enzyme_display_name: pyranose dehydrogenase (acceptor)

organism: Agaricus campestris

substrate_name: ferrocenium ion

column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `Fc+PF6 (pH 8.5)` the AcPDH group prints Km 1.19, kcat 19.92 and kcat/Km 16.7.

normalized_value_unit_evidence: kcat: printed Table 4 cell 19.92 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 19.92 s^(-1). Km: printed cell 1.19 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 1.19 mM. kcat/Km: printed cell 16.7 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 16.7 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 19.92 / 1.19 = 16.73949579831933 s^-1 mM^-1, against the printed efficiency cell 16.7.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `Fc+PF6 (pH 8.5)`, AcPDH column group: Km = 1.19 mM; kcat = 19.92 s-1; kcat/Km = 16.7 mM-1 s-1.

row_label: Table 4, substrate row `Fc+PF6 (pH 8.5)`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)

table_label: Table 4: Apparent kinetic constants for selected electron acceptors determined at 30 °C with 25 mM D-glucose as the electron donor. (Biomolecules 2013, 3(3):535-552)

enzyme: pyranose dehydrogenase (acceptor)

substrate: ferrocenium ion


organism: Agaricus xanthodermus

source_db: brenda

verification_status: corrected

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_source: multiple

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

column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `Fc+PF6 (pH 8.5)` the AxPDH group prints Km 0.03, kcat 22.07 and kcat/Km 735.7.

normalized_value_unit_evidence: kcat: printed Table 4 cell 22.07 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 22.07 s^(-1). Km: printed cell 0.03 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.03 mM. kcat/Km: printed cell 735.7 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 735.7 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 22.07 / 0.03 = 735.6666666666667 s^-1 mM^-1, against the printed efficiency cell 735.7.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `Fc+PF6 (pH 8.5)`, AxPDH column group: Km = 0.03 mM; kcat = 22.07 s-1; kcat/Km = 735.7 mM-1 s-1.

row_label: Table 4, substrate row `Fc+PF6 (pH 8.5)`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)

source_databases_merged: brenda uniprot

status: corrected

source: brenda


enzyme_display_name: UniProt Q3L245

organism: Leucoagaricus meleagris

substrate_name: ferricenium ion

source_db: skid

verification_status: unverified

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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=30°C, pH=4
Raw SKiD Env: Temp=30°C, pH=7.5

source_databases_merged: skid uniprot

enzyme: UniProt Q3L245

substrate: ferricenium ion

status: unverified

source: skid


enzyme_display_name: Pyranose dehydrogenase

organism: Agaricus bisporus

substrate_name: Unknown

source_db: uniprot

kcat_display: Not reported

km_display: Not reported

enzyme: Pyranose dehydrogenase

substrate: Unknown

source: uniprot


enzyme_display_name: (S)-mandelate dehydrogenase

organism: Pseudomonas putida

substrate_name: (S)-Mandelate; Riboflavin-5-phosphate

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

assay_conditions_summary: pH 7.5; 293.15 K; buffer 0.1 M potassium phosphate; cofactor FMN

proof_lines: in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C

source_databases_merged: sabio_rk brenda skid uniprot

enzyme: (S)-mandelate dehydrogenase

substrate: (S)-Mandelate; Riboflavin-5-phosphate


substrate_name: (R,S)-p-chloromandelate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H274G to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant enzyme H274G, in presence of 20 mM imidazole

substrate: (R,S)-p-chloromandelate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 20°C, mutant enzyme G81A
mutant G81A
mutant G81A of chimera MDH-GOX2


substrate_name: ethyl-(S)-mandelate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R277G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5

substrate: ethyl-(S)-mandelate


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

proof_lines: pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach

proof_lines: pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach


proof_lines: wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5


substrate_name: methyl-(S)-mandelate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R277K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5

substrate: methyl-(S)-mandelate


organism: Rhodotorula graminis

proof_lines: pH 7.5, 25°C, cosubstrate ferricyanide, LMDH holoenzyme

proof_lines: pH 7.5, 25°C, cosubstrate cytochrome, LMDH holoenzyme


ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165K/R277K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165G/R277K to reconstruct the assayed variant sequence.


smiles: CCOC(=O)C(C#C)O

assay_conditions_summary: pH 7.5; buffer 0.1 M potassium phosphate

data_origin: experimental


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165G to reconstruct the assayed variant sequence.


enzyme_display_name: soluble quinoprotein glucose dehydrogenase

organism: Acinetobacter calcoaceticus

substrate_name: D-Lyxose

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

proof_lines: stopped-flow measurement of reductive half-reaction, 15°C

substrate: D-Lyxose


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

enzyme: soluble quinoprotein glucose dehydrogenase


substrate_name: melibiose

mutation_signature: stopped-flow measurement of reductive half-reaction

substrate: melibiose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-fucose

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

substrate: D-fucose


substrate_name: lactose

substrate: lactose


enzyme_display_name: NDMA-dependent alcohol dehydrogenase

organism: Rhodococcus erythropolis

substrate_name: N,N-Dimethyl-4-nitrosoaniline; Ethanol

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

sequence: MKTKAAVLFETHKPFEIVELEL

wild_type_sequence: MKTKAAVLFETHKPFEIVELEL

proof_lines: The lower limit of the determination of KM with NDMA as electron acceptor was 0.001 mM. KM was even lower for hexan-1-ol, pentan-1-ol, and citronellol.

enzyme: NDMA-dependent alcohol dehydrogenase

substrate: N,N-Dimethyl-4-nitrosoaniline; Ethanol


enzyme_display_name: alcohol dehydrogenase (nicotinoprotein)

organism: Amycolatopsis methanolica

proof_lines: uncompetitive inhibition term reflecting binding to the enzyme containing the oxidized coenzyme

proof_lines: competitive inhibition term with respect to NDMA

enzyme: alcohol dehydrogenase (nicotinoprotein)


organism: Niallia circulans

substrate_name: DOIA

proof_lines: Kinetic parameter was determined with saturating SAM. DOIA displays substrate inhibition.

substrate: DOIA


organism: Homo sapiens


enzyme_display_name: D-2-hydroxyglutarate dehydrogenase

organism: Escherichia coli (strain K12)

enzyme: D-2-hydroxyglutarate dehydrogenase


organism: Stutzerimonas stutzeri (strain A1501)

substrate_name: electron transfer flavoprotein (at pH 7.4 and 37 degrees Celsius)

proof_lines: kcat is 7.9 sec(-1) with D-2-hydroxyglutarate as substrate and DCIP as the electron acceptor (at pH 7.4 and 37 degrees Celsius). kcat is 13.0 sec(-1) with D-2-hydroxyglutarate as substrate and electron transfer flavoprotein (ETF) as the ele


organism: Pantoea ananatis (strain AJ13355)


enzyme_display_name: aldehyde dehydrogenase (NAD+)

organism: Rattus norvegicus

substrate_name: H2O; Propanal; NAD+

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

assay_conditions_summary: cofactor NAD+

enzyme: aldehyde dehydrogenase (NAD+)

substrate: H2O; Propanal; NAD+


substrate_name: NAD+; H2O; Propanal

assay_conditions_summary: pH 7.5; 310.15 K; buffer 0.1 M sodium diphosphate; cofactor NAD+

proof_lines: isoform ALDH2, in 0.1 M sodium diphosphate buffer (pH 9.5), at 21-23°C

unit: lgwedgeoneswedgeone

substrate: NAD+; H2O; Propanal


substrate_name: NAD+; H2O; 20-CHO-Leukotriene B4

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

substrate: NAD+; H2O; 20-CHO-Leukotriene B4


substrate_name: H2O; NAD+; Citral

substrate: H2O; NAD+; Citral


substrate_name: NAD+; Glycolaldehyde; H2O

substrate: NAD+; Glycolaldehyde; H2O


substrate_name: H2O; Formaldehyde; NAD+

substrate: H2O; Formaldehyde; NAD+


substrate_name: H2O; NAD+; Betaine aldehyde

substrate: H2O; NAD+; Betaine aldehyde


substrate_name: 4-Carboxybenzaldehyde; H2O; NAD+

substrate: 4-Carboxybenzaldehyde; H2O; NAD+


substrate_name: NADP+; Benzaldehyde; H2O

assay_conditions_summary: cofactor NADP+

substrate: NADP+; Benzaldehyde; H2O


organism: Mesocricetus auratus

substrate_name: H2O; Acetaldehyde; NAD+

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

substrate: H2O; Acetaldehyde; NAD+


organism: Equus caballus

substrate_name: 3-Methylbutanal; H2O; NAD+

substrate: 3-Methylbutanal; H2O; NAD+


organism: Mus musculus

substrate_name: NAD+; H2O; Acetaldehyde

substrate: NAD+; H2O; Acetaldehyde


substrate_name: H2O; NAD+; Acetaldehyde

substrate: H2O; NAD+; Acetaldehyde


organism: Bos taurus

substrate_name: H2O; NAD+; D-Glyceraldehyde

substrate: H2O; NAD+; D-Glyceraldehyde


substrate_name: Propanal; H2O; NAD+

substrate: Propanal; H2O; NAD+


organism: Bacillus subtilis

substrate_name: 2,5-Dioxopentanoate; NAD+; H2O

substrate: 2,5-Dioxopentanoate; NAD+; H2O


organism: Arthrobacter nicotinovorans

substrate_name: H2O; NAD+; Butanal

substrate: H2O; NAD+; Butanal


substrate_name: Benzaldehyde; NAD+; H2O

substrate: Benzaldehyde; NAD+; H2O


substrate_name: H2O; Nonanal; NAD+

substrate: H2O; Nonanal; NAD+


organism: Cupriavidus necator

substrate_name: NADH; H+; Dimethylglyoxal

assay_conditions_summary: cofactor NADH

substrate: NADH; H+; Dimethylglyoxal


organism: Loktanella sp.

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


enzyme_display_name: UniProt Q92UV7

organism: Sinorhizobium meliloti

substrate_name: 3-oxopropyl phosphonate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q92UV7

substrate: 3-oxopropyl phosphonate


enzyme_display_name: Aldehyde dehydrogenase 1A1

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

enzyme: Aldehyde dehydrogenase 1A1


enzyme_display_name: Aldehyde dehydrogenase family 3 member I1, chloroplastic

organism: Arabidopsis thaliana


enzyme_display_name: Aldehyde dehydrogenase family 3 member H1


organism: Macaca fascicularis

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


organism: Oryctolagus cuniculus


organism: Antirrhinum majus

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


enzyme_display_name: Aldehyde dehydrogenase

organism: Craterostigma plantagineum

enzyme: Aldehyde dehydrogenase


enzyme_display_name: aldehyde dehydrogenase (NADP+)

organism: Escherichia coli

substrate_name: H2O; Acetaldehyde; NADP+

enzyme: aldehyde dehydrogenase (NADP+)

substrate: H2O; Acetaldehyde; NADP+


organism: Thermoplasma acidophilum

substrate_name: Glyceraldehyde; NADP+; H2O

substrate: Glyceraldehyde; NADP+; H2O


substrate_name: Butanal; NADP+; H2O

substrate: Butanal; NADP+; H2O


organism: Saccharomyces cerevisiae

substrate_name: NADP+; H2O; Propanal

substrate: NADP+; H2O; Propanal


organism: Acinetobacter calcoaceticus


organism: Acetobacter pasteurianus


enzyme_display_name: Aldehyde dehydrogenase 5, mitochondrial

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Aldehyde dehydrogenase 5, mitochondrial


enzyme_display_name: aldehyde dehydrogenase [NAD(P)+]

organism: Homo sapiens

substrate_name: Benzaldehyde; H2O; NAD+

enzyme: aldehyde dehydrogenase [NAD(P)+]

substrate: Benzaldehyde; H2O; NAD+


organism: Rattus norvegicus

substrate_name: Propanal; NAD+; H2O

substrate: Propanal; NAD+; H2O


organism: Mus musculus

substrate_name: H2O; all-trans-Retinal; NAD+

substrate: H2O; all-trans-Retinal; NAD+


substrate_name: NADP+; Propanal; H2O

substrate: NADP+; Propanal; H2O


enzyme_display_name: Aldehyde dehydrogenase family 3 member B1


enzyme_display_name: NADP/NAD-dependent aldehyde dehydrogenase PuuC

organism: Escherichia coli (strain K12)


enzyme_display_name: Aldehyde dehydrogenase 1

organism: Tanacetum cinerariifolium

substrate_name: trans-chrysanthemal (in the presence of NAD(+))

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

enzyme: Aldehyde dehydrogenase 1


enzyme: Aldehyde dehydrogenase family 3 member B1


enzyme_display_name: betaine-aldehyde dehydrogenase

substrate_name: Betaine aldehyde; NAD+; H2O

enzyme: betaine-aldehyde dehydrogenase

substrate: Betaine aldehyde; NAD+; H2O


substrate_name: Betaine aldehyde; H2O; NAD+

substrate: Betaine aldehyde; H2O; NAD+


organism: Oryza sativa

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


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

organism: Arabidopsis thaliana


enzyme_display_name: Betaine aldehyde dehydrogenase

enzyme: Betaine aldehyde dehydrogenase


enzyme_display_name: Betaine aldehyde dehydrogenase 2

organism: Oryza sativa subsp. japonica

substrate_name: gamma-guanidinobutyraldehyde (GGBald)

enzyme: Betaine aldehyde dehydrogenase 2

substrate: gamma-guanidinobutyraldehyde (GGBald)


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

enzyme: Aminoaldehyde dehydrogenase 1a


enzyme_display_name: NAD/NADP-dependent betaine aldehyde dehydrogenase

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

substrate_name: betaine aldehyde (at pH 8.0 and 30 degrees Celsius, in the presence of NADP(+))

assay_conditions_summary: pH 8

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


enzyme_display_name: Aminoaldehyde dehydrogenase BADH

organism: Spinacia oleracea

enzyme: Aminoaldehyde dehydrogenase BADH


organism: Giardia duodenalis

substrate_name: acetyl-CoA

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

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA


substrate_name: NADH

substrate: NADH


substrate_name: CoA

substrate: CoA


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: propanal

smiles: CCC=O

substrate: propanal


organism: Synechococcus sp.

substrate_name: NADPH; Glycerate 3-phosphate; H+

substrate: NADPH; Glycerate 3-phosphate; H+


organism: Burkholderia xenovorans LB400

substrate_name: Coenzyme A; Acetaldehyde; NAD+

unit: Mswedgeone

substrate: Coenzyme A; Acetaldehyde; NAD+


organism: Thermus thermophilus

substrate_name: Acetaldehyde; Coenzyme A; NAD+

verification_status: verified

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat; cells Km 15.4+/-1.5, kcat 3.5+/-0.01.

normalized_value_unit_evidence: kcat normalized_value=3.5 normalized_unit=s^-1; Km normalized_value=15.4 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde: Km 15.4+/-1.5; kcat 3.5+/-0.01 s^-1.

substrate: Acetaldehyde; Coenzyme A; NAD+

status: verified


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde; columns Km, kcat; cells Km 9.4+/-0.8, kcat 2.8+/-0.07.

normalized_value_unit_evidence: kcat normalized_value=2.8 normalized_unit=s^-1; Km normalized_value=9.4 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde: Km 9.4+/-0.8; kcat 2.8+/-0.07 s^-1.


organism: Burkholderia xenovorans

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat; cells Km 15.7+/-1.3, kcat 2.2+/-0.06.

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; Km normalized_value=15.7 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde: Km 15.7+/-1.3; kcat 2.2+/-0.06 s^-1.


substrate_name: NAD+; Coenzyme A; Acetaldehyde

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde; columns Km, kcat; cells Km 23.6+/-1.8, kcat 17.2+/-0.5.

normalized_value_unit_evidence: kcat normalized_value=17.2 normalized_unit=s^-1; Km normalized_value=23.6 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde: Km 23.6+/-1.8; kcat 17.2+/-0.5 s^-1.

substrate: NAD+; Coenzyme A; Acetaldehyde


substrate_name: Acetaldehyde

source_db: oed

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 23.6+/-1.8, kcat 17.2+/-0.5, kcat/Km 7.3+/-0.06 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=17.2 normalized_unit=s^-1; Km normalized_value=23.6 normalized_unit=mM; kcat/Km normalized_value=0.73 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate acetaldehyde: Km 23.6+/-1.8; kcat 17.2+/-0.5 s^-1; kcat/Km 7.3+/-0.06 x10^2 M^-1 s^-1.

substrate: Acetaldehyde

source: oed


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 15.7+/-1.3, kcat 2.2+/-0.06, kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; Km normalized_value=15.7 normalized_unit=mM; kcat/Km normalized_value=0.14 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate acetaldehyde: Km 15.7+/-1.3; kcat 2.2+/-0.06 s^-1; kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 9.4+/-0.8, kcat 2.8+/-0.07, kcat/Km 3.0+/-0.3 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.8 normalized_unit=s^-1; Km normalized_value=9.4 normalized_unit=mM; kcat/Km normalized_value=0.30 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase BphI / substrate acetaldehyde: Km 9.4+/-0.8; kcat 2.8+/-0.07 s^-1; kcat/Km 3.0+/-0.3 x10^2 M^-1 s^-1.


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 15.4+/-1.5, kcat 3.5+/-0.01, kcat/Km 2.3+/-0.3 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=3.5 normalized_unit=s^-1; Km normalized_value=15.4 normalized_unit=mM; kcat/Km normalized_value=0.23 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase TTHB246 / substrate acetaldehyde: Km 15.4+/-1.5; kcat 3.5+/-0.01 s^-1; kcat/Km 2.3+/-0.3 x10^2 M^-1 s^-1.


organism: Saccharomyces cerevisiae

substrate_name: NAD+; D-Glyceraldehyde 3-phosphate; Phosphate


substrate_name: Glycerate 1,3-bisphosphate; H+; NADH

substrate: Glycerate 1,3-bisphosphate; H+; NADH


substrate_name: Phosphate; D-Glyceraldehyde 3-phosphate; NAD+


substrate_name: D-Glyceraldehyde 3-phosphate; NAD+; Phosphate


substrate_name: D-Glyceraldehyde 3-phosphate; Phosphate; NAD+


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

substrate_name: NADPH; Glycerate 1,3-bisphosphate; H+

assay_conditions_summary: cofactor NADPH

substrate: NADPH; Glycerate 1,3-bisphosphate; H+


substrate_name: NADPH; H+; Glycerate 1,3-bisphosphate

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

substrate: NADPH; H+; Glycerate 1,3-bisphosphate


organism: Thermoanaerobacter ethanolicus

substrate_name: n-butyryl-CoA

substrate: n-butyryl-CoA


substrate_name: acetyl-CoA


substrate_name: NADH


substrate_name: CoA


substrate_name: NAD+

substrate: NAD+


substrate_name: acetaldehyde


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


organism: Crocosphaera subtropica

substrate_name: succinate semialdehyde

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

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

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

proof_lines: pH 9.0, 25°C, recombinant mutant K154A, with NADP+

proof_lines: pH 9.0, 25°C, recombinant mutant K154A, with NAD+

substrate: succinate semialdehyde


substrate_name: NADP+

substrate: NADP+


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

proof_lines: pH 9.0, 25°C, recombinant mutant S157E, with NAD+

proof_lines: pH 9.0, 25°C, recombinant mutant S157E, with NADP+


proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme, with NAD+

proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme, with NADP+


proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme


organism: Methanothermus fervidus

substrate_name: NADPH

column_label: Table 2 columns Reaction Reduction of GriP2; Variable substrate NADPH; fixed GriP2 0.7 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.002 mM.

raw_value_unit_evidence: Table 2 row NADPH: Km=0.002 mM and Vmax=7.5 U/mg protein.

row_label: Reduction of GriP2 row NADPH

table_label: Table 2

substrate: NADPH


column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate NADP+; fixed GraP 2 mM; fixed arsenate 120 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.003 mM.

raw_value_unit_evidence: Table 2 row NADP+: Km=0.003 mM and Vmax=4.3 U/mg protein.

row_label: Oxidation of GraP row NADP+


column_label: Table 2 columns Reaction Reduction of GriP2; Variable substrate NADH; fixed GriP2 0.7 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.066 mM.

raw_value_unit_evidence: Table 2 row NADH: Km=0.066 mM and Vmax=12.6 U/mg protein.

row_label: Reduction of GriP2 row NADH

substrate: NADH


column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate NAD+; fixed GraP 2 mM; fixed arsenate 120 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=0.65 mM.

raw_value_unit_evidence: Table 2 row NAD+: Km=0.65 mM and Vmax=12.0 U/mg protein.

row_label: Oxidation of GraP row NAD+


substrate_name: arsenate

column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate arsenate; fixed NAD+ 1 mM; fixed GraP 2 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=43 mM.

raw_value_unit_evidence: Table 2 row arsenate: Km=43 mM and Vmax=12.5 U/mg protein.

row_label: Oxidation of GraP row arsenate

substrate: arsenate


substrate_name: phosphate

smiles: OP(=O)(O)O

column_label: Table 2 columns Reaction Oxidation of GraP; Variable substrate phosphate; fixed NAD+ 1 mM; fixed GraP 2 mM; Km; Vmax.

normalized_value_unit_evidence: Table 2 normalized central value: Km=53 mM.

raw_value_unit_evidence: Table 2 row phosphate: Km=53 mM and Vmax=13.7 U/mg protein.

row_label: Oxidation of GraP row phosphate

substrate: phosphate


organism: Propionibacterium freudenreichii

substrate: CoA


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


substrate_name: propanal

substrate: propanal


substrate: acetaldehyde


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; cofactor NADPH

column_label: PMID 22841742 Table 4, Reduction / NADPH, Km (mM) = 0.18 +/- 0.07.

normalized_value_unit_evidence: Km normalized_value=0.18 mM.

raw_value_unit_evidence: Table 4 row Reduction / NADPH, Km column: 0.18 +/- 0.07 mM.

row_label: Reduction / NADPH

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


substrate_name: DL-glyceraldehyde 3-phosphate

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

assay_conditions_summary: pH 8; cofactor NADP+

column_label: PMID 22841742 Table 4, Oxidation / DL-GAP row under NADP+ condition, Km (mM) = 0.21 +/- 0.04.

normalized_value_unit_evidence: Km normalized_value=0.21 mM.

raw_value_unit_evidence: Table 4 row Oxidation / DL-GAP with 0.5 mM NADP+ and 20 mM phosphate, Km column: 0.21 +/- 0.04 mM.

row_label: Oxidation / DL-GAP with NADP+

substrate: DL-glyceraldehyde 3-phosphate


normalized_value_unit_evidence: Km normalized_value=0.28 mM.

raw_value_unit_evidence: Table 4 row Oxidation / NADP+, Km column: 0.28 +/- 0.08 mM.

row_label: Oxidation / NADP+


assay_conditions_summary: pH 8; cofactor NADH

normalized_value_unit_evidence: Km normalized_value=0.61 mM.

raw_value_unit_evidence: Table 4 row Reduction / NADH, Km column: 0.61 +/- 0.07 mM.

row_label: Reduction / NADH


substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines: wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C

substrate: 3-phospho-D-glyceroyl phosphate


column_label: PMID 22841742 Table 4, Oxidation / Phosphate, Km (mM) = 107 +/- 22; no phosphate Km = 10.7 mM cell.

normalized_value_unit_evidence: Km normalized_value=107 mM for phosphate row; expected 10.7 mM is not a Km cell.

raw_value_unit_evidence: Table 4 row Oxidation / Phosphate, Km column: 107 +/- 22 mM. The 10.7 +/- 5.3 mM value appears in the Ki column for the adjacent NAD+ row, not the phosphate Km cell.

row_label: Oxidation / Phosphate


assay_conditions_summary: pH 8; cofactor NAD+

normalized_value_unit_evidence: Km normalized_value=16.8 mM.

raw_value_unit_evidence: Table 4 row Oxidation / NAD+, Km column: 16.8 +/- 8.9 mM.

row_label: Oxidation / NAD+


substrate_name: Unknown

substrate: Unknown


organism: Thermoanaerobacter sp.

substrate_name: butyryl-CoA

assay_conditions_summary: pH 7.9; 333.15 K; cofactor CoA

substrate: butyryl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: Butyraldehyde

substrate: Butyraldehyde


organism: Leuconostoc mesenteroides

substrate_name: CoA


substrate_name: NAD+

substrate: NAD+


substrate_name: acetaldehyde


assay_conditions_summary: cofactor ATP


organism: Clostridium kluyveri


substrate_name: Butanal

substrate: Butanal


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


organism: Bacillus anthracis

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: at pH 8.5, temperature not specified in the publication

proof_lines: pH 8.6, temperature not specified in the publication


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Thermoproteus tenax

substrate_name: NADP+

substrate: NADP+


substrate_name: arsenate

substrate: arsenate


substrate_name: phosphate

substrate: phosphate


substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+


substrate_name: Succinic semialdehyde

proof_lines: with NAD+ as cosubstrate, at pH 6.5 and 70°C

proof_lines: with NADP+ as cosubstrate, at pH 6.5 and 70°C

substrate: Succinic semialdehyde


substrate_name: 2-oxoglutarate semialdehyde

substrate: 2-oxoglutarate semialdehyde


assay_conditions_summary: pH 6.5; 343.15 K; cofactor NAD+


substrate_name: NADPH

assay_conditions_summary: pH 6.5; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 7.5; cofactor NADP+


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: malonate-semialdehyde dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: malonate semialdehyde

enzyme: malonate-semialdehyde dehydrogenase

substrate: malonate semialdehyde


assay_conditions_summary: cofactor NAD+


substrate_name: Unknown

substrate: Unknown


organism: Bacillus subtilis

assay_conditions_summary: 303.15 K; cofactor NAD+

proof_lines: pH not specified in the publication, 30°C


assay_conditions_summary: 303.15 K; cofactor NADP+

proof_lines: cofactor NAD+, pH not specified in the publication, 30°C

proof_lines: cofactor NADP+, pH not specified in the publication, 30°C


organism: Pyrococcus woesei

assay_conditions_summary: cofactor NADP+


organism: Synechococcus sp.

assay_conditions_summary: cofactor NADPH


organism: Kluyveromyces lactis

assay_conditions_summary: pH 9.2; cofactor NADP+

column_label: Official ACS article visible text, Affinity for NADP, NAD, and D-glyceraldehyde 3-phosphate section

row_label: GDP1/NADP-GAPDH; NADP substrate

table_label: Official ACS article visible prose


assay_conditions_summary: pH 9.2; cofactor NAD+

row_label: GDP1/NADP-GAPDH; NAD substrate


raw_value_unit_evidence: D-glyceraldehyde 3-phosphate Km 750 uM

row_label: GDP1/NADP-GAPDH; D-glyceraldehyde 3-phosphate substrate


assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 313.15 K; cofactor NADP+

proof_lines:
pH 8.0, 40°C, cosubstrate: NAD+
pH 8.0, 40°C, cosubstrate: NADP+
pH 8.0, 60°C, cosubstrate: NAD+


assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+


substrate_name: 3-phospho-D-glyceroyl phosphate

substrate: 3-phospho-D-glyceroyl phosphate


organism: Rattus norvegicus

proof_lines:
synaptosomes
mitochondria of non-synaptic origin


proof_lines:
mitochondria of non-synaptic origin
synaptosomes


organism: Thermococcus kodakarensis


organism: Euglena gracilis


organism: Thermus thermophilus


organism: Chlamydomonas reinhardtii

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: pH 7.0, temperature not specified in the publication

substrate: acetyl-CoA


organism: Hippoglossus hippoglossus

substrate_name: NADH; H+; Glycerate 1,3-bisphosphate

substrate: NADH; H+; Glycerate 1,3-bisphosphate


organism: Trichoderma koningii


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 338.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7.5; 323.15 K; cofactor NAD+


organism: Paraburkholderia xenovorans

substrate_name: picolinaldehyde

kcat_over_km_origin: calculated

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

assay_conditions_summary: pH 8; buffer 100 mM HEPES

proof_lines: mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)

substrate: picolinaldehyde


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

proof_lines: mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0)


substrate_name: propionaldehyde

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

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

source_databases_merged: brenda oed

substrate: propionaldehyde


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


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


organism: Geobacillus stearothermophilus

sequence_variant_note: Mutation signature S48G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E276G 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_ec_organism_unique and applied mutation signature S186G with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


substrate_name: D-glyceraldehyde 3-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y46G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: D-glyceraldehyde 3-phosphate


sequence_variant_note: Mutation signature D186G/S48G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D186G and mutant enzyme S48G


substrate_name: phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E276G/S48G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E276G and mutant enzyme S48G

substrate: phosphate


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


substrate_name: NADP+

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

substrate: NADP+


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


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.


proof_lines:
mutant enzyme D32A/L187N
mutant enzyme D32A and L187N


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

proof_lines: wild-type enzyme and mutant enzyme L187N


organism: Staphylococcus aureus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C151S/H178N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H178N with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C151S to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.7; cofactor NAD+


enzyme_display_name: UniProt Q6GIL8

assay_conditions_summary: pH 8.7; 298.15 K; cofactor NAD+

proof_lines: kcat is 70 sec(-1) for dehydrogenase activity.

enzyme: UniProt Q6GIL8


organism: Spinacia oleracea

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.


proof_lines: GapB, analyzed under reducing conditions

proof_lines: AB-GAPDH, analyzed under reducing conditions


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R77A to reconstruct the assayed variant sequence.


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

proof_lines: mutant B(188)A, analyzed under oxidizing conditions

proof_lines: A(plusCTE) mutant, analyzed under oxidizing conditions


proof_lines: A(plusCTE) mutant, analyzed under reducing conditions


proof_lines: GapB, analyzed under oxidizing conditions


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C

proof_lines: mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C


proof_lines: wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C

proof_lines: wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C


proof_lines: mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C

proof_lines: mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C


assay_conditions_summary: pH 8; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y139R with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R136K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E141D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L138T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K137E to reconstruct the assayed variant sequence.


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y317A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N313T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y317G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature T34Q/T39S/L43Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant T34Q/T39S/L43Q


sequence_variant_note: Mutation signature D282G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant D282G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant N313T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W310F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant W310F


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

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, wild-type


sequence_variant_note: Mutation signature Y283V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, tetrameric enzyme form, mutant Y283V


organism: Corynebacterium glutamicum

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


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

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


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

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


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

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


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


proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme


assay_conditions_summary: cofactor NADPH

proof_lines: wild type enzyme, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature S195A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme S195A, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature R82D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme R82D, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature R82A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme R82A, pH and temperature not specified in the publication


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


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

assay_conditions_summary: cofactor NADH

proof_lines: mutant enzyme R190A, pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetaldehyde (in the presence of HsaF)

assay_conditions_summary: cofactor CoA

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

substrate: acetaldehyde (in the presence of HsaF)


substrate_name: propanal (in the presence of HsaF)

substrate: propanal (in the presence of HsaF)


substrate_name: coenzyme A (in the presence of HsaF)

substrate: coenzyme A (in the presence of HsaF)


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


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

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


organism: Nitrosomonas europaea

assay_conditions_summary: pH 8.5; cofactor NAD+

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


substrate_name: succinate semialdehyde

assay_conditions_summary: pH 8.5; cofactor NADP+

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

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

substrate: succinate semialdehyde


substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines: GapB, analyzed under reducing conditions

proof_lines: GapB, analyzed under oxidizing conditions


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R77A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W84F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature W48F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


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)

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


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

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)

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

enzyme: aspartate-semialdehyde dehydrogenase


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_name: D-glyceraldehyde 3-phosphate


enzyme_display_name: Acetaldehyde dehydrogenase

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

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


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(+)

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)

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

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

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.

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


organism: Escherichia coli (strain K12)

substrate_name: NAD

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

substrate: NAD


organism: Geobacillus stearothermophilus

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

substrate: NAD+


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+

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+


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


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


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'


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.


substrate_name: succinate semialdehyde

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


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

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


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+


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

substrate: NADP+


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

substrate: succinate semialdehyde


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


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

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.