH 7

proof_lines:
enzyme form E6.8, pH 7
enzyme form E9.0, pH 9
enzyme form E8.5, pH 9

substrate: 3-phospho-D-glyceroyl phosphate


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

proof_lines:
enzyme form E8.5, pH 9
pH 8.5, 25°C
enzyme form E9.0, pH 9


substrate_name: 1,3-diphosphoglyceric acid

assay_conditions_summary: pH 7; cofactor NAD+

proof_lines:
enzyme form E6.6, pH 7
enzyme form E8.5, pH 7
enzyme form E9.0, pH 7

substrate: 1,3-diphosphoglyceric acid


substrate_name: DL-glyceraldehyde

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

substrate: DL-glyceraldehyde


substrate_name: erythrose 4-phosphate

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

proof_lines:
enzyme form E8.5, pH 7
enzyme form E9.0, pH 7

substrate: erythrose 4-phosphate


enzyme_display_name: sulfoacetaldehyde dehydrogenase

organism: Rhodopseudomonas palustris

enzyme: sulfoacetaldehyde dehydrogenase


assay_conditions_summary: pH 9; 295.15 K; cofactor NAD+


assay_conditions_summary: pH 9; 295.15 K; cofactor NADP+


enzyme_display_name: 2-formylbenzoate dehydrogenase

organism: Alcaligenes faecalis

enzyme: 2-formylbenzoate dehydrogenase


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Euglena gracilis

assay_conditions_summary: pH 8.7; 308.15 K; cofactor NADP+


enzyme_display_name: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)

substrate_name: propionaldehyde

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:Q13WK4 and applied mutation signature H485A to reconstruct the assayed variant sequence.

smiles: CCC=O

mutation_type: substitution

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Figure 1B; H485A_ALDHC row; kcat (min^-1) column; raw value 5.75 +/- 0.31 min^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 5.75 +/- 0.31 min^-1.

row_label: H485A_ALDHC row

table_label: PMID 21495107, Figure 1B: kcat values for native and mutant ALDHC

substrate: propionaldehyde

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K168A to reconstruct the assayed variant sequence.

proof_lines: K168A mutant enzyme, pH 7.5, temperature not specified in the publication

enzyme: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E400A to reconstruct the assayed variant sequence.

proof_lines: E400A mutant enzyme, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:Q13WK4 and applied mutation signature E496A to reconstruct the assayed variant sequence.

column_label: Figure 1B; E496A_ALDHC row; kcat (min^-1) column; raw value 16.2 +/- 0.77 min^-1.

normalized_value_unit_evidence: 16.2 +/- 0.77 min^-1 normalized to 0.27 s^-1; exported row is 16.2 s^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 16.2 +/- 0.77 min^-1.

row_label: E496A_ALDHC row


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:Q13WK4 and applied mutation signature E167A to reconstruct the assayed variant sequence.

column_label: Figure 1B; E167A_ALDHC row; kcat (min^-1) column; raw value 36.8 +/- 1.6 min^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 36.8 +/- 1.6 min^-1.

row_label: E167A_ALDHC row


column_label: Figure 1B; Native_ALDHC row; kcat (min^-1) column; raw value 162 +/- 6.2 min^-1.

normalized_value_unit_evidence: 162 +/- 6.2 min^-1 normalized to 2.7 s^-1; exported row is 162.0 s^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 162 +/- 6.2 min^-1.

row_label: Native_ALDHC row


organism: Mycobacterium tuberculosis

substrate_name: Succinate semialdehyde; H2O; NADP+

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

assay_conditions_summary: cofactor NADP+

substrate: Succinate semialdehyde; H2O; NADP+


substrate_name: NAD+; H2O; Succinate semialdehyde

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O; Succinate semialdehyde


enzyme_display_name: UniProt B1XMM6

organism: Synechococcus sp.

verification_status: verified

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

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADP+

enzyme: UniProt B1XMM6

status: verified


kcat_over_km_origin: calculated

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

assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADP+

proof_lines: recombinant mutant R121A, pH 8.2, 25°C, with NADP+


proof_lines: recombinant mutant R457A, pH 8.2, 25°C, with NADP+


proof_lines: recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+


sequence_variant_note: Resolved canonical sequence from pdb_accession and applied mutation signature R228A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; 298.15 K; cofactor NAD+

proof_lines: recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde


proof_lines: recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde


proof_lines: recombinant mutant R228A, pH 8.2, 25°C, with NADP+


proof_lines: recombinant mutant Y296A, pH 8.2, 25°C, with NADP+


sequence_variant_note: Resolved canonical sequence from pdb_accession and applied mutation signature N175A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant N175A, pH 8.2, 25°C, with NADP+


organism: Nostoc sp. PCC 7120 = FACHB-418

assay_conditions_summary: pH 9.5; cofactor NADP+

proof_lines: pH 9.5, 25°C, recombinant wild-type enzyme


assay_conditions_summary: pH 9.5; cofactor NAD+


substrate_name: benzaldehyde

substrate: benzaldehyde


proof_lines: in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


substrate_name: NAD+

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: NAD+


substrate_name: Valeraldehyde

substrate: Valeraldehyde


substrate_name: heptaldehyde

smiles: CCCCCCC=O

substrate: heptaldehyde


enzyme_display_name: malonyl-CoA reductase (malonate semialdehyde-forming)

organism: Chloroflexus aurantiacus

substrate_name: NADPH

assay_conditions_summary: pH 7.8; cofactor NADPH

proof_lines: isolated C-terminal fragment, pH 7.8, 57°C

substrate: NADPH


organism: Saccharolobus solfataricus

substrate_name: NADP+

assay_conditions_summary: pH 6.5; cofactor NADP+

column_label: Table 2: SSADH-II with NADP+ as cosubstrate, row NADP+: Km=0.01 mM; kcat=16.5 s^-1; kcat/Km=3066.4 mM^-1 s^-1

row_label: NADP+

substrate: NADP+


substrate_name: succinate semialdehyde

column_label: Table 2: SSADH-II with NADP+ as cosubstrate, row Succinic semialdehyde (C4): Km=0.004 mM; kcat=18.4 s^-1; kcat/Km=3454.2 mM^-1 s^-1

row_label: Succinic semialdehyde (C4)

substrate: succinate semialdehyde


column_label: Table 3: SSADH-II with NAD+ as cosubstrate, row a-Ketoglutaric semialdehyde (C5): Km=0.1 mM; kcat=27.3 s^-1; kcat/Km=215.3 mM^-1 s^-1

row_label: a-Ketoglutaric semialdehyde (C5)


assay_conditions_summary: pH 6.5; cofactor NAD+

column_label: Table 3: SSADH-II with NAD+ as cosubstrate, row NAD+: Km=11.1 mM; kcat=136.3 s^-1; kcat/Km=12.3 mM^-1 s^-1

row_label: NAD+


substrate_name: malonyl-CoA

protein_accession_database: NCBI Protein

assay_conditions_summary: pH 7.8; cofactor CoA

enzyme: malonyl-CoA reductase (malonate semialdehyde-forming)

substrate: malonyl-CoA


organism: Cryptosporidium parvum

substrate_name: hexacosanoyl-CoA

assay_conditions_summary: pH 7.2; cofactor CoA

proof_lines: pH 7.2, temperature not specified in the publication

substrate: hexacosanoyl-CoA


organism: Arabidopsis thaliana

substrate_name: hexadecanoyl-[acyl-carrier protein]

substrate: hexadecanoyl-[acyl-carrier protein]


organism: Nocardioides sp.

sequence_source: multiple

assay_conditions_summary: pH 9.4; cofactor NAD+

proof_lines: kcat is 39 sec(-1) with 2-carboxybenzaldehyde as substrate. kcat is 32 sec(-1) with NAD as substrate.

source_databases_merged: brenda uniprot


organism: Synechocystis sp. PCC 6803

proof_lines: pH 9.7, 45°C, recombinant detagged enzyme


assay_conditions_summary: pH 9.7; 318.15 K; cofactor NADP+


enzyme_display_name: Succinate-semialdehyde dehydrogenase [NADP(+)] GabD

organism: Escherichia coli (strain K12)

proof_lines: The succinate-semialdehyde dehydrogenase activity measured in the presence of NADP(+) is approximately 20-fold higher than that measured in the presence of NAD(+).


organism: Physcomitrium patens

substrate_name: Glutaric semialdehyde

source_db: oed

smiles: O=CCCCCC(=O)O

assay_conditions_summary: pH 8.2; 298.15 K; buffer pH 8; cofactor NADP+

column_label: Table 1; row WT-PpALDH21 under GRSAL (NADP+); Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: Km paper=0.551 mM; kcat paper=0.27 s^-1; kcat/Km paper=0.5 s^-1 mM^-1.

row_label: WT-PpALDH21; GRSAL (NADP+)

table_label: Table 1. Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates

substrate: Glutaric semialdehyde

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R228A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


column_label: Table 1, NAD+ (SSAL) group, WT-PpALDH21 row reports K_m 5370 +/- 140, kcat 3.3 +/- 0.1, and kcat/K_m 6.2 +/- 0.2 x 10^2.

row_label: NAD+ (SSAL) / WT-PpALDH21

table_label: Table 1


column_label: Table 1; row WT-PpALDH21 under NADP+ (SSAL); Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: Km paper=0.024 mM; kcat paper=15.2 s^-1; kcat/Km paper=630.0 s^-1 mM^-1.

row_label: WT-PpALDH21; NADP+ (SSAL)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N175A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

smiles: O=CCCC(=O)O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9SS48 and applied mutation signature R121A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates), SSAL (NADP+) block, enzyme row R121A; column Km (uM) = 268 ± 10; column kcat (sec^-1) = 0.02 ± 0.01; column kcat/Km (sec^-1 M^-1) = 8.8 ± 0.7 x 10^1.

normalized_value_unit_evidence: Km: printed Table 1 cell 268 uM; 268 / 1000 = 0.268 mM. kcat: printed Table 1 cell 0.02 s^-1; already in s^-1, no unit conversion applies. kcat/Km: printed Table 1 cell 8.8 x 10^1 s^-1 M^-1 = 88.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 88.0 / 1000 = 0.088 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, SSAL (NADP+) block, enzyme row R121A: Km = 268 ± 10 uM; kcat = 0.02 ± 0.01 s^-1; printed kcat/Km = 8.8 ± 0.7 x 10^1 s^-1 M^-1 (the printed column heads read Km (µM), kcat (sec^-1) and kcat/Km (sec^-1 M^-1)).

table_label: Table 1: Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates (The Plant Journal 2017, 92:229-243)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9SS48 and applied mutation signature R457A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates), SSAL (NADP+) block, enzyme row R457A; column Km (uM) = 135 ± 7; column kcat (sec^-1) = 0.02 ± 0.01; column kcat/Km (sec^-1 M^-1) = 1.8 ± 0.2 x 10^2.

normalized_value_unit_evidence: Km: printed Table 1 cell 135 uM; 135 / 1000 = 0.135 mM. kcat: printed Table 1 cell 0.02 s^-1; already in s^-1, no unit conversion applies. kcat/Km: printed Table 1 cell 1.8 x 10^2 s^-1 M^-1 = 180.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 180.0 / 1000 = 0.18 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, SSAL (NADP+) block, enzyme row R457A: Km = 135 ± 7 uM; kcat = 0.02 ± 0.01 s^-1; printed kcat/Km = 1.8 ± 0.2 x 10^2 s^-1 M^-1 (the printed column heads read Km (µM), kcat (sec^-1) and kcat/Km (sec^-1 M^-1)).


column_label: Table 1; row WT-PpALDH21 under SSAL (NADP+); Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: Km paper=0.181 mM; kcat paper=15.8 s^-1; kcat/Km paper=87.0 s^-1 mM^-1.

row_label: WT-PpALDH21; SSAL (NADP+)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y296A to reconstruct the assayed variant sequence.


organism: Clostridium kluyveri

substrate_name: coenzyme A

assay_conditions_summary: pH 8.5; cofactor CoA

substrate: coenzyme A


substrate_name: succinyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

column_label: Table 3 Km mM column; direction Forward; substrate succinyl-CoA; value 3.2 (+/- 0.6) x 10^-3

raw_value_unit_evidence: Table 3 forward row succinyl-CoA Km = 3.2 (+/- 0.6) x 10^-3 mM

row_label: Forward row succinyl-CoA

table_label: Wiley PDF page 126 Table 3. Kinetic values for succinate-semialdehyde dehydrogenase

substrate: succinyl-CoA


assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: Table 3 Km mM column; direction Reverse; substrate NADP+; value 4.0 (+/- 1.7) x 10^-3

raw_value_unit_evidence: Table 3 reverse row NADP+ Km = 4.0 (+/- 1.7) x 10^-3 mM

row_label: Reverse row NADP+


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 3 Km mM column; direction Forward; substrate NADPH; value 4.3 (+/- 1.3) x 10^-3

raw_value_unit_evidence: Table 3 forward row NADPH Km = 4.3 (+/- 1.3) x 10^-3 mM

row_label: Forward row NADPH


enzyme_display_name: Malonyl-CoA reductase

organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

substrate_name: NADP (with 0.2 mM malonyl-CoA)

assay_conditions_summary: cofactor NADPH

column_label: Full-text properties paragraph maps NADPH to 25 uM Km for recombinant S. tokodaii enzyme

raw_value_unit_evidence: Km raw_value=25 raw_unit=uM

row_label: Sulfolobus tokodaii recombinant malonyl-CoA reductase NADPH item

table_label: PMID 17041055 PMC full text

enzyme: Malonyl-CoA reductase

substrate: NADP (with 0.2 mM malonyl-CoA)


substrate_name: malonyl-CoA (with 0.5 mM NADP)

assay_conditions_summary: cofactor CoA

column_label: Full-text properties paragraph maps malonyl-CoA to 40 uM Km for recombinant S. tokodaii enzyme

raw_value_unit_evidence: Km raw_value=40 raw_unit=uM

row_label: Sulfolobus tokodaii recombinant malonyl-CoA reductase malonyl-CoA item

substrate: malonyl-CoA (with 0.5 mM NADP)


organism: Listeria monocytogenes

substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Streptomyces coelicolor


enzyme_display_name: UniProt A0A2H4PMI3

organism: Zea mays

enzyme: UniProt A0A2H4PMI3


substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


substrate_name: NAD+

substrate: NAD+


substrate_name: 2-aminoadipic semialdehyde

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

substrate: 2-aminoadipic semialdehyde


substrate_name: L-glutamate 5-semialdehyde

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

substrate: L-glutamate 5-semialdehyde


enzyme_display_name: UniProt P09546

organism: Escherichia coli

enzyme: UniProt P09546


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

column_label: Table 1, row NADP+ with fixed substrate concentration 50 uM and [Mg2+] 10 mM, columns kcat (s^-1), Km (uM), and kcat/K (M^-1 s^-1), cells 2.7 +/- 0.1, 9.2 +/- 1.0, and (2.9 +/- 0.1) x 10^5.

normalized_value_unit_evidence: kcat 2.7 s^-1; Km 9.2 uM = 0.0092 mM; kcat/K 2.9 x 10^5 M^-1 s^-1 = 290 s^-1 mM^-1. Current export mixes this kcat with Km 0.0613 mM and kcat/K 44.045676998368684 s^-1 mM^-1 from a different condition.

row_label: NADP+, fixed substrate concentration 50 uM, [Mg2+] 10 mM

table_label: Table 1: Steady-State Kinetic Parameters for GabD1


substrate_name: Succinic semialdehyde

column_label: Table 1, row SSA with fixed substrate concentration 200 uM and [Mg2+] 10 mM, columns kcat (s^-1), Km (uM), and kcat/K (M^-1 s^-1), cells 4.7 +/- 0.1, 3.0 +/- 0.2, and (1.6 +/- 0.1) x 10^6.

normalized_value_unit_evidence: kcat 4.7 s^-1; Km 3.0 uM = 0.003 mM; kcat/K 1.6 x 10^6 M^-1 s^-1 = 1600 s^-1 mM^-1. Current export mixes this kcat with Km 0.0133 mM and kcat/K 353.3834586466166 s^-1 mM^-1 from a different condition.

row_label: SSA, fixed substrate concentration 200 uM, [Mg2+] 10 mM

substrate: Succinic semialdehyde


organism: Streptococcus pyogenes

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

column_label: Table 2. Steady-state kinetic parameters of SpSSADH; row Variable ligand NAD+; fixed substrate SSA (0.5 mM)

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.


substrate_name: NADP+

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

column_label: Table 2 columns Km, kcat, and kcat/Km for variable ligand NADP+ with fixed substrate SSA (0.5 mM).

normalized_value_unit_evidence: kcat/Km normalized_value=72.0 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=0.10 +/- 0.01 raw_unit=mM; kcat raw_value=7.20 +/- 0.12 raw_unit=s^-1; kcat/Km raw_value=7.2 +/- 0.3 x 10^4 raw_unit=M^-1 s^-1

row_label: Variable ligand NADP+; fixed substrate SSA (0.5 mM)

table_label: Table 2. Steady-state kinetic parameters of SpSSADH

substrate: NADP+


organism: Acinetobacter baumannii

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


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

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+

column_label: Tables 2 and 3: SSADH-II NADP+/NAD+ rows, row a-Ketoglutaric semialdehyde (C5): Km=0.1 or 0.2 mM; kcat=27.3 or 21.2 s^-1; kcat/Km=215.3 or 134.1 mM^-1 s^-1


assay_conditions_summary: pH 6.5; 343.15 K; cofactor NAD+

column_label: Table 3: SSADH-II with NAD+ as cosubstrate, row NAD+: Km=11.1 mM; kcat=136.3 s^-1; kcat/Km=12.3 mM^-1 s^-1


column_label: Table 2: SSADH-II with NADP+ as cosubstrate, row Succinic semialdehyde (C4): Km=0.004 mM; kcat=18.4 s^-1; kcat/Km=3454.2 mM^-1 s^-1


organism: Neptuniibacter caesariensis

assay_conditions_summary: pH 9; cofactor NAD+


substrate_name: Sulfoacetaldehyde

assay_conditions_summary: pH 9

substrate: Sulfoacetaldehyde


assay_conditions_summary: pH 9; cofactor NADP+


organism: Aromatoleum evansii

substrate_name: 3,4-dehydroadipyl-CoA semialdehyde

assay_conditions_summary: pH 7.2; cofactor CoA

substrate: 3,4-dehydroadipyl-CoA semialdehyde


assay_conditions_summary: pH 7.2; cofactor NADP+


enzyme_display_name: geranial dehydrogenase

organism: Persicaria minor

assay_conditions_summary: pH 9.5; 308.15 K; cofactor NAD+

proof_lines: isoform citral dehydrogenase II, at pH 9.5 and 35°C

proof_lines: isoform citral dehydrogenase I, at pH 9.5 and 35°C

enzyme: geranial dehydrogenase


substrate_name: citral

substrate: citral


substrate_name: trans-cinnamaldehyde

substrate: trans-cinnamaldehyde


substrate_name: alpha-methyl cinnamaldehyde

substrate: alpha-methyl cinnamaldehyde


substrate_name: S-perillyl aldehyde

substrate: S-perillyl aldehyde


enzyme_display_name: malonyl CoA reductase (malonate semialdehyde-forming)

organism: Chloroflexus aurantiacus

substrate_name: NADPH

substrate: NADPH


organism: Hyalomma dromedarii

substrate_name: D-glucose

substrate: D-glucose


assay_conditions_summary: cofactor NADP+

proof_lines:
isoform B, with NADP+
isoform B, with NAD+
isoform A, with NADP+


proof_lines:
isoform A
isoform B


substrate_name: p-nitrobenzaldehyde

substrate: p-nitrobenzaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


assay_conditions_summary: cofactor NAD+


substrate_name: formaldehyde

substrate: formaldehyde


substrate_name: glyoxylic acid

substrate: glyoxylic acid


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Solanum tuberosum


substrate_name: NAD+

substrate: NAD+


substrate_name: 2-aminoadipic semialdehyde

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme

substrate: 2-aminoadipic semialdehyde


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


substrate_name: Glutaric semialdehyde

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

substrate: Glutaric semialdehyde


substrate_name: L-glutamate 5-semialdehyde

substrate: L-glutamate 5-semialdehyde


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.15; 303.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Oryza sativa

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADP+


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+


proof_lines:
cosubstrate NADP+, pH 7.5, 35°C
cosubstrate NAD+, pH 7.5, 35°C


organism: Klebsiella pneumoniae


organism: Nicotiana plumbaginifolia

proof_lines:
isoform I
isoform II


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature F505A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM sodium pyrophosphate; cofactor NAD+

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row F505A: Km (uM) = 170; kcat (s^-1) = 0.03; kcat/Km (s^-1 M^-1) = 1.9 x 10^2.

normalized_value_unit_evidence: Km: printed cell 170 uM; 1 uM is 1/1000 mM, so 170 / 1000 = 0.17 mM. kcat: printed cell 0.03 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.03 s^(-1). kcat/Km: printed cell 1.9 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 190 / 1000 = 0.19 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.03 / 0.17 = 0.1764705882352941 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.19 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row F505A: Km = 170 uM; kcat = 0.03 s^-1; printed kcat/Km = 1.9 x 10^2 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row F505A

table_label: Table 2. Kinetic parameters for ZmALDH12 active-site mutant variants. (J Mol Biol 2019, 431(3):576-592); printed column heads Enzyme | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 M^-1), GSAL block


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

assay_conditions_summary: pH 7.5; buffer 3.0 mM NAD+ in 100 mM pyrophosphate; cofactor NAD+

column_label: The literal ZmALDH12 AASAL row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.173 mM; kcat=0.04 s^-1; current same-row quotient=0.23121387283236997 s^-1 mM^-1; printed efficiency=0.2 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: AASAL cells: Km 173 ± 12 μM; kcat 0.04 ± 0.02 s^-1; printed kcat/Km 2.0 ± 0.2 × 10^2 s^-1 M^-1.

row_label: ZmALDH12 / AASAL

table_label: Table 1. Kinetic parameters for ZmALDH12 and PpALDH12


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature F202A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row F202A: Km (uM) = 969; kcat (s^-1) = 0.15; kcat/Km (s^-1 M^-1) = 1.5 x 10^2.

normalized_value_unit_evidence: Km: printed cell 969 uM; 1 uM is 1/1000 mM, so 969 / 1000 = 0.969 mM. kcat: printed cell 0.15 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.15 s^(-1). kcat/Km: printed cell 1.5 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150 / 1000 = 0.15 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.15 / 0.969 = 0.15479876160990713 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.15 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row F202A: Km = 969 uM; kcat = 0.15 s^-1; printed kcat/Km = 1.5 x 10^2 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row F202A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E205A to reconstruct the assayed variant sequence.


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row F202A: Km (uM) = 480; kcat (s^-1) = 0.21; kcat/Km (s^-1 M^-1) = 4.4 x 10^2.

normalized_value_unit_evidence: Km: printed cell 480 uM; 1 uM is 1/1000 mM, so 480 / 1000 = 0.48 mM. kcat: printed cell 0.21 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.21 s^(-1). kcat/Km: printed cell 4.4 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 440 / 1000 = 0.44 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.21 / 0.48 = 0.4375 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.44 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row F202A: Km = 480 uM; kcat = 0.21 s^-1; printed kcat/Km = 4.4 x 10^2 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row F202A

table_label: Table 2. Kinetic parameters for ZmALDH12 active-site mutant variants. (J Mol Biol 2019, 431(3):576-592); printed column heads Enzyme | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 M^-1), GRSAL block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature K329A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row K329A: Km (uM) = 958; kcat (s^-1) = 0.26; kcat/Km (s^-1 M^-1) = 2.7 x 10^2.

normalized_value_unit_evidence: Km: printed cell 958 uM; 1 uM is 1/1000 mM, so 958 / 1000 = 0.958 mM. kcat: printed cell 0.26 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.26 s^(-1). kcat/Km: printed cell 2.7 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 270 / 1000 = 0.27 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.26 / 0.958 = 0.27139874739039666 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.27 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row K329A: Km = 958 uM; kcat = 0.26 s^-1; printed kcat/Km = 2.7 x 10^2 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row K329A


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row K329A: Km (uM) = 442; kcat (s^-1) = 0.31; kcat/Km (s^-1 M^-1) = 7.0 x 10^2.

normalized_value_unit_evidence: Km: printed cell 442 uM; 1 uM is 1/1000 mM, so 442 / 1000 = 0.442 mM. kcat: printed cell 0.31 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.31 s^(-1). kcat/Km: printed cell 7.0 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 700 / 1000 = 0.7 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.31 / 0.442 = 0.7013574660633484 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row K329A: Km = 442 uM; kcat = 0.31 s^-1; printed kcat/Km = 7.0 x 10^2 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row K329A


substrate_name: D-glyceraldehyde 3-phosphate

column_label: The literal ZmALDH12 D-GAP row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=1.86 mM; kcat=0.4 s^-1; current same-row quotient=0.21505376344086022 s^-1 mM^-1; printed efficiency=0.21 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: D-GAP cells: Km 1860 ± 99 μM; kcat 0.4 ± 0.1 s^-1; printed kcat/Km 2.1 ± 0.2 × 10^2 s^-1 M^-1.

row_label: ZmALDH12 / D-GAP

substrate: D-glyceraldehyde 3-phosphate


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row F505A: Km (uM) = 379; kcat (s^-1) = 0.52; kcat/Km (s^-1 M^-1) = 1.4 x 10^3.

normalized_value_unit_evidence: Km: printed cell 379 uM; 1 uM is 1/1000 mM, so 379 / 1000 = 0.379 mM. kcat: printed cell 0.52 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.52 s^(-1). kcat/Km: printed cell 1.4 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1400 / 1000 = 1.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.52 / 0.379 = 1.3720316622691293 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row F505A: Km = 379 uM; kcat = 0.52 s^-1; printed kcat/Km = 1.4 x 10^3 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row F505A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature E205A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row E205A: Km (uM) = 32; kcat (s^-1) = 0.53; kcat/Km (s^-1 M^-1) = 1.6 x 10^4.

normalized_value_unit_evidence: Km: printed cell 32 uM; 1 uM is 1/1000 mM, so 32 / 1000 = 0.032 mM. kcat: printed cell 0.53 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.53 s^(-1). kcat/Km: printed cell 1.6 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 16000 / 1000 = 16.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.53 / 0.032 = 16.5625 s^-1 mM^-1, against the printed catalytic-efficiency cell 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row E205A: Km = 32 uM; kcat = 0.53 s^-1; printed kcat/Km = 1.6 x 10^4 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row E205A


assay_conditions_summary: pH 7.5; buffer 0.3 mM sub-saturating GSAL in 100 mM pyrophosphate; cofactor NADP+

column_label: The literal ZmALDH12 NADP+ row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=2.872 mM; kcat=0.8 s^-1; current same-row quotient=0.2785515320334262 s^-1 mM^-1; printed efficiency=0.27 s^-1 mM^-1; printed cell is preserved separately.

row_label: ZmALDH12 / NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature S331A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row S331A: Km (uM) = 227; kcat (s^-1) = 0.89; kcat/Km (s^-1 M^-1) = 3.9 x 10^3.

normalized_value_unit_evidence: Km: printed cell 227 uM; 1 uM is 1/1000 mM, so 227 / 1000 = 0.227 mM. kcat: printed cell 0.89 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.89 s^(-1). kcat/Km: printed cell 3.9 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3900 / 1000 = 3.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.89 / 0.227 = 3.920704845814978 s^-1 mM^-1, against the printed catalytic-efficiency cell 3.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row S331A: Km = 227 uM; kcat = 0.89 s^-1; printed kcat/Km = 3.9 x 10^3 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row S331A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature D226A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM sodium pyrophosphate; cofactor NADP+

column_label: Table 1 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 1, ZmALDH12 D226A block, substrate row NADP+: Km (uM) = 71; kcat (s^-1) = 1.5; kcat/Km (s^-1 M^-1) = 2.1 x 10^4.

normalized_value_unit_evidence: Km: printed cell 71 uM; 1 uM is 1/1000 mM, so 71 / 1000 = 0.071 mM. kcat: printed cell 1.5 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.5 s^(-1). kcat/Km: printed cell 2.1 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.5 / 0.071 = 21.126760563380284 s^-1 mM^-1, against the printed catalytic-efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ZmALDH12 D226A block, substrate row NADP+: Km = 71 uM; kcat = 1.5 s^-1; printed kcat/Km = 2.1 x 10^4 s^-1 M^-1.

table_label: Table 1. Kinetic parameters for ZmALDH12 and PpALDH12. (J Mol Biol 2019, 431(3):576-592); printed column heads Substrate | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 M^-1), ZmALDH12 D226A block


column_label: Table 1 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 1, ZmALDH12 D226A block, substrate row NAD+: Km (uM) = 119; kcat (s^-1) = 1.7; kcat/Km (s^-1 M^-1) = 1.4 x 10^4.

normalized_value_unit_evidence: Km: printed cell 119 uM; 1 uM is 1/1000 mM, so 119 / 1000 = 0.119 mM. kcat: printed cell 1.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.7 s^(-1). kcat/Km: printed cell 1.4 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 14000 / 1000 = 14.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.7 / 0.119 = 14.285714285714286 s^-1 mM^-1, against the printed catalytic-efficiency cell 14.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ZmALDH12 D226A block, substrate row NAD+: Km = 119 uM; kcat = 1.7 s^-1; printed kcat/Km = 1.4 x 10^4 s^-1 M^-1.


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row S331A: Km (uM) = 624; kcat (s^-1) = 1.83; kcat/Km (s^-1 M^-1) = 2.8 x 10^3.

normalized_value_unit_evidence: Km: printed cell 624 uM; 1 uM is 1/1000 mM, so 624 / 1000 = 0.624 mM. kcat: printed cell 1.83 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.83 s^(-1). kcat/Km: printed cell 2.8 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2800 / 1000 = 2.8 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.83 / 0.624 = 2.932692307692308 s^-1 mM^-1, against the printed catalytic-efficiency cell 2.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row S331A: Km = 624 uM; kcat = 1.83 s^-1; printed kcat/Km = 2.8 x 10^3 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row S331A


column_label: The literal ZmALDH12 GRSAL row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.084 mM; kcat=1.9 s^-1; current same-row quotient=22.619047619047617 s^-1 mM^-1; printed efficiency=23 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: GRSAL cells: Km 84 ± 5 μM; kcat 1.9 ± 0.2 s^-1; printed kcat/Km 2.3 ± 0.4 × 10^4 s^-1 M^-1.

row_label: ZmALDH12 / GRSAL


assay_conditions_summary: pH 7.5; buffer 0.3 mM sub-saturating GSAL in 100 mM pyrophosphate; cofactor NAD+

column_label: The literal ZmALDH12 NAD+ row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.185 mM; kcat=3.1 s^-1; current same-row quotient=16.756756756756758 s^-1 mM^-1; printed efficiency=17 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: NAD+ cells: Km 185 ± 14 μM; kcat 3.1 ± 0.1 s^-1; printed kcat/Km 1.7 ± 0.2 × 10^4 s^-1 M^-1.

row_label: ZmALDH12 / NAD+


column_label: Table 1 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 1, ZmALDH12 D226A block, substrate row GSAL: Km (uM) = 266; kcat (s^-1) = 3.6; kcat/Km (s^-1 M^-1) = 1.3 x 10^4.

normalized_value_unit_evidence: Km: printed cell 266 uM; 1 uM is 1/1000 mM, so 266 / 1000 = 0.266 mM. kcat: printed cell 3.6 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.6 s^(-1). kcat/Km: printed cell 1.3 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13000 / 1000 = 13.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.6 / 0.266 = 13.533834586466165 s^-1 mM^-1, against the printed catalytic-efficiency cell 13.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ZmALDH12 D226A block, substrate row GSAL: Km = 266 uM; kcat = 3.6 s^-1; printed kcat/Km = 1.3 x 10^4 s^-1 M^-1.


column_label: The literal ZmALDH12 GSAL row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.198 mM; kcat=6.8 s^-1; current same-row quotient=34.34343434343434 s^-1 mM^-1; printed efficiency=34 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: GSAL cells: Km 198 ± 21 μM; kcat 6.8 ± 0.5 s^-1; printed kcat/Km 3.4 ± 0.6 × 10^4 s^-1 M^-1.

row_label: ZmALDH12 / GSAL


organism: Salmonella enterica

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


organism: Paraburkholderia xenovorans

substrate_name: propionaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I195F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: I195F mutant, steady state, pH 8.0, 25°C

substrate: propionaldehyde


proof_lines: wild-type protein, steady state, pH 8.0, 25°C

source_databases_merged: brenda oed


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I195L to reconstruct the assayed variant sequence.

proof_lines: I195L mutant, steady state, pH 8.0, 25°C


substrate_name: Butyraldehyde

smiles: CCCC=O

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: kcat is 17.2 and 16.3 sec(-1) with acetaldehyde and propanaldehyde as substrate, respectively (at pH 8 and 25 degrees Celsius).

substrate: Butyraldehyde


substrate_name: Isobutyraldehyde

substrate: Isobutyraldehyde


assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C


proof_lines: with acetaldehyde as substrate, pH 8.0 and 25°C


organism: Bilophila wadsworthia (strain 3_1_6)

substrate_name: sulfoacetaldehyde

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 54.76 sec(-1) with sulfoacetaldehyde as substrate. kcat is 33.8 sec(-1) with CoA as substrate. kcat is 38.9 sec(-1) with NADP(+) as substrate.

substrate: sulfoacetaldehyde


substrate_name: CoA

substrate: CoA


substrate_name: NADP(+)

substrate: NADP(+)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetaldehyde (in the presence of HsaF)

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

substrate: acetaldehyde (in the presence of HsaF)


substrate_name: propanal (in the presence of HsaF)

substrate: propanal (in the presence of HsaF)


substrate_name: coenzyme A (in the presence of HsaF)

substrate: coenzyme A (in the presence of HsaF)


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


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

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


organism: Thermus thermophilus

substrate_name: acetaldehyde

proof_lines:
BphJ-TTHB246 complex, pH 8.0, 25°C
TTHB247-BphI complex, pH 8.0, 25°C
TTHB246-TTHB247 complex, pH 8.0, 25°C

substrate: acetaldehyde


enzyme_display_name: Acetaldehyde dehydrogenase 4

organism: Paraburkholderia xenovorans (strain LB400)

substrate_name: NADP(+) (at pH 8 and 25 degrees Celsius)

column_label: Table 4 row NADP+, column Km,app (uM), gives 561 +/- 21 uM, normalized to 0.561 mM.

row_label: BphJ / NADP+

table_label: Table 4

enzyme: Acetaldehyde dehydrogenase 4


organism: Burkholderia xenovorans

substrate_name: Propanal; NAD+; Coenzyme A

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde; columns Km, kcat; cells Km 16.1+/-1.2, kcat 2.3+/-0.05.

normalized_value_unit_evidence: kcat normalized_value=2.3 normalized_unit=s^-1; Km normalized_value=16.1 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde: Km 16.1+/-1.2; kcat 2.3+/-0.05 s^-1.

substrate: Propanal; NAD+; Coenzyme A


substrate_name: NAD+; Coenzyme A; Propanal

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde; columns Km, kcat; cells Km 23.1+/-1.7, kcat 16.3+/-0.5.

normalized_value_unit_evidence: kcat normalized_value=16.3 normalized_unit=s^-1; Km normalized_value=23.1 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde: Km 23.1+/-1.7; kcat 16.3+/-0.5 s^-1.

substrate: NAD+; Coenzyme A; Propanal


substrate_name: propanal

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde; columns Km, kcat, kcat/Km; cells Km 23.1+/-1.7, kcat 16.3+/-0.5, kcat/Km 7.0+/-0.05 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=16.3 normalized_unit=s^-1; Km normalized_value=23.1 normalized_unit=mM; kcat/Km normalized_value=0.70 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde: Km 23.1+/-1.7; kcat 16.3+/-0.5 s^-1; kcat/Km 7.0+/-0.05 x10^2 M^-1 s^-1.

substrate: propanal


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde; columns Km, kcat, kcat/Km; cells Km 16.1+/-1.2, kcat 2.3+/-0.05, kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.3 normalized_unit=s^-1; Km normalized_value=16.1 normalized_unit=mM; kcat/Km normalized_value=0.14 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde: Km 16.1+/-1.2; kcat 2.3+/-0.05 s^-1; kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.


organism: Zea mays

substrate_name: NAD+

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NAD+

column_label: Table 1 / row NAD+ / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row NAD+ normalized: Km 0.185 mM; kcat 3.1 s^-1; kcat/Km 17.0 s^-1 mM^-1.

substrate: NAD+


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature D226A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NADP+

column_label: Table 1 / row NADP+ / enzyme block ZmALDH12 D226A / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 D226A row NADP+ normalized: Km 0.071 mM; kcat 1.5 s^-1; kcat/Km 21.0 s^-1 mM^-1.

row_label: ZmALDH12 D226A / NADP+

substrate: NADP+


column_label: Table 1 / row NADP+ / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row NADP+ normalized: Km 2.872 mM; kcat 0.8 s^-1; kcat/Km 0.27 s^-1 mM^-1.


substrate_name: 2-aminoadipic semialdehyde

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

column_label: Table 1 / row AASAL / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row AASAL normalized: Km 0.173 mM; kcat 0.04 s^-1; kcat/Km 0.2 s^-1 mM^-1.

substrate: 2-aminoadipic semialdehyde


substrate_name: D-glyceraldehyde 3-phosphate

column_label: Table 1 / row D-GAP / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row D-GAP normalized: Km 1.86 mM; kcat 0.4 s^-1; kcat/Km 0.21 s^-1 mM^-1.

substrate: D-glyceraldehyde 3-phosphate


substrate_name: L-glutamate 5-semialdehyde

column_label: Table 1 / row GSAL / enzyme block ZmALDH12 D226A / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 D226A row GSAL normalized: Km 0.266 mM; kcat 3.6 s^-1; kcat/Km 13.0 s^-1 mM^-1.

row_label: ZmALDH12 D226A / GSAL

substrate: L-glutamate 5-semialdehyde


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature E205A to reconstruct the assayed variant sequence.

column_label: Table 2 / row E205A / GSAL / enzyme block E205A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 E205A row E205A / GSAL normalized: Km 0.12 mM; kcat 0.21 s^-1; kcat/Km 1.8 s^-1 mM^-1.

row_label: E205A / E205A / GSAL

table_label: Table 2


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature F202A to reconstruct the assayed variant sequence.

column_label: Table 2 / row F202A / GSAL / enzyme block F202A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 F202A row F202A / GSAL normalized: Km 0.969 mM; kcat 0.15 s^-1; kcat/Km 0.15 s^-1 mM^-1.

row_label: F202A / F202A / GSAL


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature F505A to reconstruct the assayed variant sequence.

column_label: Table 2 / row F505A / GSAL / enzyme block F505A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 F505A row F505A / GSAL normalized: Km 0.17 mM; kcat 0.03 s^-1; kcat/Km 0.19 s^-1 mM^-1.

row_label: F505A / F505A / GSAL


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature K329A to reconstruct the assayed variant sequence.

column_label: Table 2 / row K329A / GSAL / enzyme block K329A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 K329A row K329A / GSAL normalized: Km 0.958 mM; kcat 0.26 s^-1; kcat/Km 0.27 s^-1 mM^-1.

row_label: K329A / K329A / GSAL


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature S331A to reconstruct the assayed variant sequence.

column_label: Table 2 / row S331A / GSAL / enzyme block S331A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 S331A row S331A / GSAL normalized: Km 0.624 mM; kcat 1.83 s^-1; kcat/Km 2.8 s^-1 mM^-1.

row_label: S331A / S331A / GSAL


column_label: Table 1 / row GSAL / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row GSAL normalized: Km 0.198 mM; kcat 6.8 s^-1; kcat/Km 34.0 s^-1 mM^-1.


column_label: Table 1 / row NAD+ / enzyme block ZmALDH12 D226A / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 D226A row NAD+ normalized: Km 0.119 mM; kcat 1.7 s^-1; kcat/Km 14.0 s^-1 mM^-1.

row_label: ZmALDH12 D226A / NAD+


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

assay_conditions_summary: pH 9; cofactor CoA

column_label: PMC full text states Km(app) values for NADP+, CoA, and sulfoacetaldehyde were 64, 102, and 330 uM, respectively; NADP+ maps to 64 uM.

raw_value_unit_evidence: Km raw_value=64 raw_unit=uM

row_label: SauS Km(app) values prose

table_label: PMID 20693281 PMC Purification and Characterization of SauS prose


substrate_name: CoA

column_label: PMC full text states Km(app) values for NADP+, CoA, and sulfoacetaldehyde were 64, 102, and 330 uM, respectively; CoA maps to 102 uM.

raw_value_unit_evidence: Km raw_value=102 raw_unit=uM


substrate_name: sulfoacetaldehyde

column_label: PMC full text states Km(app) values for NADP+, CoA, and sulfoacetaldehyde were 64, 102, and 330 uM, respectively; sulfoacetaldehyde maps to 330 uM.

raw_value_unit_evidence: Km raw_value=330 raw_unit=uM


substrate_name: Butyraldehyde

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Table 3 row butyraldehyde confirms Km and kcat but reports kcat/Km as 3.0 x10^2 M^-1 s^-1, normalized to 0.3 s^-1*mM^-1.

normalized_value_unit_evidence: Km 31.7 mM; kcat 9.5 s^-1; paper kcat/Km 0.3 s^-1*mM^-1

row_label: BphJ / butyraldehyde

table_label: Table 3

substrate: Butyraldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

column_label: Table 3 row isobutyraldehyde reports kcat/Km,app as 14.0 x10^2 M^-1 s^-1, normalized to 1.4 s^-1*mM^-1.

normalized_value_unit_evidence: Km 7.7 mM; kcat 11.2 s^-1; paper kcat/Km 1.4 s^-1*mM^-1

row_label: BphJ / isobutyraldehyde

substrate: Isobutyraldehyde


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Table 4 row NAD+ confirms Km and kcat but reports kcat/Km as 4.0 x10^5 M^-1 s^-1, normalized to 400 s^-1*mM^-1.

row_label: BphJ / NAD+


column_label: Table 4 row NADP+ confirms Km and kcat but reports kcat/Km as 0.22 x10^5 M^-1 s^-1, normalized to 22 s^-1*mM^-1.


organism: Physcomitrium patens

column_label: Table 1 / row AASAL / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row AASAL normalized: Km 0.211 mM; kcat 0.005 s^-1; kcat/Km 0.026 s^-1 mM^-1.

row_label: PpALDH12 / AASAL


column_label: Table 1 / row GSAL / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row GSAL normalized: Km 0.228 mM; kcat 0.44 s^-1; kcat/Km 1.9 s^-1 mM^-1.

row_label: PpALDH12 / GSAL


column_label: Table 1 / row NAD+ / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row NAD+ normalized: Km 0.227 mM; kcat 0.17 s^-1; kcat/Km 0.74 s^-1 mM^-1.

row_label: PpALDH12 / NAD+


column_label: Table 1 / row NADP+ / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row NADP+ normalized: Km 3.066 mM; kcat 0.05 s^-1; kcat/Km 0.014 s^-1 mM^-1.

row_label: PpALDH12 / NADP+


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.2; 301.15 K; cofactor NAD+

column_label: PMC full-text Table 3 row gammaGS under the recombinant TcP5CDH-His6 columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: TcP5CDH-His6 gammaGS row reports Km 72 uM, kcat 7 s^-1, kcat/Km 0.097 s^-1 uM^-1.

row_label: gammaGS

table_label: PMC Table 3, recombinant TcP5CDH-His6 kinetic parameters


assay_conditions_summary: pH 7.2; 301.15 K; cofactor NADP+

column_label: PMC full-text Table 3 row NAD+ under the recombinant TcP5CDH-His6 columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: TcP5CDH-His6 NAD+ row reports Km 72.3 uM, kcat 7.5 s^-1, kcat/Km 0.103 s^-1 uM^-1.

row_label: NAD+


column_label: PMC full-text Table 3 row NADP+ under the recombinant TcP5CDH-His6 columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: TcP5CDH-His6 NADP+ row reports Km 342 uM, kcat 1.2 s^-1, kcat/Km 0.003 s^-1 uM^-1.

row_label: NADP+


organism: Homo sapiens


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S352A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 293.15 K; cofactor NAD+


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


substrate_name: NAD

assay_conditions_summary: cofactor NAD+

column_label: PMID 22516612 / PMC3372638 Results prose linked to Table S1; human wild-type ALDH4A1; NAD+ Km 100 uM.

normalized_value_unit_evidence: Human wild-type ALDH4A1 NAD+ Km normalized_value=0.1 normalized_unit=mM.

raw_value_unit_evidence: Human wild-type ALDH4A1; NAD+ Km raw_value=100 raw_unit=uM.

row_label: Human wild-type ALDH4A1, NAD+

substrate: NAD


enzyme_display_name: Malonyl CoA reductase (NADP)

organism: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

substrate_name: malonyl-CoA (with 0.5 mM NADP)

assay_conditions_summary: cofactor NADPH

column_label: Full-text organism-specific properties paragraph reports M. sedula malonyl-CoA apparent Km 0.1 mM

raw_value_unit_evidence: Km raw_value=0.1 raw_unit=mM

row_label: Metallosphaera sedula partially purified native malonyl-CoA reductase

enzyme: Malonyl CoA reductase (NADP)

substrate: malonyl-CoA (with 0.5 mM NADP)


enzyme_display_name: Fatty acyl-CoA reductase 2, chloroplastic

organism: Arabidopsis thaliana

substrate_name: hexadecanoyl-CoA (at pH 7 and 30 degrees Celsius)

assay_conditions_summary: pH 7; buffer 100 mM potassium phosphate; cofactor CoA

column_label: Results prose under 'Kinetics of AtFAR2 utilizing C16:0-CoA and the effect of BSA on the enzyme activity' reports AtFAR2 had a Km value of 5.31 uM for C16:0-CoA; Figure 4A is the corresponding kinetics plot.

raw_value_unit_evidence: Km raw_value=5.31 raw_unit=uM

row_label: AtFAR2 / C16:0-CoA / hexadecanoyl-CoA

table_label: Figure 4A and Results prose: Kinetics of AtFAR2 utilizing C16:0-CoA


organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

substrate_name: oleoyl-CoA

proof_lines:
alkane biosynthesis pathway
acyl-acyl carrier protein reductase
aldehyde decarbonylase

substrate: oleoyl-CoA


organism: Streptococcus pyogenes

substrate_name: succinate semialdehyde

proof_lines: complete uncompetitive substrate inhibition

substrate: succinate semialdehyde


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

proof_lines:
rat liver mitochondria
P5C dehydrogenase


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

proof_lines: in the absence of Mg2+, at pH 7.5 and 37°C


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

proof_lines: with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C

proof_lines: with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

proof_lines: in the presence of 10 mM Mg2+, at pH 7.5 and 37°C


proof_lines: steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C

proof_lines: steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C


substrate_name: Succinic semialdehyde

proof_lines: steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C

proof_lines: steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C

proof_lines: partial substrate inhibition, pH 7.5 and 37°C

substrate: Succinic semialdehyde


organism: Klebsiella pneumoniae

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADP+


enzyme_display_name: UniProt O57693

organism: Thermoproteus tenax

proof_lines:
Raw SKiD Env: Temp=45°C, pH=7
Raw SKiD Env: Temp=70°C, pH=7

enzyme: UniProt O57693


proof_lines:
Raw SKiD Env: Temp=70°C, pH=7
Raw SKiD Env: Temp=45°C, pH=7


organism: Synechocystis sp. PCC 6803


organism: Trypanosoma brucei

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
cytosolic enzyme
glyoxysomal enzyme

substrate: NADH


substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines:
glyoxysomal enzyme
cytosolic enzyme

substrate: 3-phospho-D-glyceroyl phosphate


organism: Escherichia coli

substrate_name: 2-oxoglutarate semialdehyde

substrate: 2-oxoglutarate semialdehyde


substrate_name: NAD+

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+


organism: Pseudomonas putida

proof_lines: apparent value, in 100 mM Tris-HCl, pH 8.5, at 25°C


proof_lines: apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C


assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+

proof_lines: apparent value, in the presence of benzaldehyde, 100 mM glycine-NaOH (pH 9.2), at 25°C


substrate_name: benzaldehyde

proof_lines: in 100 mM glycine-NaOH (pH 9.2), at 25°C

substrate: benzaldehyde


organism: Saccharomyces cerevisiae


enzyme_display_name: D-glyceraldehyde dehydrogenase (NADP+)

organism: Picrophilus oshimae

substrate_name: D-glyceraldehyde

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

enzyme: D-glyceraldehyde dehydrogenase (NADP+)

substrate: D-glyceraldehyde


assay_conditions_summary: pH 6.9; 331.15 K; cofactor NADP+


substrate_name: D-glycerate

substrate: D-glycerate


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


organism: Vibrio variabilis

sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature L249A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 313.15 K; cofactor NADP+

row_label: L249A / L-AHG columns

table_label: Table 2. Kinetic parameters of VvAHGD and its mutants against NADP+ and L-AHG


sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature S176A to reconstruct the assayed variant sequence.

column_label: Table 2 row S176A, L-AHG columns: Km 1.45 ± 0.11 mM; kcat 10.67 ± 0.68 s^-1; kcat/Km 7.36 mM^-1 s^-1.

normalized_value_unit_evidence: Table 2 row S176A, L-AHG columns: Km 1.45 ± 0.11 mM; kcat 10.67 ± 0.68 s^-1; kcat/Km 7.36 s^-1 mM^-1.

row_label: S176A / L-AHG columns


sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature S227A to reconstruct the assayed variant sequence.

row_label: S227A / L-AHG columns


sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature S233A to reconstruct the assayed variant sequence.

row_label: S233A / L-AHG columns


assay_conditions_summary: pH 7; 313.15 K; buffer triplicate in 20 mM Tris-HCl; cofactor NADP+

column_label: Journal of Molecular Biology 2020 Table 2, row label Wild Type / L-AHG

normalized_value_unit_evidence: Normalized evidence: kcat=58.29 s^-1; km=1.2 mM.

raw_value_unit_evidence: Kinetic parameters of VvAHGD and its mutants against the cofactor NADP+ and the substrate L-AHG; row Wild Type / L-AHG; Km 1.2 mM; kcat 58.29 s^-1; kcat/Km 48.58 mM^-1 s^-1. To measure kinetic parameters against L-AHG, reactions were conducted in triplicate in 20 mM Tris-HCl buffer (pH 7.0) using L-AHG over 0-4.4 mM and NADP+ fixed at 1.5 mM.

row_label: Wild Type / L-AHG


row_label: L249A / NADP+ columns

substrate: NADP+


row_label: S176A / NADP+ columns


row_label: S227A / NADP+ columns


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S233A to reconstruct the assayed variant sequence.


organism: Nitrosomonas europaea

substrate_name: L-Glyceraldehyde 3-phosphate

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

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

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

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

substrate: L-Glyceraldehyde 3-phosphate


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


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

substrate: NAD+


enzyme_display_name: farnesal dehydrogenase

organism: Persicaria minor

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

assay_conditions_summary: pH 9.5; 308.15 K; cofactor NAD+

enzyme: farnesal dehydrogenase


substrate_name: citral

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

substrate: citral


substrate_name: trans-cinnamaldehyde

substrate: trans-cinnamaldehyde


substrate_name: alpha-methyl-cinnamaldehyde

substrate: alpha-methyl-cinnamaldehyde


enzyme_display_name: Aldehyde dehydrogenase family 3 member A2

organism: Homo sapiens

substrate_name: hexanal

smiles: CCCCCC=O

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

substrate: hexanal


substrate_name: octanal

smiles: CCCCCCCC=O

enzyme: Aldehyde dehydrogenase family 3 member A2

substrate: octanal


substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

substrate: dodecanal


substrate_name: tetradecanal

smiles: CCCCCCCCCCCCCC=O

substrate: tetradecanal


substrate_name: octadecanal

smiles: CCCCCCCCCCCCCCCCCC=O

substrate: octadecanal


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


organism: Thermoplasma acidophilum

substrate_name: NAD+

assay_conditions_summary: pH 7; 323.15 K; cofactor NAD+

column_label: Table 4: Cofactor Km- and kcat-values of key TaAlDH variants (Enzyme and Microbial Technology 53 (2013) 307-314); printed column heads TaAlDH variant | Km NADP+ (mM) | Km NAD+ (mM) | kcat NAD+ (s^-1) | kcat/Km NAD+ (s^-1 mM^-1). Table 4, variant row Wildtype; column Km NADP+ (mM) = 0.021; column Km NAD+ (mM) = 22.7; column kcat NAD+ (s^-1) = 1.64; column kcat/Km NAD+ (s^-1 mM^-1) = 0.07. captured primary segment: Table 4, variant row Wildtype | Cofactor Km and kcat values of key TaAlDH variants | construct Wildtype TaAlDH | cofactor substrate NAD+ | Km NADP+ 0.021 mM | Km NAD+ 22.7 mM | kcat NAD+ 1.64 s^-1 | kcat/Km NAD+ 0.07 s^-1 mM^-1 | assay 100 mM HEPES pH 7, 50 C

normalized_value_unit_evidence: Km: printed Table 4 cell Km NAD+ 22.7 mM; the cell is already in mM, so no unit conversion applies; the exported value is 22.7 mM. kcat: printed Table 4 cell kcat NAD+ 1.64 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 1.64 s^(-1). kcat/Km: printed Table 4 cell kcat/Km NAD+ 0.07 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and it normalizes to 0.07 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.64 / 22.7 = 0.0722466960352423 s^-1 mM^-1, which is the exported catalytic efficiency, and the printed efficiency cell 0.07 s^-1 mM^-1 is that same quotient written to the two decimals of the printed column.

raw_value_unit_evidence: Table 4, variant row Wildtype: Km NAD+ = 22.7 mM; kcat NAD+ = 1.64 s^-1; printed kcat/Km NAD+ = 0.07 s^-1 mM^-1; the same row prints Km NADP+ = 0.021 mM.

row_label: Table 4, variant row Wildtype


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9HK01 and applied mutation signature F34M/Y399C/S405N to reconstruct the assayed variant sequence.

column_label: Table 4: Cofactor Km- and kcat-values of key TaAlDH variants (Enzyme and Microbial Technology 53 (2013) 307-314); printed column heads TaAlDH variant | Km NADP+ (mM) | Km NAD+ (mM) | kcat NAD+ (s^-1) | kcat/Km NAD+ (s^-1 mM^-1). Table 4, variant row F34M-Y399C-S405N; column Km NADP+ (mM) = 0.031; column Km NAD+ (mM) = 16.7; column kcat NAD+ (s^-1) = 10.54; column kcat/Km NAD+ (s^-1 mM^-1) = 0.63. captured primary segment: Table 4, variant row F34M-Y399C-S405N | Cofactor Km and kcat values of key TaAlDH variants | construct TaAlDH F34M-Y399C-S405N | cofactor substrate NAD+ | Km NADP+ 0.031 mM | Km NAD+ 16.7 mM | kcat NAD+ 10.54 s^-1 | kcat/Km NAD+ 0.63 s^-1 mM^-1 | assay 100 mM HEPES pH 7, 50 C

normalized_value_unit_evidence: Km: printed Table 4 cell Km NAD+ 16.7 mM; the cell is already in mM, so no unit conversion applies; the exported value is 16.7 mM. kcat: printed Table 4 cell kcat NAD+ 10.54 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 10.54 s^(-1). kcat/Km: printed Table 4 cell kcat/Km NAD+ 0.63 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and it normalizes to 0.63 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.54 / 16.7 = 0.6311377245508982 s^-1 mM^-1, which is the exported catalytic efficiency, and the printed efficiency cell 0.63 s^-1 mM^-1 is that same quotient written to the two decimals of the printed column.

raw_value_unit_evidence: Table 4, variant row F34M-Y399C-S405N: Km NAD+ = 16.7 mM; kcat NAD+ = 10.54 s^-1; printed kcat/Km NAD+ = 0.63 s^-1 mM^-1; the same row prints Km NADP+ = 0.031 mM.

row_label: Table 4, variant row F34M-Y399C-S405N


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9HK01 and applied mutation signature F34M/S405N to reconstruct the assayed variant sequence.

column_label: Table 4: Cofactor Km- and kcat-values of key TaAlDH variants (Enzyme and Microbial Technology 53 (2013) 307-314); printed column heads TaAlDH variant | Km NADP+ (mM) | Km NAD+ (mM) | kcat NAD+ (s^-1) | kcat/Km NAD+ (s^-1 mM^-1). Table 4, variant row F34M-S405N; column Km NADP+ (mM) = 0.036; column Km NAD+ (mM) = 17.6; column kcat NAD+ (s^-1) = 10.99; column kcat/Km NAD+ (s^-1 mM^-1) = 0.62. captured primary segment: Table 4, variant row F34M-S405N | Cofactor Km and kcat values of key TaAlDH variants | construct TaAlDH F34M-S405N | cofactor substrate NAD+ | Km NADP+ 0.036 mM | Km NAD+ 17.6 mM | kcat NAD+ 10.99 s^-1 | kcat/Km NAD+ 0.62 s^-1 mM^-1 | assay 100 mM HEPES pH 7, 50 C

normalized_value_unit_evidence: Km: printed Table 4 cell Km NAD+ 17.6 mM; the cell is already in mM, so no unit conversion applies; the exported value is 17.6 mM. kcat: printed Table 4 cell kcat NAD+ 10.99 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 10.99 s^(-1). kcat/Km: printed Table 4 cell kcat/Km NAD+ 0.62 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and it normalizes to 0.62 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.99 / 17.6 = 0.6244318181818181 s^-1 mM^-1, which is the exported catalytic efficiency, and the printed efficiency cell 0.62 s^-1 mM^-1 is that same quotient written to the two decimals of the printed column.

raw_value_unit_evidence: Table 4, variant row F34M-S405N: Km NAD+ = 17.6 mM; kcat NAD+ = 10.99 s^-1; printed kcat/Km NAD+ = 0.62 s^-1 mM^-1; the same row prints Km NADP+ = 0.036 mM.

row_label: Table 4, variant row F34M-S405N


substrate_name: NADP+

assay_conditions_summary: pH 7; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F34M/Y399C/S405N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F34M/S405N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S176A to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 2 row S176A, L-AHG columns: Km 1.45 ± 0.11 mM; kcat 10.67 ± 0.68 s^-1; kcat/Km 7.36 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L249A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; buffer triplicate in 20 mM Tris-HCl; cofactor NADP+

column_label: Journal of Molecular Biology 2020 Table 2, row label Wild Type / L-AHG; kcat_over_km paper=48.58 s^-1 mM^-1; export=48.575 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=58.29 s^-1; km=1.2 mM; kcat_over_km=48.58 s^-1 mM^-1.


column_label: Journal of Molecular Biology 2020 Table 2, row label Wild Type / NADP+; kcat_over_km paper=209.36 s^-1 mM^-1; export=209.36363636363637 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=69.09 s^-1; km=0.33 mM; kcat_over_km=209.36 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic parameters of VvAHGD and its mutants against the cofactor NADP+ and the substrate L-AHG; row Wild Type / NADP+; Km 0.33 mM; kcat 69.09 s^-1; kcat/Km 209.36 mM^-1 s^-1. To measure kinetic parameters against NADP+, reactions were conducted in triplicate in 20 mM Tris-HCl buffer (pH 7.0) using NADP+ over 0-4.8 mM and L-AHG fixed at 3.52 mM.

row_label: Wild Type / NADP+


row_label: S233A / NADP+ columns


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: glyceraldehyde (at pH 6.9 and 58 degrees Celsius)

proof_lines: kcat is 10 sec(-1) with glyceraldehyde as substrate, 12 sec(-1) with glyceraldehyde-3-phosphate as substrate, 20 sec(-1) with glycolaldehyde as substrate and 10 sec(-1) with NADP as substrate (at pH 6.9 and 58 degrees Celsius).


substrate_name: glyceraldehyde-3-phosphate (at pH 6.9 and 58 degrees Celsius)

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


substrate_name: glycolaldehyde (at pH 6.9 and 58 degrees Celsius)


substrate_name: NADP (at pH 6.9 and 58 degrees Celsius)

substrate: NADP (at pH 6.9 and 58 degrees Celsius)


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: glyceraldehyde-3-phosphate (at pH 7.9 and 58 degrees Celsius)

proof_lines: kcat is 26 sec(-1) with glyceraldehyde as substrate, 20 sec(-1) with glyceraldehyde-3-phosphate as substrate, 37 sec(-1) with glycolaldehyde as substrate and 25 sec(-1) with NADP as substrate (at pH 7.9 and 58 degrees Celsius).


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

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


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


substrate_name: NAD (with G1P as effector)

sequence_variant_note: Mutation signature G1P/F6P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: cofactor ADP

proof_lines: Km applies to a data set exhibiting Michaelis-Menten kinetics. When an enzyme does not exhibit Michaelis-Menten kinetics the binding affinity is simply expressed as S0.5 which corresponds to the observed substrate concentration for 0.5 x Vm

substrate: NAD (with G1P as effector)


substrate_name: D-glyceraldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N286H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NAD+

substrate: D-glyceraldehyde


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 NADP+

proof_lines: pH and temperature not specified in the publication

substrate: NADP+


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

substrate: hexadecanal


substrate_name: farnesal

substrate: farnesal


substrate_name: D-glycerate

assay_conditions_summary: pH 6.9; cofactor NADP+

substrate: D-glycerate


column_label: Table 2 row Glyceraldehyde, T. acidophilum column: Km 0.2 mM; Kcat 26 s^-1; Kcat/Km 130 s^-1 mM^-1. Table 2 lines 195, 201, and 207: Glyceraldehyde row reports Km 0.2 mM, Kcat 26 s^-1, and Kcat/Km 130 s^-1 mM^-1 under T. acidophilum.

normalized_value_unit_evidence: km 0.2 mM; kcat 26 s^-1; kcat_over_km 130 s^-1*mM^-1

row_label: Glyceraldehyde, T. acidophilum column


substrate_name: glycolaldehyde

smiles: O=CCO

column_label: Table 2 row Glycolaldehyde, T. acidophilum column: Km 12.3 mM; Kcat 37 s^-1; Kcat/Km 3 s^-1 mM^-1. Table 2 lines 197, 203, and 209: Glycolaldehyde row reports Km 12.3 mM, Kcat 37 s^-1, and Kcat/Km 3 s^-1 mM^-1 under T. acidophilum.

normalized_value_unit_evidence: km 12.3 mM; kcat 37 s^-1; kcat_over_km 3 s^-1*mM^-1

row_label: Glycolaldehyde, T. acidophilum column

substrate: glycolaldehyde


substrate_name: NADP+

column_label: Table 2 row NADP+, T. acidophilum column: Km 0.36 mM; Kcat 25 s^-1; Kcat/Km 70 s^-1 mM^-1. Table 2 lines 198, 204, and 210: NADP+ row reports Km 0.36 mM, Kcat 25 s^-1, and Kcat/Km 70 s^-1 mM^-1 under T. acidophilum.

normalized_value_unit_evidence: km 0.36 mM; kcat 25 s^-1; kcat_over_km 70 s^-1*mM^-1

row_label: NADP+, T. acidophilum column


substrate_name: D-Glycerate

substrate: D-Glycerate


enzyme_display_name: L-2-aminoadipate reductase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: L-2-aminoadipate reductase

substrate: NADPH


substrate_name: D-glyceraldehyde 3-phosphate

column_label: Table 3 row D-Ga3P reports kcat 1.0 +/- 0.2 min^-1, Km 2.20 +/- 0.10 mM, and kcat/Km 8 M^-1 s^-1

raw_value_unit_evidence: Table 3 D-Ga3P row in the D-Ga3P/NAD+ block: kcat 1.0 +/- 0.2 min^-1; Km 2.20 +/- 0.10 mM; kcat/Km 8 M^-1 s^-1

substrate: D-glyceraldehyde 3-phosphate


substrate_name: L-Glyceraldehyde 3-phosphate

substrate: L-Glyceraldehyde 3-phosphate


substrate_name: NAD+

column_label: Table 3 row NAD+ reports kcat 1.0 +/- 0.2 min^-1, Km 0.40 +/- 0.03 mM, and kcat/Km 50 M^-1 s^-1

raw_value_unit_evidence: Table 3 NAD+ row in the D-Ga3P/NAD+ block: kcat 1.0 +/- 0.2 min^-1; Km 0.40 +/- 0.03 mM; kcat/Km 50 M^-1 s^-1

row_label: NAD+

substrate: NAD+


column_label: Table 3 row NADP+ reports kcat 0.80 +/- 0.01 min^-1, Km 0.23 +/- 0.01 mM, and kcat/Km 56 M^-1 s^-1

raw_value_unit_evidence: Table 3 NADP+ row in the D-Ga3P/NADP+ block: kcat 0.80 +/- 0.01 min^-1; Km 0.23 +/- 0.01 mM; kcat/Km 56 M^-1 s^-1

row_label: NADP+


assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines: with NAD+ as cosubstrate, at pH 8.0 and 30°C

proof_lines: with NADP+ as cosubstrate, at pH 8.0 and 30°C


organism: Picrophilus torridus

column_label: Table 2 row Glyceraldehyde, P. torridus column: Km 0.06 mM; Kcat 10 s^-1; Kcat/Km 167 s^-1 mM^-1. Table 2 lines 194-207: Glyceraldehyde row reports Km 0.06 mM, Kcat 10 s^-1, and Kcat/Km 167 s^-1 mM^-1 under P. torridus.

row_label: Glyceraldehyde, P. torridus column


column_label: Table 2 row Glycolaldehyde, P. torridus column: Km 11.1 mM; Kcat 20 s^-1; Kcat/Km 1.8 s^-1 mM^-1. Table 2 lines 197, 203, and 209: Glycolaldehyde row reports Km 11.1 mM, Kcat 20 s^-1, and Kcat/Km 1.8 s^-1 mM^-1 under P. torridus.

row_label: Glycolaldehyde, P. torridus column


column_label: Table 2 row NADP+, P. torridus column: Km 0.42 mM; Kcat 10 s^-1; Kcat/Km 24 s^-1 mM^-1. Table 2 lines 198, 204, and 210: NADP+ row reports Km 0.42 mM, Kcat 10 s^-1, and Kcat/Km 24 s^-1 mM^-1 under P. torridus.

normalized_value_unit_evidence: km 0.42 mM; kcat 10 s^-1; kcat_over_km 24 s^-1*mM^-1

row_label: NADP+, P. torridus column


proof_lines:
glyceraldehyde-3-phosphate
glycolaldehyde
glyceraldehyde dehydrogenase


table_label: Table 4: Cofactor Km- and kcat-values of key TaAlDH variants (Enzyme and Microbial Technology 53 (2013) 307-314); printed column heads TaAlDH variant | Km NADP+ (mM) | Km NAD+ (mM) | kcat NAD+ (s^-1) | kcat/Km NAD+ (s^-1 mM^-1)


column_label: PDF page 6 Table 4 row Wildtype reports Km NAD+ = 22.7 mM, kcat NAD+ = 1.64 s^-1, and rounded kcat/Km NAD+ = 0.07 s^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.64 normalized_unit=s^-1; Km normalized_value=22.7 normalized_unit=mM; kcat/Km table_normalized_value=0.07 normalized_unit=s^-1 mM^-1; CatLog computed ratio=0.0722466960352423.

row_label: Wildtype

table_label: Table 4: Cofactor Km- and kcat-values of key TaAlDH variants


proof_lines: Saccharomyces cerevisiae aminoadipate reductase


substrate_name: S-Carboxymethyl-L-cysteine

substrate: S-Carboxymethyl-L-cysteine


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: NADP (at 70 degrees Celsius)

column_label: Results prose states that S. solfataricus GAPN follows Michaelis-Menten kinetics for NADP+ and gives K_m 0.099 +/- 0.009 mM.

raw_value_unit_evidence: Km raw_value=0.099 +/- 0.009 raw_unit=mM

row_label: S. solfataricus GAPN / NADP+ Km

table_label: PMC full text PMID 15869466 S. solfataricus GAPN kinetic prose

substrate: NADP (at 70 degrees Celsius)


substrate_name: alpha-aminoadipate semialdehyde

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

substrate: alpha-aminoadipate semialdehyde


substrate_name: adipate

substrate: adipate


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


substrate_name: S-carboxymethyl-L-cysteine

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

substrate: S-carboxymethyl-L-cysteine


assay_conditions_summary: pH 8.8; 310.15 K; cofactor NADPH


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Pseudomonas sp.

substrate_name: Glutaric semialdehyde

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

enzyme: 2,5-dioxovalerate dehydrogenase

substrate: Glutaric semialdehyde


assay_conditions_summary: cofactor NADP+


assay_conditions_summary: cofactor NAD+


enzyme_display_name: UniProt P0AFG8

substrate_name: thiamine diphosphate

enzyme: UniProt P0AFG8

substrate: thiamine diphosphate


substrate_name: pyruvate

substrate: pyruvate


organism: Pseudomonas aeruginosa


smiles: C(CS)O


substrate_name: propanal

smiles: CCC=O

substrate: propanal


organism: Escherichia coli

substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


organism: Vibrio sp. EJY3

assay_conditions_summary: pH 8

proof_lines:
VejAHGD
Km
pH 8.0


enzyme_display_name: retinal dehydrogenase

organism: Rattus norvegicus

substrate_name: benzaldehyde

enzyme: retinal dehydrogenase

substrate: benzaldehyde


substrate_name: octanal

substrate: octanal


proof_lines: microsomes, high-fate diet rats, pH and temperature not specified in the publication

proof_lines: microsomes, control rats, pH and temperature not specified in the publication


enzyme_display_name: Bifunctional protein PaaZ

organism: Escherichia coli (strain K12)

substrate_name: oxepin-CoA (at 22 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; cofactor CoA

proof_lines:
PaaZ
oxepin-CoA
hydrolytic ring cleavage

enzyme: Bifunctional protein PaaZ


substrate_name: malonate semialdehyde

substrate: malonate semialdehyde


substrate_name: CoA

assay_conditions_summary: cofactor CoA

substrate: CoA


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: pyruvate dehydrogenase system

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

proof_lines: mutant Y177A, Hill coefficient 1.0, pH 7.0, 30°C

enzyme: pyruvate dehydrogenase system


proof_lines: wild-type, Hill coefficient 1.38, pH 7.0, 30°C


enzyme_display_name: glutamate-5-semialdehyde dehydrogenase

substrate_name: NADP+

enzyme: glutamate-5-semialdehyde dehydrogenase

substrate: NADP+


substrate_name: phosphate

substrate: phosphate


substrate_name: NADPH

substrate: NADPH


organism: Sus scrofa

proof_lines: wild boar, pH 7.5, temperature not specified in the publication


smiles: CC(=O)SCCNC(=O)CCNC(=O)[O-]

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: domestic pig, pH 7.5, temperature not specified in the publication


substrate_name: NAD+

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: NAD+


organism: Klebsiella pneumoniae

smiles: C(CO)C=O

assay_conditions_summary: pH 8; 318.15 K; cofactor NAD+


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


proof_lines: pH 7.0, 37°C, mutant S271E of isoform PDH2


proof_lines: pH 7.0, 37°C, mutant S203A of isoform PDH2


proof_lines: pH 7.0, 37°C, mutant S271A of isoform PDH2


proof_lines: pH 7.0, 37°C, mutant S203E of isoform PDH2


organism: Ascaris suum

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NAD+


organism: Lathyrus oleraceus

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


assay_conditions_summary: pH 7.6; 295.15 K; cofactor NAD+


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


organism: Arthrobacter sp. Cr-7

substrate_name: Isopyridoxal

substrate: Isopyridoxal


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


enzyme_display_name: 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase

organism: Pseudomonas sp. MA-1

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, temperature not specified in the publication


enzyme: 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase


organism: Solanum tuberosum

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


substrate_name: pyruvate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


organism: Ricinus communis

substrate_name: coenzyme A

substrate: coenzyme A


substrate: pyruvate


organism: Bacillus subtilis

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


organism: Bos taurus

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate, in presence of 2 mM Mn2+

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate, in presence of 2 mM Ca2+

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate, in presence of 2 mM Mn2+


proof_lines: pH 7.6, 30°C, overall reaction of complex


organism: Lactococcus lactis subsp. lactis

substrate_name: hydroxyethyl thiamine diphosphate

substrate: hydroxyethyl thiamine diphosphate


proof_lines: the complex displays cooperativity, Hill coefficient is 0.7, pH not specified in the publication, temperature not specified in the publication


assay_conditions_summary: pH 7.6; 303.15 K; cofactor CoA

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate


assay_conditions_summary: pH 7.6; 303.15 K; cofactor NAD+


organism: Brassica oleracea


organism: Hordeum vulgare

assay_conditions_summary: pH 7.6; cofactor CoA

proof_lines: absence of malate, pH 7.6, temperature not specified in the publication

proof_lines: presence of 1 mM malate, pH 7.6, temperature not specified in the publication


assay_conditions_summary: pH 7.6; cofactor NAD+


organism: Escherichia coli

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

assay_conditions_summary: pH 8; cofactor NADH

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label 3-Hydroxypropionic acid (footnote b) / NADH; kcat_over_km paper=2.2 s^-1 mM^-1; export=2.166666666666667 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.26 s^-1; km=0.12 mM; kcat_over_km=2.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row 3-Hydroxypropionic acid (footnote b) / NADH; Vmax 0.30 +/- 0.05 U mg^-1 protein; Km 0.12 +/- 0.004 mM; kcat 0.26 +/- 0.04 s^-1; kcat/Km 2.20 +/- 0.35 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NADH. Footnote: Reverse reaction.


assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
pH 8.0, 37°C, cofactor: NADP+
pH 8.0, 37°C, cofactor: NAD+


substrate_name: acetaldehyde

smiles: CC=O

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Acetaldehyde / NAD+

normalized_value_unit_evidence: Normalized evidence: kcat=11.03 s^-1; km=1 mM; kcat_over_km=11.03 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Acetaldehyde / NAD+; Vmax 12.39 +/- 1.98 U mg^-1 protein; Km 1.00 +/- 0.030 mM; kcat 11.03 +/- 1.76 s^-1; kcat/Km 11.03 +/- 1.76 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Acetaldehyde / NAD+

substrate: acetaldehyde


substrate_name: benzaldehyde

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Benzaldehyde / NADP+; kcat_over_km paper=3.23 s^-1 mM^-1; export=3.23463687150838 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=17.37 s^-1; km=5.37 mM; kcat_over_km=3.23 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Benzaldehyde / NADP+; Vmax 19.51 +/- 3.12 U mg^-1 protein; Km 5.37 +/- 0.161 mM; kcat 17.37 +/- 2.78 s^-1; kcat/Km 3.23 +/- 0.52 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NADP+.

row_label: Benzaldehyde / NADP+

substrate: benzaldehyde


substrate_name: propionaldehyde

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Propionaldehyde / NAD+; kcat_over_km paper=20.12 s^-1 mM^-1; export=20.123966942148762 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=24.35 s^-1; km=1.21 mM; kcat_over_km=20.12 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Propionaldehyde / NAD+; Vmax 27.35 +/- 5.90 U mg^-1 protein; Km 1.21 +/- 0.036 mM; kcat 24.35 +/- 3.89 s^-1; kcat/Km 20.12 +/- 3.21 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Propionaldehyde / NAD+

substrate: propionaldehyde


column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Valeraldehyde / NAD+; kcat_over_km paper=109.32 s^-1 mM^-1; export=109.33333333333333 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=26.24 s^-1; km=0.24 mM; kcat_over_km=109.32 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Valeraldehyde / NAD+; Vmax 29.47 +/- 4.99 U mg^-1 protein; Km 0.24 +/- 0.007 mM; kcat 26.24 +/- 4.20 s^-1; kcat/Km 109.32 +/- 17.5 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Valeraldehyde / NAD+


column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Butyraldehyde / NAD+; kcat_over_km paper=27.79 s^-1 mM^-1; export=27.783505154639176 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=26.95 s^-1; km=0.97 mM; kcat_over_km=27.79 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Butyraldehyde / NAD+; Vmax 30.07 +/- 4.81 U mg^-1 protein; Km 0.97 +/- 0.029 mM; kcat 26.95 +/- 4.31 s^-1; kcat/Km 27.79 +/- 4.45 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Butyraldehyde / NAD+


column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Isovaleraldehyde / NAD+; kcat_over_km paper=40.16 s^-1 mM^-1; export=40.16176470588235 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=27.31 s^-1; km=0.68 mM; kcat_over_km=40.16 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Isovaleraldehyde / NAD+; Vmax 30.67 +/- 4.91 U mg^-1 protein; Km 0.68 +/- 0.020 mM; kcat 27.31 +/- 4.37 s^-1; kcat/Km 40.16 +/- 6.43 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Isovaleraldehyde / NAD+


organism: Mammalia

proof_lines: pyruvate dehydrogenase preparation with high activity


organism: Homo sapiens

proof_lines:
E1 component, pH 7.6, 30°C
pH 7.0, 37°C, isoform PDH2
pH 7.0, 37°C, isoform PDH1


organism: [Bacillus] caldolyticus


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


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: cooperativity is observed, Hill coefficient is 1.6, pH 7.6, 37°C


organism: Synechocystis sp. PCC 6803

proof_lines: presence of 0.002 mM inhibitor N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-nitrobenzenesulfonamide, pH 7.2, 37°C


substrate_name: acetylphosphinate

substrate: acetylphosphinate


organism: Rhodospirillum rubrum

substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Pigeon


organism: Sus scrofa

proof_lines: domestic pig, pH 7.5, temperature not specified in the publication


organism: Dictyostelium discoideum


organism: Neurospora crassa

proof_lines:
similar values
pH 7.4, 30°C


substrate_name: lipoyl domain

proof_lines:
assay with whole enzyme complex
pH 8.0, 30°C

substrate: lipoyl domain


organism: Saccharomyces pastorianus

substrate_name: Unknown

proof_lines: assay with whole enzyme complex, competitive inhibition

substrate: Unknown


organism: Ricinus communis

assay_conditions_summary: cofactor NAD+

proof_lines: competitive inhibition vs. NAD+, whole enzyme complex

proof_lines: competitive inhibition vs. CoA, whole enzyme complex


organism: Lathyrus oleraceus

substrate_name: CoA

assay_conditions_summary: pH 7.6; 295.15 K; cofactor CoA

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

substrate: CoA


organism: Saccharomyces cerevisiae


enzyme_display_name: 2-oxoglutarate dehydrogenase system

organism: Urocitellus richardsonii

assay_conditions_summary: pH 7.8; 295.15 K; cofactor CoA

proof_lines: overall reaction, enzyme from euthermic animals, 22°C, pH 7.8

proof_lines: overall reaction, enzyme from euthermic animals, 37°C, pH 7.8

proof_lines: overall reaction, enzyme from euthermic animals, 5°C, pH 7.8

enzyme: 2-oxoglutarate dehydrogenase system


assay_conditions_summary: pH 7.8; 278.15 K; cofactor NAD+

proof_lines: overall reaction, enzyme from hibernating animals, 5°C, pH 7.8

proof_lines: overall reaction, enzyme from hibernating animals, 37°C, pH 7.8


assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: S0.5 value, 0.15 M ionic strength, pH 7.8, 30°C

proof_lines: S0.5 value, 0.10 M ionic strength, pH 7.8, 30°C

proof_lines: S0.5 value, 0.05 M ionic strength, pH 7.8, 30°C


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: S0.5 value, Hill coefficient 0.4, pH 7.5, temperature not specified in the publication


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


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

proof_lines:
enzyme-specific activity, pH 7.5, 37°C
overall-assay, pH 7.5, 37°C
component E1, pH 7.5, 37°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


enzyme_display_name: [amino-group carrier protein]-5-phospho-L-glutamate reductase

organism: Thermus thermophilus

substrate_name: [amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde


substrate_name: phosphate

enzyme: [amino-group carrier protein]-5-phospho-L-glutamate reductase

substrate: phosphate


substrate_name: NADP+

assay_conditions_summary: pH 9.5; cofactor NADP+

substrate: NADP+


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H298T to reconstruct the assayed variant sequence.

proof_lines: mutant H298T, pH not specified in the publication, temperature not specified in the publication


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H260E to reconstruct the assayed variant sequence.

proof_lines: mutant H260E, pH not specified in the publication, temperature not specified in the publication


column_label: Table 2. Effect of H298 and H260/H298 substitutions on E1-specific activity of OGDHc; bottom panel, 2-OV; row none / 2-OV; columns kcat (s^-1); Km; kcat/Km (s^-1 mM^-1)

normalized_value_unit_evidence: kcat normalized_value=0.076 normalized_unit=s^-1; Km normalized_value=16.3 normalized_unit=mM; kcat/Km normalized_value=0.0047 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.076 +/- 0.007 raw_unit=s^-1; Km raw_value=16.3 +/- 4.00 in Km (mM) raw_unit=mM; kcat/Km raw_value=0.0047 raw_unit=s^-1*mM^-1

row_label: none / 2-OV


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H298L to reconstruct the assayed variant sequence.

proof_lines: mutant H298L, pH not specified in the publication, temperature not specified in the publication