enzyme_display_name: Acetaldehyde dehydrogenase 4

organism: Paraburkholderia xenovorans (strain LB400)

substrate_name: acetaldehyde (at pH 8 and 25 degrees Celsius)

column_label: Table 3 row acetaldehyde, column Km,app (mM), gives 23.6 +/- 1.8 mM.

row_label: BphJ / acetaldehyde

table_label: Table 3

enzyme: Acetaldehyde dehydrogenase 4


substrate_name: propanaldehyde (at pH 8 and 25 degrees Celsius)

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

smiles: CCC=O

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 3 row propionaldehyde, column Km,app (mM), gives 23.1 +/- 1.7 mM. Source substrate label propanaldehyde is the same aldehyde name as paper propionaldehyde.

row_label: BphJ / propionaldehyde

data_origin: experimental

status: verified

source: uniprot


substrate_name: butyraldehyde (at pH 8 and 25 degrees Celsius)

smiles: CCCC=O

column_label: Table 3 row butyraldehyde, column Km,app (mM), gives 31.7 +/- 2.2 mM.

row_label: BphJ / butyraldehyde


substrate_name: isobutyraldehyde (at pH 8 and 25 degrees Celsius)

smiles: CC(C)C=O

column_label: Table 3 row isobutyraldehyde, column Km,app (mM), gives 7.7 +/- 0.5 mM.

row_label: BphJ / isobutyraldehyde


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

column_label: Table 4 row NAD+, column Km,app (uM), gives 34.8 +/- 1.9 uM, normalized to 0.0348 mM.

row_label: BphJ / NAD+

table_label: Table 4

substrate: NAD(+) (at pH 8 and 25 degrees Celsius)


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

assay_conditions_summary: pH 8; cofactor NADP+

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

row_label: BphJ / NADP+


enzyme_display_name: aspartate-semialdehyde dehydrogenase

organism: Neurospora crassa

substrate_name: NADPH

source_db: brenda

verification_status: unverified

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

assay_conditions_summary: cofactor NADPH

enzyme: aspartate-semialdehyde dehydrogenase

substrate: NADPH

status: unverified

source: brenda


organism: Cryptosporidium parvum

substrate_name: NAD+

assay_conditions_summary: pH 8.8; cofactor NAD+

proof_lines: wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, pH 8.8, temperature not specified in the publication

substrate: NAD+


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: Acetaldehyde dehydrogenase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

smiles: CC=O

assay_conditions_summary: pH 8

proof_lines: The catalytic efficiency is similar when using acetaldehyde or propanaldehyde as substrate.

enzyme: Acetaldehyde dehydrogenase

substrate: acetaldehyde (at pH 8 and 25 degrees Celsius)


substrate: propanaldehyde (at pH 8 and 25 degrees Celsius)


organism: Triticum aestivum

substrate_name: NADP

proof_lines: When the protein is phosphorylated, the affinity for substrates is similar but the Vmax is lowered.

substrate: NADP


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


enzyme_display_name: Aspartate-semialdehyde dehydrogenase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: NADP(+)

proof_lines: kcat is 4 sec(-1) for the L-4-aspartyl-phosphate-forming reaction (at 70 degrees Celsius).

enzyme: Aspartate-semialdehyde dehydrogenase

substrate: NADP(+)


substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

substrate: NAD(+)


organism: Apium graveolens

proof_lines: Measured at pH 7.7 and 30 degrees Celsius for all experiments.


organism: Saccharomyces cerevisiae


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


organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

proof_lines: kcat is 33 sec(-1) with D-glyceraldehyde 3-phosphate.


proof_lines: kcat is 165 sec(-1) with D-glyceraldehyde 3-phosphate.


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: succinate semialdehyde

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F138A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

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

mutation_type: substitution

proof_lines: mutant enzyme F138A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C

substrate: succinate semialdehyde


organism: Escherichia coli (strain K12)

substrate_name: NAD

proof_lines: kcat is 1056 sec(-1) for dehydrogenase activity.

substrate: NAD


organism: Geobacillus stearothermophilus

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

sequence_source: multiple

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
poly(ethylene glycol)-bound NAD+
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

source_databases_merged: brenda skid


enzyme_display_name: Succinate-semialdehyde dehydrogenase

organism: Paenarthrobacter nicotinovorans

proof_lines: kcat is 23000 sec(-1) with NADP(+) as cosubstrate.

enzyme: Succinate-semialdehyde dehydrogenase


enzyme_display_name: Succinate semialdehyde dehydrogenase [NAD(P)+] Sad

substrate_name: succinate semialdehyde (with 0.6 mM NAD, at pH 8 and at 30 degrees Celsius)

proof_lines: The enzyme reduced NADP at 15 % of the rate of NAD reduction.


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: L-aspartate 4-semialdehyde

proof_lines: kcat is 6.1 sec(-1) with L-aspartate 4-semialdehyde as substrate.

substrate: L-aspartate 4-semialdehyde


organism: Escherichia coli

substrate_name: NADP+

source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q162N with inferred residue-numbering offset +16 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADP+

substrate: NADP+

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q39D with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31D/Q39D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31L to reconstruct the assayed variant sequence.


substrate_name: Phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q162H with inferred residue-numbering offset +16 to reconstruct the assayed variant sequence.

smiles: O=P(O)(O)O

substrate: Phosphate


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_cached_fasta_accession:P0A9Q9 and applied mutation signature R267L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.6; 298.15 K; buffer pH 8; cofactor NADPH

column_label: Table 1: Kinetic Parameters of Mutated ASA DH (Biochemistry 1995, 34(19):6394-6399); printed column heads enzyme | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1) for the phosphate block. Table 1, enzyme row 'R267L'; column kcat (s-1) = 58; column Km (mM) = 19; column kcat/Km (s-1 mM-1) = 3.0. captured primary segment: Table 1. Kinetic Parameters of Mutated ASA DH | phosphate | Escherichia coli ASA DH R267L | kcat 58 s-1 | Km 19 mM | kcat/Km 3.0 s-1 mM-1 | assay 200 mM CHES buffer pH 8.6, 25 C

normalized_value_unit_evidence: Km: printed Table 1 cell 19 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 19 mM. kcat: printed Table 1 cell 58 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 58.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 3.0 s-1 mM-1 is already in the canonical unit, so the paper value for this metric is 3.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 58 / 19 = 3.0526315789473686 s^-1 mM^-1, which falls outside the rounding interval of the printed cell 3.0 at every place value that literal could carry, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 1, enzyme row 'R267L', phosphate block: kcat = 58 s-1; Km = 19 mM; printed kcat/Km = 3.0 s-1 mM-1.

row_label: Table 1. Kinetic Parameters of Mutated ASA DH, enzyme row 'R267L', phosphate block

status: corrected


assay_conditions_summary: pH 8.6; 298.15 K; cofactor NAD+


substrate_name: L-Aspartate 4-semialdehyde

substrate: L-Aspartate 4-semialdehyde


sequence_variant_note: Resolved canonical sequence from uniprot_cached_fasta_accession:P0A9Q9 and applied mutation signature Q39D to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of Mutated ASA DH (Biochemistry 1995, 34(19):6394-6399); printed column heads enzyme | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1) for the l-ASA block. Table 1, enzyme row 'Q39D'; column kcat (s-1) = 290; column Km (mM) = 0.13; column kcat/Km (s-1 mM-1) = 2300. captured primary segment: Table 1. Kinetic Parameters of Mutated ASA DH | l-ASA | Escherichia coli ASA DH Q39D | kcat 290 s-1 | Km 0.13 mM | kcat/Km 2300 s-1 mM-1 | assay 200 mM CHES buffer pH 8.6, 25 C

normalized_value_unit_evidence: Km: printed Table 1 cell 0.13 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 0.13 mM. kcat: printed Table 1 cell 290 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 290.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 2300 s-1 mM-1 is already in the canonical unit, so the paper value for this metric is 2300.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 290 / 0.13 = 2230.7692307692305 s^-1 mM^-1, which falls outside the rounding interval of the printed cell 2300 at every place value that literal could carry, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 1, enzyme row 'Q39D', l-ASA block: kcat = 290 s-1; Km = 0.13 mM; printed kcat/Km = 2300 s-1 mM-1.

row_label: Table 1. Kinetic Parameters of Mutated ASA DH, enzyme row 'Q39D', l-ASA block


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R267L with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


organism: Oryza sativa

substrate_name: 3-Phospho-D-glyceroyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37G with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADH

column_label: Table 6, Kinetic parameters of wild-type and mutant OsGAPDHs; row F37G; Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [BPG] (mM) = 0.051 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.14 s^-1; calculated kcat/Km from these cells = 2.7450980392156867 s^-1 mM^-1.

raw_value_unit_evidence: Table 6 row F37G: Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [BPG] (mM) = 0.051 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.14 s^-1; kcat/Km calculated as 0.14 / 0.051 = 2.7450980392156867 s^-1 mM^-1.

substrate: 3-Phospho-D-glyceroyl phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37L with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: Table 6, Kinetic parameters of wild-type and mutant OsGAPDHs; row F37L; Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [BPG] (mM) = 0.049 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.06 s^-1; calculated kcat/Km from these cells = 1.2244897959183672 s^-1 mM^-1.

raw_value_unit_evidence: Table 6 row F37L: Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [BPG] (mM) = 0.049 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.06 s^-1; kcat/Km calculated as 0.06 / 0.049 = 1.2244897959183672 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37T with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: Table 6, Kinetic parameters of wild-type and mutant OsGAPDHs; row F37T; Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [BPG] (mM) = 0.053 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.08 s^-1; calculated kcat/Km from these cells = 1.509433962264151 s^-1 mM^-1.

raw_value_unit_evidence: Table 6 row F37T: Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [BPG] (mM) = 0.053 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.08 s^-1; kcat/Km calculated as 0.08 / 0.053 = 1.509433962264151 s^-1 mM^-1.


column_label: Table 6; row Wild type; reverse reaction [coenzyme: NAD(P)H] block, column KM [BPG] (mM) raw value 0.036 and column kcat (s^-1) raw value 73.56; kcat/Km computed by division of those two table cells.

normalized_value_unit_evidence: kcat 73.56 s^-1 = 73.56 s^-1 (no conversion). Km 0.036 mM = 0.036 mM (no conversion). kcat/Km is not printed in the table, so it is paper_kcat/paper_km = 73.56 / 0.036 = 2043.3333333333335 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Wild type row, reverse reaction NADH columns: KM [BPG] (mM) = 0.036 and kcat (s^-1) = 73.56 (same row also lists KM [NADH] (mM) = 0.061). kcat/Km is not printed in Table 6.

row_label: Wild type; reverse reaction [coenzyme: NAD(P)H], NADH columns

table_label: Table 6. Kinetic parameters of wild-type and mutant OsGAPDHs


substrate_name: D-Glyceraldehyde 3-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0J8A4 and applied mutation signature F37G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.8; 298.15 K; buffer NAD(P) and D-glyceraldehyde 3-phosphate in a

column_label: Table 6: Kinetic parameters of wild-type and mutant OsGAPDHs (Plant Mol Biol 2012), line 'F37G'; column 'kcat (S-1)' of the forward reaction [coenzyme: NAD(P)] = 0.24; the KM (mM) for the substrate D-glyceraldehyde 3-phosphate, forward reaction [coenzyme: NAD(P)] cell = 0.156; the NADP column of the forward reaction prints ND; Table 6 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.24 in the forward-reaction kcat (S-1) column; the unit is already per second, so no unit conversion applies and the paper value is 0.24 s^(-1). Km: printed Table 6 cell 0.156 in the column of the KM (mM) for the substrate D-glyceraldehyde 3-phosphate; the unit is already mM, so no unit conversion applies and the paper value is 0.156 mM. kcat/Km: Table 6 has no kcat/Km column, so 1.5384615384615383 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.24 / 0.156 of this line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 6, row 'F37G': the forward-reaction kcat (S-1) cell reads 0.24 and the KM (mM) for the substrate D-glyceraldehyde 3-phosphate cell reads 0.156. Table 6 carries no kcat/Km column.

row_label: Table 6, row 'F37G'

substrate: D-Glyceraldehyde 3-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0J8A4 and applied mutation signature F37L to reconstruct the assayed variant sequence.

column_label: Table 6: Kinetic parameters of wild-type and mutant OsGAPDHs (Plant Mol Biol 2012), line 'F37L'; column 'kcat (S-1)' of the forward reaction [coenzyme: NAD(P)] = 0.09; the KM (mM) for the substrate D-glyceraldehyde 3-phosphate, forward reaction [coenzyme: NAD(P)] cell = 0.149; the NADP column of the forward reaction prints ND; Table 6 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.09 in the forward-reaction kcat (S-1) column; the unit is already per second, so no unit conversion applies and the paper value is 0.09 s^(-1). Km: printed Table 6 cell 0.149 in the column of the KM (mM) for the substrate D-glyceraldehyde 3-phosphate; the unit is already mM, so no unit conversion applies and the paper value is 0.149 mM. kcat/Km: Table 6 has no kcat/Km column, so 0.6040268456375839 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.09 / 0.149 of this line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 6, row 'F37L': the forward-reaction kcat (S-1) cell reads 0.09 and the KM (mM) for the substrate D-glyceraldehyde 3-phosphate cell reads 0.149. Table 6 carries no kcat/Km column.

row_label: Table 6, row 'F37L'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0J8A4 and applied mutation signature F37T to reconstruct the assayed variant sequence.

column_label: Table 6: Kinetic parameters of wild-type and mutant OsGAPDHs (Plant Mol Biol 2012), line 'F37T'; column 'kcat (S-1)' of the forward reaction [coenzyme: NAD(P)] = 0.13; the KM (mM) for the substrate D-glyceraldehyde 3-phosphate, forward reaction [coenzyme: NAD(P)] cell = 0.161; the NADP column of the forward reaction prints ND; Table 6 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.13 in the forward-reaction kcat (S-1) column; the unit is already per second, so no unit conversion applies and the paper value is 0.13 s^(-1). Km: printed Table 6 cell 0.161 in the column of the KM (mM) for the substrate D-glyceraldehyde 3-phosphate; the unit is already mM, so no unit conversion applies and the paper value is 0.161 mM. kcat/Km: Table 6 has no kcat/Km column, so 0.8074534161490683 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.13 / 0.161 of this line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 6, row 'F37T': the forward-reaction kcat (S-1) cell reads 0.13 and the KM (mM) for the substrate D-glyceraldehyde 3-phosphate cell reads 0.161. Table 6 carries no kcat/Km column.

row_label: Table 6, row 'F37T'


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

column_label: Table 6; current measurement `a71c2374774e176c` / review `7255f36bcd81f029`; location Table 6; measurement Wild type / D-G3P forward reaction tuple; construct recombinant native wild-type OsGAPDH; substrate D-Glyceraldehyde 3-phosphate; condition Forward reaction with coenzyme NAD and D-G3P at 25 C; NAD(P)H formation monitored at 340 nm; kinetic constants from varied coenzyme or substrate concentrations and Lineweaver-Burk plots. Same-measurement primary component kcat: raw 122.24 s^(-1) (paper label s^-1), normalized 122.24 s^(-1); same-measurement primary component Km: raw 0.111 mM, normalized 0.111 mM. The paper has no kcat/Km cell; derived 122.24 / 0.111 = 1101.261261261261 s^-1*mM^-1.

raw_value_unit_evidence: Wild type forward reaction: kcat 122.24 s^-1; KM [D-G3P] 0.111 mM; no printed kcat/Km cell.

row_label: Wild type


assay_conditions_summary: pH 8.8; 298.15 K; buffer NAD(P) and D-glyceraldehyde 3-phosphate in a; cofactor NAD+

column_label: Table 6: Kinetic parameters of wild-type and mutant OsGAPDHs (Plant Mol Biol 2012), line 'F37G'; column 'kcat (S-1)' of the forward reaction [coenzyme: NAD(P)] = 0.24; the KM [NAD] (mM), forward reaction [coenzyme: NAD(P)] cell = 0.362; the NADP column of the forward reaction prints ND; Table 6 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.24 in the forward-reaction kcat (S-1) column; the unit is already per second, so no unit conversion applies and the paper value is 0.24 s^(-1). Km: printed Table 6 cell 0.362 in the column of the KM (mM) for the coenzyme NAD; the unit is already mM, so no unit conversion applies and the paper value is 0.362 mM. kcat/Km: Table 6 has no kcat/Km column, so 0.6629834254143646 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.24 / 0.362 of this line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 6, row 'F37G': the forward-reaction kcat (S-1) cell reads 0.24 and the KM (mM) for the coenzyme NAD cell reads 0.362. Table 6 carries no kcat/Km column.


column_label: Table 6: Kinetic parameters of wild-type and mutant OsGAPDHs (Plant Mol Biol 2012), line 'F37L'; column 'kcat (S-1)' of the forward reaction [coenzyme: NAD(P)] = 0.09; the KM [NAD] (mM), forward reaction [coenzyme: NAD(P)] cell = 0.527; the NADP column of the forward reaction prints ND; Table 6 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.09 in the forward-reaction kcat (S-1) column; the unit is already per second, so no unit conversion applies and the paper value is 0.09 s^(-1). Km: printed Table 6 cell 0.527 in the column of the KM (mM) for the coenzyme NAD; the unit is already mM, so no unit conversion applies and the paper value is 0.527 mM. kcat/Km: Table 6 has no kcat/Km column, so 0.17077798861480076 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.09 / 0.527 of this line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 6, row 'F37L': the forward-reaction kcat (S-1) cell reads 0.09 and the KM (mM) for the coenzyme NAD cell reads 0.527. Table 6 carries no kcat/Km column.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F138A to reconstruct the assayed variant sequence.

smiles: O=CCCC(=O)O

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row F138A / SSA (NAD+)b; Kapp_m column raw 0.12 +/- 0.02; kcat column raw 26 +/- 1; kcat/Kapp_m column raw 2.1 x 10^5; footnote b: assays performed in the presence of 2.0 mM NAD+.

normalized_value_unit_evidence: Km normalized_value=0.12 normalized_unit=mM; kcat normalized_value=26 normalized_unit=s^-1; kcat/Km normalized_value=216.66666666666669 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.12 +/- 0.02 raw_unit=mM; kcat raw_value=26 +/- 1 raw_unit=s^-1; kcat/Kapp_m raw_value=2.1 x 10^5 raw_unit=M^-1 s^-1

row_label: F138A / SSA (NAD+)b


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K92A to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row K92A / SSA (NAD+)b; Kapp_m column raw 2.6 +/- 0.5; kcat column raw 73 +/- 8; kcat/Kapp_m column raw 2.8 x 10^4; footnote b: assays performed in the presence of 2.0 mM NAD+.

normalized_value_unit_evidence: Km normalized_value=2.6 normalized_unit=mM; kcat normalized_value=73 normalized_unit=s^-1; kcat/Km normalized_value=28.076923076923077 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=2.6 +/- 0.5 raw_unit=mM; kcat raw_value=73 +/- 8 raw_unit=s^-1; kcat/Kapp_m raw_value=2.8 x 10^4 raw_unit=M^-1 s^-1

row_label: K92A / SSA (NAD+)b


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R145A to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row R145A / SSA (NAD+)b; Kapp_m column raw 2.49 +/- 0.72; kcat column raw 45 +/- 9; kcat/Kapp_m column raw 1.8 x 10^4; footnote b: assays performed in the presence of 2.0 mM NAD+.

normalized_value_unit_evidence: Km normalized_value=2.49 normalized_unit=mM; kcat normalized_value=45 normalized_unit=s^-1; kcat/Km normalized_value=18.072289156626503 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=2.49 +/- 0.72 raw_unit=mM; kcat raw_value=45 +/- 9 raw_unit=s^-1; kcat/Kapp_m raw_value=1.8 x 10^4 raw_unit=M^-1 s^-1

row_label: R145A / SSA (NAD+)b


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R428A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S425A to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row S425A / SSA (NAD+)b; Kapp_m column raw 0.22 +/- 0.01; kcat column raw 68 +/- 1; kcat/Kapp_m column raw 3.1 x 10^5; footnote b: assays performed in the presence of 2.0 mM NAD+.

normalized_value_unit_evidence: Km normalized_value=0.22 normalized_unit=mM; kcat normalized_value=68 normalized_unit=s^-1; kcat/Km normalized_value=309.09090909090907 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.22 +/- 0.01 raw_unit=mM; kcat raw_value=68 +/- 1 raw_unit=s^-1; kcat/Kapp_m raw_value=3.1 x 10^5 raw_unit=M^-1 s^-1

row_label: S425A / SSA (NAD+)b


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W141A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row W141A / SSA (NAD+)b; Kapp_m column raw 0.77 +/- 0.10; kcat column raw 66 +/- 6; kcat/Kapp_m column raw 8.6 x 10^4; footnote b: assays performed in the presence of 2.0 mM NAD+.

normalized_value_unit_evidence: Km normalized_value=0.77 normalized_unit=mM; kcat normalized_value=66 normalized_unit=s^-1; kcat/Km normalized_value=85.71428571428571 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.77 +/- 0.10 raw_unit=mM; kcat raw_value=66 +/- 6 raw_unit=s^-1; kcat/Kapp_m raw_value=8.6 x 10^4 raw_unit=M^-1 s^-1

row_label: W141A / SSA (NAD+)b


column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row WT / SSA (NADP+)c; Kapp_m column raw 0.047 +/- 0.006; kcat column raw 83 +/- 7; kcat/Kapp_m column raw 1.8 x 10^6; footnote c: assays performed in the presence of 6.0 mM NADP+.

normalized_value_unit_evidence: Km normalized_value=0.047 normalized_unit=mM; kcat normalized_value=83 normalized_unit=s^-1; kcat/Km normalized_value=1765.9574468085107 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.047 +/- 0.006 raw_unit=mM; kcat raw_value=83 +/- 7 raw_unit=s^-1; kcat/Kapp_m raw_value=1.8 x 10^6 raw_unit=M^-1 s^-1

row_label: WT / SSA (NADP+)c


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


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


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


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


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


assay_conditions_summary: pH 8.9; 298.15 K; cofactor NADH

column_label: Table II: Kinetic parameters of wild-type and mutants of GapB-encoded protein, and wild-type and mutant of B. stearothermophilus GAPDH (JBC 1997, 272(24):15106-15112); Table II, row Wild-type GapB-encoded protein, glyceraldehyde 3-phosphate assay; the kcat value 0.12 s-1 comes from the turnover-number column of the glyceraldehyde 3-phosphate substrate block and the Michaelis constant 1.10 mM comes from the Michaelis-constant column for D-glyceraldehyde 3-phosphate. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 0.12 s-1; already in s^-1, no conversion (this article prints no min^-1 kinetic value); the paper value is 0.12 s^(-1). Km: printed cell 1.10 mM; already in mM, no conversion; the paper value is 1.1 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 0.10909090909090907 s^(-1)*mM^(-1) is not a printed value; it is the quotient 0.12 / 1.10 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Table II, row Wild-type GapB-encoded protein, glyceraldehyde 3-phosphate assay: kcat = 0.12 s-1 (printed column the turnover-number column of the glyceraldehyde 3-phosphate substrate block); Km = 1.10 mM (printed column the Michaelis-constant column for D-glyceraldehyde 3-phosphate). No kcat/Km value is printed for this measurement.


substrate_name: Glycerate 1,3-bisphosphate

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7 for the reverse reaction; cofactor NADH

column_label: Results section, reverse-direction paragraph of JBC 1997, 272(24):15106-15112 (reverse reaction with 1,3-dPG); Results prose, reverse direction with 1,3-dPG, GapB-encoded protein; the kcat value 0.074 s-1 comes from the reverse-reaction turnover number stated in the Results prose and the Michaelis constant 0.08 mM comes from the reverse-reaction Michaelis constant for 1,3-dPG stated in the Results prose. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 0.074 s-1; already in s^-1, no conversion (this article prints no min^-1 kinetic value); the paper value is 0.074 s^(-1). Km: printed cell 0.08 mM; already in mM, no conversion; the paper value is 0.08 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 0.9249999999999999 s^(-1)*mM^(-1) is not a printed value; it is the quotient 0.074 / 0.08 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Results prose, reverse direction with 1,3-dPG, GapB-encoded protein: kcat = 0.074 s-1 (printed column the reverse-reaction turnover number stated in the Results prose); Km = 0.08 mM (printed column the reverse-reaction Michaelis constant for 1,3-dPG stated in the Results prose). No kcat/Km value is printed for this measurement.

substrate: Glycerate 1,3-bisphosphate


assay_conditions_summary: pH 8.9; 298.15 K; cofactor NAD+


column_label: Table 6: Kinetic parameters of wild-type and mutant OsGAPDHs (Plant Mol Biol 2012), line 'F37T'; column 'kcat (S-1)' of the forward reaction [coenzyme: NAD(P)] = 0.13; the KM [NAD] (mM), forward reaction [coenzyme: NAD(P)] cell = 0.417; the NADP column of the forward reaction prints ND; Table 6 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.13 in the forward-reaction kcat (S-1) column; the unit is already per second, so no unit conversion applies and the paper value is 0.13 s^(-1). Km: printed Table 6 cell 0.417 in the column of the KM (mM) for the coenzyme NAD; the unit is already mM, so no unit conversion applies and the paper value is 0.417 mM. kcat/Km: Table 6 has no kcat/Km column, so 0.3117505995203837 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.13 / 0.417 of this line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 6, row 'F37T': the forward-reaction kcat (S-1) cell reads 0.13 and the KM (mM) for the coenzyme NAD cell reads 0.417. Table 6 carries no kcat/Km column.


assay_conditions_summary: pH 8.8; 298.15 K; cofactor NAD+

column_label: Table 6; current measurement `c3ae989909b3ccfa` / review `17395f3738340ae4`; location Table 6; measurement Wild type / NAD forward reaction tuple; construct recombinant native wild-type OsGAPDH; substrate NAD+; condition Forward reaction with coenzyme NAD and D-G3P at 25 C; NAD(P)H formation monitored at 340 nm; kinetic constants from varied coenzyme or substrate concentrations and Lineweaver-Burk plots. Same-measurement primary component kcat: raw 122.24 s^(-1) (paper label s^-1), normalized 122.24 s^(-1); same-measurement primary component Km: raw 0.059 mM, normalized 0.059 mM. The paper has no kcat/Km cell; derived 122.24 / 0.059 = 2071.864406779661 s^-1*mM^-1.

raw_value_unit_evidence: Wild type forward reaction: kcat 122.24 s^-1; KM [NAD] 0.059 mM; no printed kcat/Km cell.


substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37G with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: Table 6, Kinetic parameters of wild-type and mutant OsGAPDHs; row F37G; Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.367 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.14 s^-1; calculated kcat/Km from these cells = 0.3814713896457766 s^-1 mM^-1.

raw_value_unit_evidence: Table 6 row F37G: Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.367 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.14 s^-1; kcat/Km calculated as 0.14 / 0.367 = 0.3814713896457766 s^-1 mM^-1.

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37L with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: Table 6, Kinetic parameters of wild-type and mutant OsGAPDHs; row F37L; Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.537 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.06 s^-1; calculated kcat/Km from these cells = 0.11173184357541899 s^-1 mM^-1.

raw_value_unit_evidence: Table 6 row F37L: Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.537 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.06 s^-1; kcat/Km calculated as 0.06 / 0.537 = 0.11173184357541899 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37T with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: Table 6, Kinetic parameters of wild-type and mutant OsGAPDHs; row F37T; Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.403 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.08 s^-1; calculated kcat/Km from these cells = 0.19851116625310172 s^-1 mM^-1.

raw_value_unit_evidence: Table 6 row F37T: Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.403 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 0.08 s^-1; kcat/Km calculated as 0.08 / 0.403 = 0.19851116625310172 s^-1 mM^-1.


column_label: Table 6, Kinetic parameters of wild-type and mutant OsGAPDHs; row Wild type; Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.061 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 73.56 s^-1; calculated kcat/Km from these cells = 1205.9016393442623 s^-1 mM^-1.

raw_value_unit_evidence: Table 6 row Wild type: Reverse reaction [coenzyme: NAD(P)H] / NADH / KM [NADH] (mM) = 0.061 mM; Reverse reaction [coenzyme: NAD(P)H] / NADH / kcat (s^-1) = 73.56 s^-1; kcat/Km calculated as 73.56 / 0.061 = 1205.9016393442623 s^-1 mM^-1.


organism: Paraburkholderia xenovorans

substrate_name: picolinaldehyde

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row WT, substrate picolinaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 18.2 +/- 1.3; 2.8 +/- 0.1; 154 +/- 12.

normalized_value_unit_evidence: Km 18.2 mM; kcat 2.8 s^-1; printed kcat/Km 0.154 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 WT — picolinaldehyde: Km 18.2 +/- 1.3 mM; kcat 2.8 +/- 0.1 s^-1; printed kcat/Km 154 +/- 12 M^-1 s^-1.

row_label: WT — picolinaldehyde

substrate: picolinaldehyde


substrate_name: propionaldehyde

sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:Q79AF6 and applied mutation signature I195A to reconstruct the assayed variant sequence.

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I195A, substrate propionaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 31.5 +/- 2.7; 12.1 +/- 0.6; 384 +/- 35.

raw_value_unit_evidence: Table 2 I195A — propionaldehyde: Km 31.5 +/- 2.7 mM; kcat 12.1 +/- 0.6 s^-1; printed kcat/Km 384 +/- 35 M^-1 s^-1.

row_label: I195A — propionaldehyde

substrate: propionaldehyde


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:Q79AF6 and applied mutation signature I195F to reconstruct the assayed variant sequence.

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I195F, substrate propionaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 45.7 +/- 4.1; 7.6 +/- 0.3; 167 +/- 16.

normalized_value_unit_evidence: Km 45.7 mM; kcat 7.6 s^-1; printed kcat/Km 0.167 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 I195F — propionaldehyde: Km 45.7 +/- 4.1 mM; kcat 7.6 +/- 0.3 s^-1; printed kcat/Km 167 +/- 16 M^-1 s^-1.

row_label: I195F — propionaldehyde


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

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row WT, substrate propionaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 23.1 +/- 1.7; 16.3 +/- 0.5; 700 +/- 50.

normalized_value_unit_evidence: Km 23.1 mM; kcat 16.3 s^-1; printed kcat/Km 0.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 WT — propionaldehyde: Km 23.1 +/- 1.7 mM; kcat 16.3 +/- 0.5 s^-1; printed kcat/Km 700 +/- 50 M^-1 s^-1.

row_label: WT — propionaldehyde


substrate_name: NAD+

substrate: NAD+


column_label: Table II row Wild-type GapB-encoded protein / NAD+ (GAPDH activity): kcat cell 0.12 s^-1; KM cell 0.9 mM; no kcat/KM column/cell is printed, so kcat_over_km 0.13333333333333333 s^-1 mM^-1 is the quotient 0.12 / 0.9 of the two printed cells.

normalized_value_unit_evidence: kcat 0.12 s^-1; Km 0.9 mM; kcat/Km derived as 0.12 / 0.9 = 0.13333333333333333 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type GapB-encoded protein / NAD+ (GAPDH activity): kcat=0.12 s^-1; km=0.9 mM; kcat_over_km=not explicitly reported.

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

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


column_label: Results main text, JBC page 15110, paragraph on the reverse direction with 1,3-dPG as substrate; Wild-type GapB-encoded protein / NADH (reverse reaction with 1,3-dPG): kcat 0.074 s^-1; KM 0.05 mM; no kcat/KM value is printed, so kcat_over_km 1.4799999999999998 s^-1 mM^-1 is the quotient 0.074 / 0.05 of the two printed prose values.

normalized_value_unit_evidence: kcat 0.074 s^-1; Km 0.05 mM; kcat/Km derived as 0.074 / 0.05 = 1.4799999999999998 s^-1 mM^-1 from the two printed prose values; the paper prints no kcat/KM value.

raw_value_unit_evidence: Results main text, JBC page 15110, paragraph on the reverse direction with 1,3-dPG as substrate; Wild-type GapB-encoded protein / NADH (reverse reaction with 1,3-dPG): kcat=0.074 s^-1; km=0.05 mM; kcat_over_km=1.4799999999999998 s^-1 mM^-1 derived as the quotient 0.074 / 0.05 s^-1 / mM; no kcat/KM value is printed in the paper.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K160A to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row K160A / NAD+a; Kapp_m column raw 10 +/- 1; kcat column raw 39 +/- 2; kcat/Kapp_m column raw 3.8 x 10^3; footnote a: assays performed in the presence of 0.1 mM SSA.

normalized_value_unit_evidence: Km normalized_value=10 normalized_unit=mM; kcat normalized_value=39 normalized_unit=s^-1; kcat/Km normalized_value=3.9 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=10 +/- 1 raw_unit=mM; kcat raw_value=39 +/- 2 raw_unit=s^-1; kcat/Kapp_m raw_value=3.8 x 10^3 raw_unit=M^-1 s^-1

row_label: K160A / NAD+a


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K160E to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row K160E / NAD+a; Kapp_m column raw 11 +/- 2; kcat column raw 80 +/- 3; kcat/Kapp_m column raw 7.3 x 10^3; footnote a: assays performed in the presence of 0.1 mM SSA.

normalized_value_unit_evidence: Km normalized_value=11 normalized_unit=mM; kcat normalized_value=80 normalized_unit=s^-1; kcat/Km normalized_value=7.2727272727272725 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=11 +/- 2 raw_unit=mM; kcat raw_value=80 +/- 3 raw_unit=s^-1; kcat/Kapp_m raw_value=7.3 x 10^3 raw_unit=M^-1 s^-1

row_label: K160E / NAD+a


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N193A to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row N193A / NAD+d; Kapp_m column raw 0.15 +/- 0.02; kcat column raw 14 +/- 1; kcat/Kapp_m column raw 9.7 x 10^4; footnote d: assays performed in the presence of 0.5 mM SSA.

normalized_value_unit_evidence: Km normalized_value=0.15 normalized_unit=mM; kcat normalized_value=14 normalized_unit=s^-1; kcat/Km normalized_value=93.33333333333334 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.15 +/- 0.02 raw_unit=mM; kcat raw_value=14 +/- 1 raw_unit=s^-1; kcat/Kapp_m raw_value=9.7 x 10^4 raw_unit=M^-1 s^-1

row_label: N193A / NAD+d


column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row WT / NAD+a; Kapp_m column raw 0.043 +/- 0.003; kcat column raw 38 +/- 1; kcat/Kapp_m column raw 8.8 x 10^5; footnote a: assays performed in the presence of 0.1 mM SSA.

normalized_value_unit_evidence: Km normalized_value=0.043 normalized_unit=mM; kcat normalized_value=38 normalized_unit=s^-1; kcat/Km normalized_value=883.7209302325582 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.043 +/- 0.003 raw_unit=mM; kcat raw_value=38 +/- 1 raw_unit=s^-1; kcat/Kapp_m raw_value=8.8 x 10^5 raw_unit=M^-1 s^-1

row_label: WT / NAD+a


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row K160A / NADP+a; Kapp_m column raw 26 +/- 7; kcat column raw 2.6 +/- 0.3; kcat/Kapp_m column raw 1.0 x 10^2; footnote a: assays performed in the presence of 0.1 mM SSA.

normalized_value_unit_evidence: Km normalized_value=26 normalized_unit=mM; kcat normalized_value=2.6 normalized_unit=s^-1; kcat/Km normalized_value=0.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=26 +/- 7 raw_unit=mM; kcat raw_value=2.6 +/- 0.3 raw_unit=s^-1; kcat/Kapp_m raw_value=1.0 x 10^2 raw_unit=M^-1 s^-1

row_label: K160A / NADP+a


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ZPI3 and applied mutation signature K160E to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row K160E / NADP+a; Kapp_m column raw 27 +/- 7; kcat column raw 2.1 +/- 0.2; kcat/Kapp_m column raw 7.7 x 10; footnote a: assays performed in the presence of 0.1 mM SSA.

normalized_value_unit_evidence: Km normalized_value=27 normalized_unit=mM; kcat normalized_value=2.1 normalized_unit=s^-1; kcat/Km normalized_value=0.07777777777777778 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=27 +/- 7 raw_unit=mM; kcat raw_value=2.1 +/- 0.2 raw_unit=s^-1; kcat/Kapp_m raw_value=7.7 x 10 raw_unit=M^-1 s^-1

row_label: K160E / NADP+a


column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row N193A / NADP+d; Kapp_m column raw 2.4 +/- 0.5; kcat column raw 21 +/- 2; kcat/Kapp_m column raw 8.6 x 10^3; footnote d: assays performed in the presence of 0.5 mM SSA.

normalized_value_unit_evidence: Km normalized_value=2.4 normalized_unit=mM; kcat normalized_value=21 normalized_unit=s^-1; kcat/Km normalized_value=8.75 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=2.4 +/- 0.5 raw_unit=mM; kcat raw_value=21 +/- 2 raw_unit=s^-1; kcat/Kapp_m raw_value=8.6 x 10^3 raw_unit=M^-1 s^-1

row_label: N193A / NADP+d


column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row WT / NADP+a; Kapp_m column raw 0.48 +/- 0.04; kcat column raw 46 +/- 1; kcat/Kapp_m column raw 9.5 x 10^4; footnote a: assays performed in the presence of 0.1 mM SSA.

normalized_value_unit_evidence: Km normalized_value=0.48 normalized_unit=mM; kcat normalized_value=46 normalized_unit=s^-1; kcat/Km normalized_value=95.83333333333334 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.48 +/- 0.04 raw_unit=mM; kcat raw_value=46 +/- 1 raw_unit=s^-1; kcat/Kapp_m raw_value=9.5 x 10^4 raw_unit=M^-1 s^-1

row_label: WT / NADP+a


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ZPI3 and applied mutation signature D426A to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row D426A / SSA (NAD+)b; Kapp_m column raw 0.23 +/- 0.05; kcat column raw 0.3 +/- 0.1; kcat/Kapp_m column raw 1.3 x 10^3; footnote b: assays performed in the presence of 2.0 mM NAD+.

normalized_value_unit_evidence: Km normalized_value=0.23 normalized_unit=mM; kcat normalized_value=0.3 normalized_unit=s^-1; kcat/Km normalized_value=1.3043478260869563 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.23 +/- 0.05 raw_unit=mM; kcat raw_value=0.3 +/- 0.1 raw_unit=s^-1; kcat/Kapp_m raw_value=1.3 x 10^3 raw_unit=M^-1 s^-1

row_label: D426A / SSA (NAD+)b


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E442A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

column_label: Table II. Kinetic Parameters of the Wild-Type and Mutant YneI with SSA as a Substrate; row E442A / SSA (NAD+)b; Kapp_m column raw 0.14 +/- 0.02; kcat column raw 164 +/- 17; kcat/Kapp_m column raw 1.1 x 10^6; footnote b: assays performed in the presence of 2.0 mM NAD+.

normalized_value_unit_evidence: Km normalized_value=0.14 normalized_unit=mM; kcat normalized_value=164 normalized_unit=s^-1; kcat/Km normalized_value=1171.4285714285713 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Kapp_m raw_value=0.14 +/- 0.02 raw_unit=mM; kcat raw_value=164 +/- 17 raw_unit=s^-1; kcat/Kapp_m raw_value=1.1 x 10^6 raw_unit=M^-1 s^-1

row_label: E442A / SSA (NAD+)b


organism: Corynebacterium glutamicum

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

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

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

row_label: D35G / NAD


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


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

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

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


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

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

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


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

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

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

row_label: L36T / NAD


column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row Wildtype / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.048+/-0.002, Kcat 387+/-28, Kcat/Km 8063+/-540.

normalized_value_unit_evidence: Km normalized_value=0.048 normalized_unit=mM; kcat normalized_value=6.45 normalized_unit=s^-1; kcat/Km normalized_value=134.383333333333 normalized_unit=s^-1 mM^-1.

row_label: Wildtype / NAD


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADP+

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

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

row_label: D35G / NADP


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

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

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


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

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


substrate_name: acetaldehyde

sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:Q79AF6 and applied mutation signature D208A to reconstruct the assayed variant sequence.

column_label: Official ACS publisher PDF, Table 1. Steady-State Kinetic Parameters of BphJ with Acetaldehyde as the Substrate, row D208A, substrate acetaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 18.7 +/- 1.4; 7.6 +/- 0.2; 406 +/- 34.

normalized_value_unit_evidence: Km 18.7 mM; kcat 7.6 s^-1; printed kcat/Km 0.406 s^-1 mM^-1.

row_label: D208A — acetaldehyde

substrate: acetaldehyde


column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I195A, substrate acetaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 133 +/- 12; 19.7 +/- 0.9; 147 +/- 15.

normalized_value_unit_evidence: Km 133 mM; kcat 19.7 s^-1; printed kcat/Km 0.147 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 I195A — acetaldehyde: Km 133 +/- 12 mM; kcat 19.7 +/- 0.9 s^-1; printed kcat/Km 147 +/- 15 M^-1 s^-1.

row_label: I195A — acetaldehyde


column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I195F, substrate acetaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 33.7 +/- 3.2; 15.4 +/- 0.6; 457 +/- 48.

row_label: I195F — acetaldehyde


column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row WT, substrate acetaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 23.6 +/- 1.8; 17.2 +/- 0.5; 730 +/- 60.

normalized_value_unit_evidence: Km 23.6 mM; kcat 17.2 s^-1; printed kcat/Km 0.73 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 WT — acetaldehyde: Km 23.6 +/- 1.8 mM; kcat 17.2 +/- 0.5 s^-1; printed kcat/Km 730 +/- 60 M^-1 s^-1.

row_label: WT — acetaldehyde


substrate_name: Butyraldehyde

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I195A, substrate butyraldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 4.6 +/- 0.3; 12.6 +/- 0.3; 2763 +/- 181.

normalized_value_unit_evidence: Km 4.6 mM; kcat 12.6 s^-1; printed kcat/Km 2.763 s^-1 mM^-1.

row_label: I195A — butyraldehyde

substrate: Butyraldehyde


column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row WT, substrate butyraldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 31.7 +/- 2.2; 9.5 +/- 0.2; 300 +/- 20.

normalized_value_unit_evidence: Km 31.7 mM; kcat 9.5 s^-1; printed kcat/Km 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 WT — butyraldehyde: Km 31.7 +/- 2.2 mM; kcat 9.5 +/- 0.2 s^-1; printed kcat/Km 300 +/- 20 M^-1 s^-1.

row_label: WT — butyraldehyde


substrate_name: pentaldehyde

smiles: CCCCC=O

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I195A, substrate pentaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 8.2 +/- 0.8; 13.0 +/- 0.4; 1584 +/- 156.

normalized_value_unit_evidence: Km 8.2 mM; kcat 13 s^-1; printed kcat/Km 1.584 s^-1 mM^-1.

row_label: I195A — pentaldehyde

substrate: pentaldehyde


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:Q79AF6 and applied mutation signature I171A to reconstruct the assayed variant sequence.

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I171A, substrate picolinaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 3.2 +/- 0.3; 1.9 +/- 0.1; 597 +/- 53.

normalized_value_unit_evidence: Km 3.2 mM; kcat 1.9 s^-1; printed kcat/Km 0.597 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 I171A — picolinaldehyde: Km 3.2 +/- 0.3 mM; kcat 1.9 +/- 0.1 s^-1; printed kcat/Km 597 +/- 53 M^-1 s^-1.

row_label: I171A — picolinaldehyde


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:Q79AF6 and applied mutation signature I171F to reconstruct the assayed variant sequence.

column_label: Official ACS publisher PDF, Table 2. Substrate Specificity of BphJ in the Dehydrogenase Reaction, row I171F, substrate picolinaldehyde, columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 12.0 +/- 1.0; 2.4 +/- 0.1; 202 +/- 17.

normalized_value_unit_evidence: Km 12 mM; kcat 2.4 s^-1; printed kcat/Km 0.202 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 I171F — picolinaldehyde: Km 12.0 +/- 1.0 mM; kcat 2.4 +/- 0.1 s^-1; printed kcat/Km 202 +/- 17 M^-1 s^-1.

row_label: I171F — picolinaldehyde


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:Q79AF6 and applied mutation signature I195A to reconstruct the assayed variant sequence.

column_label: Preserved review/source evidence states the PMID 22574886 Table 2 I195A picolinaldehyde entry matches Km 6.9 mM, kcat 3.2 s^-1, and kcat/Km 0.468 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=3.2 normalized_unit=s^-1; Km normalized_value=6.9 normalized_unit=mM; kcat/Km normalized_value=0.468 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=3.2 raw_unit=s^-1; Km raw_value=6.9 raw_unit=mM; kcat/Km raw_value=0.468 raw_unit=s^-1 mM^-1

row_label: BphJ I195A / picolinaldehyde

table_label: Preserved PMID 22574886 Table 2 evidence from current verified_catlog note/source record


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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Table 2 row L36T / NADP gives Km 1.46 mM, Kcat 95 min^-1, and Kcat/Km 65 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=1.46 mM; Kcat normalized_value=1.5833333333333333 s^-1; Kcat/Km normalized_value=1.0833333333333333 s^-1 mM^-1

raw_value_unit_evidence: NADP row: Km raw_value=1.46 mM; Kcat raw_value=95 min^-1; Kcat/Km raw_value=65 mM^-1 min^-1

row_label: L36T GAPDH mutant / NADP coenzyme

table_label: ScienceDirect full-text Table 2: Enzyme kinetics of GAPDH and mutants


organism: Crocosphaera subtropica

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

assay_conditions_summary: pH 9; 298.15 K; buffer for 5 min; cofactor NADP+

column_label: Table 1 (Kinetic parameters of cce4228 wild-type and mutants with different cofactors), NADP+ cofactor block, wild-type column head 'wild-typee' (the trailing e is Table 1 footnote marker e); printed row 'kcatSSA (s-1) a' = 3.9 ± 0.3; printed row 'KNADP+ m (mM) b' = 0.034 ± 0.002; Table 1 prints no kcat/Km cell for the NADP+ substrate axis of this column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.9 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 3.9 s^(-1). Km: printed Table 1 cell 0.034 mM; already in mM, no unit conversion applies; the paper value is 0.034 mM. kcat/Km: Table 1 prints no kcat/Km cell for the NADP+ substrate axis of this column, so the paper value 114.70588235294116 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 3.9 / 0.034 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, NADP+ cofactor block, wild-type column: kcat = 3.9 ± 0.3 s-1 (printed row 'kcatSSA (s-1) a'); Km = 0.034 ± 0.002 mM (printed row 'KNADP+ m (mM) b'); Table 1 prints no kcat/Km cell for the NADP+ substrate axis of this column.

table_label: Table 1: Kinetic parameters of cce4228 wild-type and mutants with different cofactors (PLoS ONE 2020, 15(9):e0239372)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B1WSJ7 and applied mutation signature K154A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 298.15 K; buffer for 5 min; cofactor NAD+

column_label: Table 1 (Kinetic parameters of cce4228 wild-type and mutants with different cofactors), NAD+ cofactor block, column head 'Lys154Ala'; printed row 'k catSSA (s-1) c' = 0.13± 0.07; printed row 'KNAD+ m (mM) d' = 1.5 ± 0.4; Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.13 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.13 s^(-1). Km: printed Table 1 cell 1.5 mM; already in mM, no unit conversion applies; the paper value is 1.5 mM. kcat/Km: Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column, so the paper value 0.08666666666666667 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.13 / 1.5 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, NAD+ cofactor block, Lys154Ala column: kcat = 0.13± 0.07 s-1 (printed row 'k catSSA (s-1) c'); Km = 1.5 ± 0.4 mM (printed row 'KNAD+ m (mM) d'); Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B1WSJ7 and applied mutation signature S157E to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of cce4228 wild-type and mutants with different cofactors), NAD+ cofactor block, column head 'Ser157Glu'; printed row 'k catSSA (s-1) c' = 0.58 ± 0.05; printed row 'KNAD+ m (mM) d' = 0.51 ± 0.04; Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.58 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.58 s^(-1). Km: printed Table 1 cell 0.51 mM; already in mM, no unit conversion applies; the paper value is 0.51 mM. kcat/Km: Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column, so the paper value 1.1372549019607843 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.58 / 0.51 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, NAD+ cofactor block, Ser157Glu column: kcat = 0.58 ± 0.05 s-1 (printed row 'k catSSA (s-1) c'); Km = 0.51 ± 0.04 mM (printed row 'KNAD+ m (mM) d'); Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column.


column_label: Table 1 (Kinetic parameters of cce4228 wild-type and mutants with different cofactors), NAD+ cofactor block, wild-type column head 'wild-typee' (the trailing e is Table 1 footnote marker e); printed row 'k catSSA (s-1) c' = 1.74 ± 0.08; printed row 'KNAD+ m (mM) d' = 1.7 ± 0.2; Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.74 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 1.74 s^(-1). Km: printed Table 1 cell 1.7 mM; already in mM, no unit conversion applies; the paper value is 1.7 mM. kcat/Km: Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column, so the paper value 1.0235294117647058 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.74 / 1.7 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, NAD+ cofactor block, wild-type column: kcat = 1.74 ± 0.08 s-1 (printed row 'k catSSA (s-1) c'); Km = 1.7 ± 0.2 mM (printed row 'KNAD+ m (mM) d'); Table 1 prints no kcat/Km cell for the NAD+ substrate axis of this column.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S157E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+


substrate_name: succinate semialdehyde

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K154A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

column_label: PLOS ONE DOI 10.1371/journal.pone.0239372 Table 1; Lys154Ala column; NAD+ block SSA rows KmSSA, kcatSSA, and kcat/KmSSA.

raw_value_unit_evidence: Table 1 Lys154Ala NAD+ block for SSA: KmSSA 0.02 +/- 0.01 mM; kcatSSA 0.13 +/- 0.07 s^-1; kcat/KmSSA 6.5 mM^-1 s^-1.

row_label: Lys154Ala / succinate semialdehyde in NAD+ block

table_label: Table 1. Kinetic parameters of cce4228 wild type and variants


column_label: PLOS ONE DOI 10.1371/journal.pone.0239372 Table 1; Ser157Glu column; NADP+ block SSA rows KmSSA, kcatSSA, and kcat/KmSSA.

raw_value_unit_evidence: Table 1 Ser157Glu NADP+ block for SSA: KmSSA 0.0028 +/- 0.0007 mM; kcatSSA 1.5 +/- 0.1 s^-1; kcat/KmSSA 535 mM^-1 s^-1.

row_label: Ser157Glu / succinate semialdehyde in NADP+ block


column_label: PLOS ONE DOI 10.1371/journal.pone.0239372 Table 1; WT column; NADP+ block SSA rows KmSSA, kcatSSA, and kcat/KmSSA.

raw_value_unit_evidence: Table 1 WT NADP+ block for SSA: KmSSA 0.008 +/- 0.003 mM; kcatSSA 3.9 +/- 0.3 s^-1; kcat/KmSSA 487 mM^-1 s^-1.

row_label: WT / succinate semialdehyde in NADP+ block


enzyme_display_name: Aspartate-semialdehyde dehydrogenase 2

organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

enzyme: Aspartate-semialdehyde dehydrogenase 2


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: Aspartate-semialdehyde dehydrogenase 1

substrate_name: L-aspartate 4-semialdehyde

enzyme: Aspartate-semialdehyde dehydrogenase 1


organism: Vibrio cholerae

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row V. cholerae II; kcat column = 58 s^-1; ASA Km (mM) column = 0.16; ASA kcat/Km (M^-1 s^-1) column = 3.6 x 10^5 (normalized 360 s^-1 mM^-1).

row_label: V. cholerae II / ASA


column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row V. cholerae I; kcat column = 120 s^-1; ASA Km (mM) column = 0.19; ASA kcat/Km (M^-1 s^-1) column = 6.3 x 10^5 (normalized 630 s^-1 mM^-1).

row_label: V. cholerae I / ASA


substrate_name: NADP+

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row V. cholerae II; kcat column = 58 s^-1; NADP Km (mM) column = 0.36; NADP kcat/Km (M^-1 s^-1) column = 1.6 x 10^5 (normalized 160 s^-1 mM^-1).

raw_value_unit_evidence: kcat 58 s^-1; NADP Km 0.36 mM; NADP kcat/Km 1.6 x 10^5 M^-1 s^-1

row_label: V. cholerae II / NADP


column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row V. cholerae I; kcat column = 120 s^-1; NADP Km (mM) column = 0.32; NADP kcat/Km (M^-1 s^-1) column = 3.8 x 10^5 (normalized 380 s^-1 mM^-1).

raw_value_unit_evidence: kcat 120 s^-1; NADP Km 0.32 mM; NADP kcat/Km 3.8 x 10^5 M^-1 s^-1

row_label: V. cholerae I / NADP


substrate_name: Phosphate


column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row V. cholerae I; kcat column = 120 s^-1; Phosphate Km (mM) column = 1.1; Phosphate kcat/Km (M^-1 s^-1) column = 1.1 x 10^5 (normalized 110 s^-1 mM^-1).

raw_value_unit_evidence: kcat 120 s^-1; Phosphate Km 1.1 mM; Phosphate kcat/Km 1.1 x 10^5 M^-1 s^-1

row_label: V. cholerae I / Phosphate


enzyme_display_name: Aldehyde-alcohol dehydrogenase 2

organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)

substrate_name: ethanol

smiles: CCO

assay_conditions_summary: cofactor NAD+

column_label: Km values for acetyl-CoA, acetaldehyde and ethanol were 0.015, 0.15 and 80 mM respectively in the presence of 0.2 mM NAD+.

raw_value_unit_evidence: Km raw_value=80 mM raw_unit=mM

row_label: Prose segment: ethanol Km

table_label: PubMed PMID 7980441 abstract

enzyme: Aldehyde-alcohol dehydrogenase 2

substrate: ethanol


raw_value_unit_evidence: Km raw_value=0.15 mM raw_unit=mM

row_label: Prose segment: acetaldehyde Km


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; cofactor NAD+

column_label: PMCID PMC1137609 scanned page 745, left column, Molecular characterization of EhADH2, K_m values paragraph; acetyl-CoA is listed in the ACDH activity sentence.

raw_value_unit_evidence: Primary paper page 745 reports ACDH K_m 0.015 mM for acetyl-CoA.

row_label: ACDH activity; acetyl-CoA

table_label: Prose: Molecular characterization of EhADH2 / K_m values

substrate: acetyl-CoA


substrate_name: NAD(+) (for ADH activity)

substrate: NAD(+) (for ADH activity)


substrate_name: NADH (for ADH activity)

assay_conditions_summary: cofactor NADH

substrate: NADH (for ADH activity)


substrate_name: L-4-aspartyl phosphate

column_label: Table 1, Enzyme ASD, Km column, ASD / aspp row: 0.022 mM.

normalized_value_unit_evidence: 0.022 mM; already in mM in Table 1.

raw_value_unit_evidence: Table 1 lists ASD aspp Km = 0.022 +/- 0.001 mM; aspp is beta-aspartyl phosphate.

row_label: ASD / aspp row

table_label: Table 1: Kinetic parameters of the threonine-pathway enzymes

substrate: L-4-aspartyl phosphate


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

column_label: Table 1, Enzyme ASD, Km column, ASD / NADPH row: 0.029 mM.

normalized_value_unit_evidence: 0.029 mM; already in mM in Table 1.

raw_value_unit_evidence: Table 1 lists ASD NADPH Km = 0.029 +/- 0.002 mM.

row_label: ASD / NADPH row

substrate: NADPH


column_label: Table 1, Enzyme ASD, Km column, ASD / ASA row: 0.11 mM.

normalized_value_unit_evidence: 0.11 mM; already in mM in Table 1.

raw_value_unit_evidence: Table 1 lists ASD ASA Km = 0.11 +/- 0.008 mM; ASA is D,L-aspartic beta-semialdehyde.

row_label: ASD / ASA row

substrate: L-aspartate 4-semialdehyde


assay_conditions_summary: cofactor NADP+

column_label: Table 1, Enzyme ASD, Km column, ASD / NADP+ row: 0.144 mM.

normalized_value_unit_evidence: 0.144 mM; already in mM in Table 1.

raw_value_unit_evidence: Table 1 lists ASD NADP+ Km = 0.144 +/- 0.02 mM.

row_label: ASD / NADP+ row


column_label: Table 1, Enzyme ASD, Km column, ASD / Pi row: 10.2 mM.

normalized_value_unit_evidence: 10.2 mM; already in mM in Table 1.

raw_value_unit_evidence: Table 1 lists ASD Pi Km = 10.2 +/- 1.4 mM.

row_label: ASD / Pi row


enzyme_display_name: UniProt P44801

organism: Haemophilus influenzae

source_db: skid

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row Ha. influenzae; kcat column = 330 s^-1; Phosphate Km (mM) column = 1.6; Phosphate kcat/Km (M^-1 s^-1) column = 2.1 x 10^5 (normalized 210 s^-1 mM^-1).

raw_value_unit_evidence: kcat 330 s^-1; Phosphate Km 1.6 mM; Phosphate kcat/Km 2.1 x 10^5 M^-1 s^-1

row_label: Ha. influenzae / Phosphate

source_databases_merged: skid uniprot

enzyme: UniProt P44801

source: skid


substrate_name: L-Aspartate 4-semialdehyde

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row Ha. influenzae; kcat column = 330 s^-1; ASA Km (mM) column = 0.24; ASA kcat/Km (M^-1 s^-1) column = 1.4 x 10^6 (normalized 1400 s^-1 mM^-1).

row_label: Ha. influenzae / ASA

substrate: L-Aspartate 4-semialdehyde


column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row Ha. influenzae; kcat column = 330 s^-1; NADP Km (mM) column = 0.15; NADP kcat/Km (M^-1 s^-1) column = 2.2 x 10^6 (normalized 2200 s^-1 mM^-1).

raw_value_unit_evidence: kcat 330 s^-1; NADP Km 0.15 mM; NADP kcat/Km 2.2 x 10^6 M^-1 s^-1

row_label: Ha. influenzae / NADP

substrate: NADP+


table_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases

substrate: Phosphate


organism: Haloarcula vallismortis

substrate_name: D-glyceraldehyde 3-phosphate

sequence: KVLISAPPKGDEPVKKILTWYDNEYGFSNRMLDVAEYIT

wild_type_sequence: KVLISAPPKGDEPVKKILTWYDNEYGFSNRMLDVAEYIT

assay_conditions_summary: pH 7.8; cofactor NAD+

substrate: D-glyceraldehyde 3-phosphate


substrate_name: NAD+

substrate: NAD+


substrate_name: arsenate

substrate: arsenate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q350N with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q350N/H171A to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt P9WNX5

organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 9; 303.15 K; cofactor NADPH

column_label: OUP full text Table 1 row Pi reports Km (mM)=11.39.

raw_value_unit_evidence: Table 1 row Pi reports Km raw_value=11.39 raw_unit=mM.

row_label: Pi

table_label: Table 1: Apparent kinetic parameters of purified recombinant ASD of Mycobacterium tuberculosis H37Rv

enzyme: UniProt P9WNX5


column_label: Primary OUP full-text Table 1 row L-ASA; columns Km (mM) and Kcat/Km (M^-1 s^-1); exact printed cells 0.955 and 8.89 x 10^3, respectively.

raw_value_unit_evidence: Table 1 row L-ASA reports Km=0.955 mM and an explicit kcat/Km=8.89 x 10^3 M^-1 s^-1; the article reports turnover number kcat=8.49 s^-1.

row_label: L-ASA


column_label: Primary OUP full-text Table 1 row NADP; columns Km (mM) and Kcat/Km (M^-1 s^-1); exact printed cells 0.065 and 1.31 x 10^5, respectively.

raw_value_unit_evidence: Table 1 row NADP reports Km=0.065 mM and an explicit kcat/Km=1.31 x 10^5 M^-1 s^-1; the article reports turnover number kcat=8.49 s^-1.

row_label: NADP


column_label: Primary OUP full-text Table 1 row Pi; columns Km (mM) and Kcat/Km (M^-1 s^-1); exact printed cells 11.39 and 7.45 x 10^2, respectively.

raw_value_unit_evidence: Table 1 row Pi reports Km=11.39 mM and an explicit kcat/Km=7.45 x 10^2 M^-1 s^-1; the article reports turnover number kcat=8.49 s^-1.


enzyme_display_name: UniProt B2HN69

organism: Mycobacterium marinum

source_license: CC BY-NC-ND 4.0

enzyme: UniProt B2HN69


substrate_name: ATP

substrate: ATP


substrate_name: benzoic acid

substrate: benzoic acid


organism: Candida maltosa


substrate_name: alpha-aminoadipate

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

substrate: alpha-aminoadipate


substrate_name: NADH

substrate: NADH


organism: Acanthopagrus schlegelii

substrate_name: acetaldehyde

sequence: SGLLINQPKYSWLKELGL

wild_type_sequence: SGLLINQPKYSWLKELGL

substrate: acetaldehyde


substrate_name: D-Glyceraldehyde 3-phosphate

substrate: D-Glyceraldehyde 3-phosphate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +10, so it is treated as a source-provided variant sequence.

proof_lines: Two single [Gly317] and [Ala317] GAPDH mutants... were constructed.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 8.9; 295.15 K; cofactor NAD+

proof_lines: the role of the invariant Asn 313 residue... was examined.


sequence_variant_note: Mutation signature Y317G matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: dissociation constant for NAD+ is 13 times higher


substrate_name: Phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N313T/Y317G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: dissociation constant for NAD+ is 300 times higher


organism: Geobacillus stearothermophilus

sequence_variant_note: Mutation signature D32A/L187N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NADP+


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+


substrate_name: NADP+


column_label: Table II row Wild-type B. stearothermophilus GAPDH / D-Glyceraldehyde 3-phosphate (GAPDH activity): kcat cell 76 s^-1; KM cell 0.9 mM; no kcat/KM column/cell is printed, so kcat_over_km 84.44444444444444 s^-1 mM^-1 is the quotient 76 / 0.9 of the two printed cells.

normalized_value_unit_evidence: kcat 76 s^-1; Km 0.9 mM; kcat/Km derived as 76 / 0.9 = 84.44444444444444 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type B. stearothermophilus GAPDH / D-Glyceraldehyde 3-phosphate (GAPDH activity): kcat=76 s^-1; km=0.9 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type B. stearothermophilus GAPDH | D-Glyceraldehyde 3-phosphate (GAPDH activity)


substrate_name: Glycerate 1,3-bisphosphate

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7 for the reverse reaction; cofactor NADH

column_label: Results section, reverse-direction paragraph of JBC 1997, 272(24):15106-15112 (reverse reaction with 1,3-dPG); Results prose, reverse direction with 1,3-dPG, GAPDH of B. stearothermophilus; the kcat value 65 s-1 comes from the reverse-reaction turnover number stated in the Results prose and the Michaelis constant 0.005 mM comes from the reverse-reaction Michaelis constant for 1,3-dPG stated in the Results prose. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 65 s-1; already in s^-1, no conversion (this article prints no min^-1 kinetic value); the paper value is 65.0 s^(-1). Km: printed cell 0.005 mM; already in mM, no conversion; the paper value is 0.005 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 13000.0 s^(-1)*mM^(-1) is not a printed value; it is the quotient 65 / 0.005 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Results prose, reverse direction with 1,3-dPG, GAPDH of B. stearothermophilus: kcat = 65 s-1 (printed column the reverse-reaction turnover number stated in the Results prose); Km = 0.005 mM (printed column the reverse-reaction Michaelis constant for 1,3-dPG stated in the Results prose). No kcat/Km value is printed for this measurement.

substrate: Glycerate 1,3-bisphosphate


assay_conditions_summary: pH 8.9; 298.15 K; cofactor NAD+

column_label: Table II row Wild-type B. stearothermophilus GAPDH / NAD+ (GAPDH activity): kcat cell 76 s^-1; KM cell 0.09 mM; no kcat/KM column/cell is printed, so kcat_over_km 844.4444444444445 s^-1 mM^-1 is the quotient 76 / 0.09 of the two printed cells.

normalized_value_unit_evidence: kcat 76 s^-1; Km 0.09 mM; kcat/Km derived as 76 / 0.09 = 844.4444444444445 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type B. stearothermophilus GAPDH / NAD+ (GAPDH activity): kcat=76 s^-1; km=0.09 mM; kcat_over_km=not explicitly reported.

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


column_label: Results main text, JBC page 15110, paragraph on the reverse direction with 1,3-dPG as substrate; Wild-type B. stearothermophilus GAPDH / NADH (reverse reaction with 1,3-dPG): kcat 65 s^-1; KM 0.011 mM; no kcat/KM value is printed, so kcat_over_km 5909.090909090909 s^-1 mM^-1 is the quotient 65 / 0.011 of the two printed prose values.

normalized_value_unit_evidence: kcat 65 s^-1; Km 0.011 mM; kcat/Km derived as 65 / 0.011 = 5909.090909090909 s^-1 mM^-1 from the two printed prose values; the paper prints no kcat/KM value.

raw_value_unit_evidence: Results main text, JBC page 15110, paragraph on the reverse direction with 1,3-dPG as substrate; Wild-type B. stearothermophilus GAPDH / NADH (reverse reaction with 1,3-dPG): kcat=65 s^-1; km=0.011 mM; kcat_over_km=5909.090909090909 s^-1 mM^-1 derived as the quotient 65 / 0.011 s^-1 / mM; no kcat/KM value is printed in the paper.


enzyme_display_name: Glyceraldehyde-3-phosphate dehydrogenase 1, cytosolic

organism: Oryza sativa subsp. japonica


substrate_name: NAD(+)

enzyme: Glyceraldehyde-3-phosphate dehydrogenase 1, cytosolic

substrate: NAD(+)


substrate_name: 3-phospho-D-glyceroyl phosphate

substrate: 3-phospho-D-glyceroyl phosphate


organism: Saccharomyces cerevisiae

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

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Kinetic constants paragraph; TPNH row/term; K = 8.3 x 10^-5 M.

raw_value_unit_evidence: Kinetic constants paragraph reports K for TPNH 8.3 x 10^-5 M; summary repeats TPNH 8.3 x 10^-5.

row_label: TPNH

table_label: Kinetic constants paragraph and summary for aspartic beta-semialdehyde dehydrogenase

substrate: NADPH


substrate_name: L-4-aspartyl phosphate

column_label: Kinetic constants paragraph; BAP row/term; K = 1.6 x 10^-4 M.

raw_value_unit_evidence: Kinetic constants paragraph reports K for BAP 1.6 x 10^-4 M; summary repeats BAP 1.6 x 10^-4.

row_label: BAP

substrate: L-4-aspartyl phosphate


substrate_name: L-aspartate 4-semialdehyde

assay_conditions_summary: pH 9; cofactor NADPH

column_label: Kinetic constants paragraph; ASA row/term; K = 2.6 x 10^-3 M.

raw_value_unit_evidence: Kinetic constants paragraph reports K values for ASA, TPN, and phosphate are respectively 2.6 x 10^-3 M, 3.6 x 10^-5 M, and 1.4 x 10^-3 M; summary repeats ASA 2.6 x 10^-3.

row_label: ASA

substrate: L-aspartate 4-semialdehyde


substrate_name: 3-Phospho-D-glyceroyl phosphate

substrate: 3-Phospho-D-glyceroyl phosphate


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

column_label: Table 2; reaction TDH; isoenzyme Tdh2p; parameter kcat value 8.63 s^-1; parameter Kgap value 0.77 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=8.63 normalized_unit=s^-1; Km normalized_value=0.77 normalized_unit=mM; kcat/Km normalized_value=11.207792207792208 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=8.63 raw_unit=s^-1; Km raw_value=0.77 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 8.63/0.77 raw_unit=s^-1*mM^-1

row_label: TDH / Tdh2p / Kgap

table_label: Table 2. Enzyme kinetics parameters determined in this project and contrasted with those of [23].


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S22Q/P24K to reconstruct the assayed variant sequence.

column_label: Table 2; reaction TDH; isoenzyme Tdh3p; parameter kcat value 18.2 s^-1; parameter Kgap value 0.423 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=18.2 normalized_unit=s^-1; Km normalized_value=0.423 normalized_unit=mM; kcat/Km normalized_value=43.026004728132385 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=18.2 raw_unit=s^-1; Km raw_value=0.423 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 18.2/0.423 raw_unit=s^-1*mM^-1

row_label: TDH / Tdh3p / Kgap


column_label: Table 2; reaction TDH; isoenzyme Tdh1p; parameter kcat value 19.1 s^-1; parameter Kgap value 0.495 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=19.1 normalized_unit=s^-1; Km normalized_value=0.495 normalized_unit=mM; kcat/Km normalized_value=38.58585858585859 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=19.1 raw_unit=s^-1; Km raw_value=0.495 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 19.1/0.495 raw_unit=s^-1*mM^-1

row_label: TDH / Tdh1p / Kgap


enzyme_display_name: carboxylate reductase (NADP+)

organism: Tsukamurella paurometabola

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

enzyme: carboxylate reductase (NADP+)


substrate_name: octadecanoate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: octadecanoate


substrate_name: Butanoate

smiles: CCCC(=O)[O-]

substrate: Butanoate


organism: Homo sapiens

substrate_name: Coenzyme A; alpha-Ketovaline; NAD+

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

substrate: Coenzyme A; alpha-Ketovaline; NAD+


substrate_name: alpha-Ketovaline; Coenzyme A; NAD+

substrate: alpha-Ketovaline; Coenzyme A; NAD+


enzyme_display_name: branched-chain alpha-keto acid dehydrogenase system

substrate_name: alpha-Ketovaline

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

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

substrate: alpha-Ketovaline


enzyme: branched-chain alpha-keto acid dehydrogenase system


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


substrate_name: L-2-Aminoadipate; H+; NADPH

substrate: L-2-Aminoadipate; H+; NADPH


substrate_name: NADPH

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; 310.15 K; cofactor NADPH


enzyme_display_name: benzaldehyde dehydrogenase (NAD+)

organism: Acinetobacter calcoaceticus

enzyme: benzaldehyde dehydrogenase (NAD+)


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Pseudomonas aeruginosa

substrate_name: L-Aspartate 4-semialdehyde

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row P. aeruginosa; kcat column = 160 s^-1; ASA Km (mM) column = 0.12; ASA kcat/Km (M^-1 s^-1) column = 1.3 x 10^6 (normalized 1300 s^-1 mM^-1).

row_label: P. aeruginosa / ASA

substrate: L-Aspartate 4-semialdehyde


substrate_name: NADP+

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row P. aeruginosa; kcat column = 160 s^-1; NADP Km (mM) column = 0.13; NADP kcat/Km (M^-1 s^-1) column = 1.6 x 10^6 (normalized 1600 s^-1 mM^-1).

raw_value_unit_evidence: kcat 160 s^-1; NADP Km 0.13 mM; NADP kcat/Km 1.6 x 10^6 M^-1 s^-1

row_label: P. aeruginosa / NADP

substrate: NADP+


substrate_name: Phosphate

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row P. aeruginosa; kcat column = 160 s^-1; Phosphate Km (mM) column = 1.5; Phosphate kcat/Km (M^-1 s^-1) column = 1.1 x 10^5 (normalized 110 s^-1 mM^-1).

raw_value_unit_evidence: kcat 160 s^-1; Phosphate Km 1.5 mM; Phosphate kcat/Km 1.1 x 10^5 M^-1 s^-1

row_label: P. aeruginosa / Phosphate

substrate: Phosphate


substrate_name: perillaldehyde

substrate: perillaldehyde


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


smiles: CCCCCCCC=O


smiles: CCCCCC=O


km_display: Not reported


assay_conditions_summary: pH 7.8; cofactor NADPH

column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups row tpCAR (Tsukamurella paurometabola), substrate column 4-Nitrobenzoic acid (6), metric row k cat [min^-1], raw cell 13+/-1, normalized 0.216666666666666666666666666667 s^-1; Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups row tpCAR (Tsukamurella paurometabola), substrate column 4-Nitrobenzoic acid (6), metric row k cat/K_m [min^-1 mM^-1], raw cell 22+/-6, normalized 0.366666666666666666666666666667 s^-1*mM^-1; Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups row tpCAR (Tsukamurella paurometabola), substrate column 4-Nitrobenzoic acid (6), metric row K_m [mM], raw cell 0.6+/-0.1, normalized 0.6 mM

normalized_value_unit_evidence: kcat normalized_value=0.216666666666666666666666666667 normalized_unit=s^-1; kcat/Km normalized_value=0.366666666666666666666666666667 normalized_unit=s^-1*mM^-1; Km normalized_value=0.6 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=13 raw_unit=min^-1 raw_cell=13+/-1; kcat/Km raw_value=22 raw_unit=min^-1*mM^-1 raw_cell=22+/-6; Km raw_value=0.6 raw_unit=mM raw_cell=0.6+/-0.1

row_label: tpCAR (Tsukamurella paurometabola) / 4-Nitrobenzoic acid (6)


substrate_name: benzoate

column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row tpCAR (Tsukamurella paurometabola) / Benzoic acid (1); kcat column kcat [min^-1] raw 142+/-3; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 72+/-6; Km column Km [mM] raw 2.0+/-0.1

normalized_value_unit_evidence: kcat normalized_value=2.37 normalized_unit=s^-1 from 142+/-3 / 60; kcat/Km normalized_value=1.185 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=72+/-6 min^-1 mM^-1; Km normalized_value=2.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=142+/-3 raw_unit=min^-1; kcat/Km raw_value=72+/-6 raw_unit=min^-1 mM^-1; Km raw_value=2.0+/-0.1 raw_unit=mM

substrate: benzoate


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row tpCAR (Tsukamurella paurometabola) / 4-Methylbenzoic acid (2); kcat column kcat [min^-1] raw 152+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 220+/-10; Km column Km [mM] raw 0.69+/-0.03

normalized_value_unit_evidence: kcat normalized_value=2.53 normalized_unit=s^-1 from 152+/-2 / 60; kcat/Km normalized_value=3.6666666666666665 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=220+/-10 min^-1 mM^-1; Km normalized_value=0.69 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=152+/-2 raw_unit=min^-1; kcat/Km raw_value=220+/-10 raw_unit=min^-1 mM^-1; Km raw_value=0.69+/-0.03 raw_unit=mM


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)[O-]

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row tpCAR (Tsukamurella paurometabola) / Dodecanoic acid (20); kcat column kcat [min^-1] raw 157+/-5; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 3600+/-400; Km column Km [mM] raw 0.04+/-0.01

normalized_value_unit_evidence: kcat normalized_value=2.62 normalized_unit=s^-1 from 157+/-5 / 60; kcat/Km normalized_value=65.5 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=3600+/-400 min^-1 mM^-1; Km normalized_value=0.04 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=157+/-5 raw_unit=min^-1; kcat/Km raw_value=3600+/-400 raw_unit=min^-1 mM^-1; Km raw_value=0.04+/-0.01 raw_unit=mM

substrate: dodecanoate


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row tpCAR (Tsukamurella paurometabola) / 3-Phenylpropionic acid (9); kcat column kcat [min^-1] raw 158+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 500+/-20; Km column Km [mM] raw 0.32+/-0.01

normalized_value_unit_evidence: kcat normalized_value=2.63 normalized_unit=s^-1 from 158+/-2 / 60; kcat/Km normalized_value=8.21875 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=500+/-20 min^-1 mM^-1; Km normalized_value=0.32 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=158+/-2 raw_unit=min^-1; kcat/Km raw_value=500+/-20 raw_unit=min^-1 mM^-1; Km raw_value=0.32+/-0.01 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row tpCAR (Tsukamurella paurometabola) / 3-Methoxybenzoic acid (4); kcat column kcat [min^-1] raw 186+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 334+/-10; Km column Km [mM] raw 0.56+/-0.02

normalized_value_unit_evidence: kcat normalized_value=3.1 normalized_unit=s^-1 from 186+/-2 / 60; kcat/Km normalized_value=5.535714285714286 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=334+/-10 min^-1 mM^-1; Km normalized_value=0.56 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=186+/-2 raw_unit=min^-1; kcat/Km raw_value=334+/-10 raw_unit=min^-1 mM^-1; Km raw_value=0.56+/-0.02 raw_unit=mM


substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row tpCAR (Tsukamurella paurometabola) / Octanoic acid (19); kcat column kcat [min^-1] raw 219+/-3; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 1140+/-50; Km column Km [mM] raw 0.2+/-0.01

normalized_value_unit_evidence: kcat normalized_value=3.65 normalized_unit=s^-1 from 219+/-3 / 60; kcat/Km normalized_value=18.25 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1140+/-50 min^-1 mM^-1; Km normalized_value=0.2 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=219+/-3 raw_unit=min^-1; kcat/Km raw_value=1140+/-50 raw_unit=min^-1 mM^-1; Km raw_value=0.2+/-0.01 raw_unit=mM

substrate: Octanoate


organism: Nocardia otitidiscaviarum

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row noCAR (Nocardia otitidiscaviarum) / Octanoic acid (19); kcat column kcat [min^-1] raw 141+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 750+/-30; Km column Km [mM] raw 0.2+/-0.01

normalized_value_unit_evidence: kcat normalized_value=2.35 normalized_unit=s^-1 from 141+/-2 / 60; kcat/Km normalized_value=11.75 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=750+/-30 min^-1 mM^-1; Km normalized_value=0.2 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=141+/-2 raw_unit=min^-1; kcat/Km raw_value=750+/-30 raw_unit=min^-1 mM^-1; Km raw_value=0.2+/-0.01 raw_unit=mM


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row noCAR (Nocardia otitidiscaviarum) / Butanoic acid (18); kcat column kcat [min^-1] raw 170+/-20*; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 3.4+/-0.7*; Km column Km [mM] raw 50+/-8*

normalized_value_unit_evidence: kcat normalized_value=2.83 normalized_unit=s^-1 from 170+/-20* / 60; kcat/Km normalized_value=0.056600000000000004 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=3.4+/-0.7* min^-1 mM^-1; Km normalized_value=50.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=170+/-20* raw_unit=min^-1; kcat/Km raw_value=3.4+/-0.7* raw_unit=min^-1 mM^-1; Km raw_value=50+/-8* raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row noCAR (Nocardia otitidiscaviarum) / Benzoic acid (1); kcat column kcat [min^-1] raw 183+/-6; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 89.1+/-8; Km column Km [mM] raw 2.1+/-0.2

normalized_value_unit_evidence: kcat normalized_value=3.05 normalized_unit=s^-1 from 183+/-6 / 60; kcat/Km normalized_value=1.4523809523809523 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=89.1+/-8 min^-1 mM^-1; Km normalized_value=2.1 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=183+/-6 raw_unit=min^-1; kcat/Km raw_value=89.1+/-8 raw_unit=min^-1 mM^-1; Km raw_value=2.1+/-0.2 raw_unit=mM


organism: Mycolicibacterium phlei

substrate_name: octadecanoate


assay_conditions_summary: pH 7.3; 303.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication, versus ATP


assay_conditions_summary: pH 7.3; cofactor NADPH

column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row mpCAR (Mycobacterium phlei) / Benzoic acid (1); kcat column kcat [min^-1] raw 140+/-20*; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 7+/-1*; Km column Km [mM] raw 20+/-4*

normalized_value_unit_evidence: kcat normalized_value=2.33 normalized_unit=s^-1 from 140+/-20* / 60; kcat/Km normalized_value=0.1165 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=7+/-1* min^-1 mM^-1; Km normalized_value=20.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=140+/-20* raw_unit=min^-1; kcat/Km raw_value=7+/-1* raw_unit=min^-1 mM^-1; Km raw_value=20+/-4* raw_unit=mM


organism: Mycolicibacterium smegmatis

column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row msCAR (Mycobacterium smegmatis) / 3-Phenylpropionic acid (9); kcat column kcat [min^-1] raw 184+/-9; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 1200+/-200; Km column Km [mM] raw 0.16+/-0.02

normalized_value_unit_evidence: kcat normalized_value=3.07 normalized_unit=s^-1 from 184+/-9 / 60; kcat/Km normalized_value=19.1875 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1200+/-200 min^-1 mM^-1; Km normalized_value=0.16 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=184+/-9 raw_unit=min^-1; kcat/Km raw_value=1200+/-200 raw_unit=min^-1 mM^-1; Km raw_value=0.16+/-0.02 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row msCAR (Mycobacterium smegmatis) / Benzoic acid (1); kcat column kcat [min^-1] raw 197+/-4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 57+/-4; Km column Km [mM] raw 3.4+/-0.2

normalized_value_unit_evidence: kcat normalized_value=3.28 normalized_unit=s^-1 from 197+/-4 / 60; kcat/Km normalized_value=0.9647058823529412 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=57+/-4 min^-1 mM^-1; Km normalized_value=3.4 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=197+/-4 raw_unit=min^-1; kcat/Km raw_value=57+/-4 raw_unit=min^-1 mM^-1; Km raw_value=3.4+/-0.2 raw_unit=mM


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row msCAR (Mycobacterium smegmatis) / Octanoic acid (19); kcat column kcat [min^-1] raw 296+/-8; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 3000+/-300; Km column Km [mM] raw 0.1+/-0.01

normalized_value_unit_evidence: kcat normalized_value=4.93 normalized_unit=s^-1 from 296+/-8 / 60; kcat/Km normalized_value=49.3 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=3000+/-300 min^-1 mM^-1; Km normalized_value=0.1 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=296+/-8 raw_unit=min^-1; kcat/Km raw_value=3000+/-300 raw_unit=min^-1 mM^-1; Km raw_value=0.1+/-0.01 raw_unit=mM


organism: Nocadia sp.

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: (R)-ibuprofen

substrate: (R)-ibuprofen


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: Unknown

ki_unit: mM

substrate: Unknown