enzyme_display_name: L-idonate 5-dehydrogenase (NAD+)

organism: Aspergillus niger

substrate_name: L-Idonate

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

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

assay_conditions_summary: pH 7; cofactor NAD+

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: L-idonate 5-dehydrogenase (NAD+)

substrate: L-Idonate


source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, temperature not specified in the publication

status: unverified

source: brenda


organism: Leuconostoc mesenteroides

substrate_name: NADP+

protein_accession_database: UniProt

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

sequence_source: multiple

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

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADP+

data_origin: experimental

source_databases_merged: brenda skid uniprot

substrate: NADP+


organism: Sphingomonas sp. PAMC 26621

substrate_name: D-glucose 6-phosphate

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

assay_conditions_summary: 293.15 K; cofactor NADP+

proof_lines: 20°C, NAD+-linked reaction, pH not specified in the publication

proof_lines: 30°C, NAD+-linked reaction, pH not specified in the publication

proof_lines: 20°C, NADP+-linked reaction, pH not specified in the publication

substrate: D-glucose 6-phosphate


enzyme_display_name: D-galacturonate reductase

substrate_name: L-galactonate

km_display: Not reported

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

assay_conditions_summary: pH 7.2; 295.15 K; cofactor NADP+

proof_lines: with NAD+ as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C

proof_lines: with NADP+ as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C

enzyme: D-galacturonate reductase

substrate: L-galactonate


substrate_name: D-glucuronate

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.2; 295.15 K; cofactor NADPH

proof_lines: with NADH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C

proof_lines: with NADPH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C

substrate: D-glucuronate


substrate_name: NADH

assay_conditions_summary: pH 7.2; 295.15 K; cofactor NADH

proof_lines: with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C

substrate: NADH


substrate_name: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P149V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.8; cofactor NADP+

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149V

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149V


substrate_name: NAD+

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature P149V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NAD+

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row P149V; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 2230 uM; kcat cell = 166 min^-1; kcat/Km NAD+ cell = 0.07. captured primary segment: NAD+ | P149V G6PD, the site-directed P149V single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 2230 uM | Table 4 kcat 166 min^-1 | Table 4 kcat/Km NAD+ printed cell 0.07 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row P149V: Km NAD+ = 2230 uM; kcat = 166 min^-1; kcat/Km NAD+ = 0.07 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row P149V

substrate: NAD+

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P149G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149G

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149G


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature P149G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADP+

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row P149G; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 24 uM; kcat cell = 512 min^-1; kcat/Km NADP+ cell = 21. captured primary segment: NADP+ | P149G G6PD, the site-directed P149G single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 24 uM | Table 3 kcat 512 min^-1 | Table 3 kcat/Km NADP+ printed cell 21 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row P149G: Km NADP+ = 24 uM; kcat = 512 min^-1; kcat/Km NADP+ = 21 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row P149G


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row P149G; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 1760 uM; kcat cell = 1 050 min^-1; kcat/Km NAD+ cell = 0.60. captured primary segment: NAD+ | P149G G6PD, the site-directed P149G single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 1760 uM | Table 4 kcat 1 050 min^-1 | Table 4 kcat/Km NAD+ printed cell 0.60 under the column head kcat/Km NAD+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NAD+ cell 1760 uM; 1 uM = 1/1000 mM, so 1760 / 1000 = 1.76 mM; the export stores 1.76 mM. kcat: printed cell 1 050 min^-1; the printed turnover column is per MINUTE, so 1050 / 60 = 17.5 s^(-1); the export stores 17.5 s^(-1). kcat/Km: Printed kcat/Km NAD+ cell 0.60 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 0.60 x 16.666666666666668 = 10.0 s^(-1)*mM^(-1). The export stores 9.943181818181818 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row P149G: Km NAD+ = 1760 uM; kcat = 1 050 min^-1; kcat/Km NAD+ = 0.60 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row P149G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D374Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme D374Q

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme D374Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature D374Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row D374Q; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 13 uM; kcat cell = 4 510 min^-1; kcat/Km NADP+ cell = 346. captured primary segment: NADP+ | D374Q G6PD, the site-directed D374Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 13 uM | Table 3 kcat 4 510 min^-1 | Table 3 kcat/Km NADP+ printed cell 346 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row D374Q: Km NADP+ = 13 uM; kcat = 4 510 min^-1; kcat/Km NADP+ = 346 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row D374Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y415F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y415F

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y415F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Y415F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row Y415F; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 6.3 uM; kcat cell = 11 000 min^-1; kcat/Km NADP+ cell = 1750. captured primary segment: NADP+ | Y415F G6PD, the site-directed Y415F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 6.3 uM | Table 3 kcat 11 000 min^-1 | Table 3 kcat/Km NADP+ printed cell 1750 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row Y415F: Km NADP+ = 6.3 uM; kcat = 11 000 min^-1; kcat/Km NADP+ = 1750 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row Y415F


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row D374Q; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 571 uM; kcat cell = 12 500 min^-1; kcat/Km NAD+ cell = 22. captured primary segment: NAD+ | D374Q G6PD, the site-directed D374Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 571 uM | Table 4 kcat 12 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 22 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row D374Q: Km NAD+ = 571 uM; kcat = 12 500 min^-1; kcat/Km NAD+ = 22 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row D374Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q47A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47A

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K182Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182Q

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K182Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row K182Q; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 82 uM; kcat cell = 15 300 min^-1; kcat/Km NAD+ cell = 187. captured primary segment: NAD+ | K182Q G6PD, the site-directed K182Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 82 uM | Table 4 kcat 15 300 min^-1 | Table 4 kcat/Km NAD+ printed cell 187 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row K182Q: Km NAD+ = 82 uM; kcat = 15 300 min^-1; kcat/Km NAD+ = 187 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row K182Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y179F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y179F

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y179F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Y179F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row Y179F; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 14 uM; kcat cell = 15 800 min^-1; kcat/Km NADP+ cell = 1130. captured primary segment: NADP+ | Y179F G6PD, the site-directed Y179F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 14 uM | Table 3 kcat 15 800 min^-1 | Table 3 kcat/Km NADP+ printed cell 1130 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row Y179F: Km NADP+ = 14 uM; kcat = 15 800 min^-1; kcat/Km NADP+ = 1130 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row Y179F


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row K182Q; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 6.5 uM; kcat cell = 18 500 min^-1; kcat/Km NADP+ cell = 2800. captured primary segment: NADP+ | K182Q G6PD, the site-directed K182Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 6.5 uM | Table 3 kcat 18 500 min^-1 | Table 3 kcat/Km NADP+ printed cell 2800 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K182Q: Km NADP+ = 6.5 uM; kcat = 18 500 min^-1; kcat/Km NADP+ = 2800 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row K182Q


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row Y415F; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 116 uM; kcat cell = 19 000 min^-1; kcat/Km NAD+ cell = 164. captured primary segment: NAD+ | Y415F G6PD, the site-directed Y415F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 116 uM | Table 4 kcat 19 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 164 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Y415F: Km NAD+ = 116 uM; kcat = 19 000 min^-1; kcat/Km NAD+ = 164 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Y415F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T14S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14S

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14S


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature T14S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row T14S; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 14 uM; kcat cell = 22 700 min^-1; kcat/Km NADP+ cell = 1620. captured primary segment: NADP+ | T14S G6PD, the site-directed T14S single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 14 uM | Table 3 kcat 22 700 min^-1 | Table 3 kcat/Km NADP+ printed cell 1620 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row T14S: Km NADP+ = 14 uM; kcat = 22 700 min^-1; kcat/Km NADP+ = 1620 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row T14S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K343R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343R

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K343R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row K343R; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 8.0 uM; kcat cell = 24 200 min^-1; kcat/Km NADP+ cell = 2030. captured primary segment: NADP+ | K343R G6PD, the site-directed K343R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 8.0 uM | Table 3 kcat 24 200 min^-1 | Table 3 kcat/Km NADP+ printed cell 2030 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K343R: Km NADP+ = 8.0 uM; kcat = 24 200 min^-1; kcat/Km NADP+ = 2030 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row K343R


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row Y179F; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 184 uM; kcat cell = 28 500 min^-1; kcat/Km NAD+ cell = 155. captured primary segment: NAD+ | Y179F G6PD, the site-directed Y179F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 184 uM | Table 4 kcat 28 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 155 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Y179F: Km NAD+ = 184 uM; kcat = 28 500 min^-1; kcat/Km NAD+ = 155 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Y179F


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47E

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47E


substrate_name: D-galactose 6-phosphate

kcat_display: Not reported

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

assay_conditions_summary: pH 7.8; cofactor NAD+

source_databases_merged: brenda uniprot

substrate: D-galactose 6-phosphate


substrate_name: 2-deoxy-D-glucose 6-phosphate

substrate: 2-deoxy-D-glucose 6-phosphate


substrate_name: D-glucose 6-sulfate

substrate: D-glucose 6-sulfate


enzyme_display_name: GDH/6PGL endoplasmic bifunctional protein

organism: Mus musculus

substrate_name: D-glucose (at pH 7.1 in the presence of NADP)

source_db: uniprot

source: uniprot


substrate_name: D-glucose 6-phosphate (at pH 9.6 in the presence of NADP)

enzyme: GDH/6PGL endoplasmic bifunctional protein


substrate_name: 2-deoxy-D-glucose 6-phosphate (at pH 7.1 in the presence of NADP)


substrate_name: D-galactopyranose 6-phosphate (at pH 7.1 in the presence of NADP)


substrate_name: NADP (at pH 7.1 in the presence of galactose 6-phosphate)


substrate_name: NAD (at pH 7.1 in the presence of D-glucose)


enzyme_display_name: Nicotine blue oxidoreductase

organism: Paenarthrobacter nicotinovorans

verification_status: verified

assay_conditions_summary: pH 7.1; buffer 200 uM NADH in potassium phosphate; cofactor NADH

column_label: Table 2 Km column maps 1,4-naphthoquinone to 6.25 uM

raw_value_unit_evidence: Km raw_value=6.25 raw_unit=uM

table_label: PMID 17293530 PMC Table 2

enzyme: Nicotine blue oxidoreductase

status: verified


column_label: Table 2 Km column maps 1,4-benzoquinone to 8.83 uM

raw_value_unit_evidence: Km raw_value=8.83 raw_unit=uM


column_label: Table 2 Km column maps 2,6-dichlorophenol-indophenol to 23 uM

raw_value_unit_evidence: Km raw_value=23 raw_unit=uM


enzyme_display_name: perakine reductase

organism: Rauvolfia serpentina

substrate_name: perakine

assay_conditions_summary: pH 8.5; 310.15 K; buffer excess NADPH: 200 ul 50 mM KPi; cofactor NADPH

column_label: Table 4 columns are Substrate/Cofactor, Km (mM), Vmax (pKat/ug), Kcat (s^-1), Kcat/Km (M^-1 s^-1); Perakine row cells 0.83, 0.368, 0.014, 16.87.

raw_value_unit_evidence: Table 4 Perakine row: Km 0.83 mM, Vmax 0.368 pKat/ug, Kcat 0.014 s^-1, Kcat/Km 16.87 M^-1 s^-1.

row_label: Perakine

table_label: Springer official article Table 4, Kinetic parameters of recombinant PR

enzyme: perakine reductase

substrate: perakine


source_db: oed

column_label: Table 4 columns are Substrate/Cofactor, Km (mM), Vmax (pKat/ug), Kcat (s^-1), Kcat/Km (M^-1 s^-1); 4-Nitrobenzaldehyde row cells 0.28, 217.39, 8.26, 29,500.

raw_value_unit_evidence: Table 4 4-Nitrobenzaldehyde row: Km 0.28 mM, Vmax 217.39 pKat/ug, Kcat 8.26 s^-1, Kcat/Km 29,500 M^-1 s^-1.

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K21Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+

column_label: Table 2. Kinetic data for the NAD-linked reactions (Protein Science 1992, 1:329-334, journal page 331). Row K21Q; column Km G6P (uM) = 2,500; column Km NAD+ (uM) = 518; column kcat (min^-1) = 85,400; column kcat/Km (G6P) (min^-1 uM^-1) = 34.2.

raw_value_unit_evidence: Journal page 331, Table 2, row K21Q, varied substrate glucose 6-phosphate: Km G6P = 2,500 uM; kcat = 85,400 min^-1; kcat/Km G6P = 34.2 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K21R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADP+

column_label: Table 3. Kinetic data for the NADP-linked reaction (Protein Science 1992, 1:329-334, journal page 331). Row K21R; column Km G6P (uM) = 239; column Km NADP+ (uM) = 8.08; column Ki (NADP+) (uM) = 6.20; column kcat (min^-1) = 34,900; column kcat/Km (G6P) (min^-1 uM^-1) = 146.

raw_value_unit_evidence: Journal page 331, Table 3, row K21R, varied substrate glucose 6-phosphate: Km G6P = 239 uM; kcat = 34,900 min^-1; kcat/Km G6P = 146 min^-1 uM^-1.


substrate_name: NADP+


enzyme_display_name: UniProt K7ZP76

organism: Paracoccus laeviglucosivorans

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt K7ZP76

source: skid


substrate_name: myo-inositol

substrate: myo-inositol


enzyme_display_name: UniProt P0A9V8

organism: Escherichia coli

enzyme: UniProt P0A9V8


enzyme_display_name: sulfolactaldehyde 3-reductase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G122S to reconstruct the assayed variant sequence.

enzyme: sulfolactaldehyde 3-reductase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R123G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T124G to reconstruct the assayed variant sequence.


organism: Weissella confusa

substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: pyruvate

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

substrate: pyruvate


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Comamonas testosteroni

substrate_name: androstenol

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase

substrate: androstenol


substrate_name: androsterone

substrate: androsterone


substrate_name: Cyclohexanol

assay_conditions_summary: pH 10.5; 298.15 K; cofactor NAD+

substrate: Cyclohexanol


enzyme_display_name: D-arabitol-phosphate dehydrogenase

organism: Enterococcus avium

substrate_name: D-xylulose 5-phosphate

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

assay_conditions_summary: pH 7.2; 293.15 K; cofactor NADH

proof_lines:
20°C, pH 7.2, cofactor: NADH
20°C, pH 7.2, cofactor NADPH

enzyme: D-arabitol-phosphate dehydrogenase

substrate: D-xylulose 5-phosphate


substrate_name: D-arabitol 5-phosphate

assay_conditions_summary: pH 8.5; 293.15 K; cofactor NAD+

substrate: D-arabitol 5-phosphate


enzyme_display_name: farnesol dehydrogenase (NAD+)

organism: Carpoglyphus lactis

substrate_name: geraniol

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

assay_conditions_summary: pH 8.5; 295.15 K; cofactor NAD+

enzyme: farnesol dehydrogenase (NAD+)

substrate: geraniol


enzyme_display_name: farnesol dehydrogenase (NAD(+))

sequence: MVQNPGASAIQCRAAVLRKEGQPMKIEQVLIQA

wild_type_sequence: MVQNPGASAIQCRAAVLRKEGQPMKIEQVLIQA

smiles: CC(C)=CCC/C(C)=C/CO

column_label: Official Wiley/FEBS full-text prose section Catalytic properties for geraniol oxidation: Km 51.0 uM, kcat 2996 s^-1, and kcat/Km 58.8 s^-1*uM^-1 for geraniol.

raw_value_unit_evidence: Km 51.0 uM for geraniol; kcat 2996 s^-1 for geraniol; kcat/Km 58.8 s^-1*uM^-1 for geraniol.

row_label: geraniol

table_label: Prose section: Catalytic properties for geraniol oxidation

enzyme: farnesol dehydrogenase (NAD(+))


enzyme_display_name: 2-dehydropantolactone reductase

organism: Candida dubliniensis

enzyme: 2-dehydropantolactone reductase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H128A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T30A to reconstruct the assayed variant sequence.


enzyme_display_name: 2-hydroxymethylglutarate dehydrogenase

organism: Eubacterium barkeri

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

enzyme: 2-hydroxymethylglutarate dehydrogenase


assay_conditions_summary: cofactor NADH

proof_lines: Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri


enzyme_display_name: Aldo-keto reductase family 1 member B1

organism: Homo sapiens

substrate_name: acrolein

smiles: C=CC=O

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: Aldo-keto reductase family 1 member B1

substrate: acrolein


smiles: CC(=CC=O)C


smiles: CCCC=CC=O


smiles: CC=CC=CC=O


smiles: CCCCCC(C=CC=O)O


enzyme_display_name: Aldo-keto reductase family 1 member A1

substrate_name: S-nitroso-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 959 min(-1) for S-nitroso-CoA as substrate (PubMed:30538128). kcat is 604 min(-1) for D-glucuronate as substrate (PubMed:30538128). kcat is 306 min(-1) for D,L-glyceraldehyde as substrate (PubMed:30538128). kcat is 948 min(-1) for S

enzyme: Aldo-keto reductase family 1 member A1

substrate: S-nitroso-CoA


substrate_name: D-glucuronate

substrate: D-glucuronate


substrate_name: D,L-glyceraldehyde

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

substrate: D,L-glyceraldehyde


proof_lines: kcat is 1.3 sec(-1) for D,L-glyceraldehyde as substrate. kcat is 0.95 sec(-1) for D-xylose as substrate. kcat is 0.9 sec(-1) for D-glucose as substrate. kcat is 1.1 sec(-1) for D-galactose as substrate. kcat is 0.9 sec(-1) for D-glucuronate


enzyme_display_name: 3-sulfolactaldehyde reductase

organism: Escherichia coli (strain K12)

substrate_name: succinic semialdehyde

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

proof_lines: kcat is 332 sec(-1) with 3-sulfolactaldehyde as substrate. kcat is 548 sec(-1) with NADH as substrate.

enzyme: 3-sulfolactaldehyde reductase

substrate: succinic semialdehyde


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Methanocaldococcus jannaschii

substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: kcat is 0.33 sec(-1) for the oxidation of (S)-malate with NAD(+). kcat is 0.069 sec(-1) for the oxidation of (S)-malate with NADP(+). kcat is 0.2 sec(-1) for the oxidation of (2S,3S)-tartrate with NAD(+). kcat is 0.15 sec(-1) for the oxidat

substrate: NADPH


substrate_name: oxaloacetate

proof_lines:
70°C, pH 8.0
70°C, pH 8.0, cofactor: NADH
70°C, pH 8.0, cofactor: NADPH

substrate: oxaloacetate


substrate_name: NADH

assay_conditions_summary: pH 8; cofactor NADH

substrate: NADH


substrate_name: glucose

substrate: glucose


substrate_name: all-trans-retinal

substrate: all-trans-retinal


organism: Rattus norvegicus

substrate_name: D,L glyceraldehyde

column_label: ScienceDirect Table 1 row DL-Glyceraldehyde, Rat liver AKR1A Km (mM) column, reports 2.9 +/- 0.3 mM.

raw_value_unit_evidence: Km raw_value=2.9 +/- 0.3 raw_unit=mM for DL-Glyceraldehyde.

row_label: DL-Glyceraldehyde

table_label: ScienceDirect Table 1: Kinetics parameters of AKR1A

substrate: D,L glyceraldehyde


substrate_name: D-glucuronic acid

column_label: ScienceDirect Table 1 row D-Glucuronic acid, Rat liver AKR1A Km (mM) column, reports 1.8 +/- 0.1 mM.

raw_value_unit_evidence: Km raw_value=1.8 +/- 0.1 raw_unit=mM for D-Glucuronic acid.

row_label: D-Glucuronic acid

substrate: D-glucuronic acid


column_label: ScienceDirect Table 1 row Methylglyoxal, Rat liver AKR1A Km (mM) column, reports 0.31 +/- 0.01 mM.

raw_value_unit_evidence: Km raw_value=0.31 +/- 0.01 raw_unit=mM for Methylglyoxal.

row_label: Methylglyoxal


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

column_label: ScienceDirect Table 1 row 3-Deoxyglucosone, Rat liver AKR1A Km (mM) column, reports 0.63 +/- 0.03 mM.

raw_value_unit_evidence: Km raw_value=0.63 +/- 0.03 raw_unit=mM for 3-Deoxyglucosone.


substrate_name: D-glucurono-gamma-lactone

column_label: ScienceDirect Table 1 row D-Glucurono-gamma-lactone, Rat liver AKR1A Km (mM) column, reports 11 +/- 0 mM.

raw_value_unit_evidence: Km raw_value=11 +/- 0 raw_unit=mM for D-Glucurono-gamma-lactone.

row_label: D-Glucurono-gamma-lactone

substrate: D-glucurono-gamma-lactone


assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

source_databases_merged: skid uniprot


substrate_name: (S)-malate

assay_conditions_summary: pH 9.5; cofactor NADP+

column_label: Table 2. NAD+- and NADP+-dependent enzymatic oxidations of various alpha-hydroxy acids; row/segment (S)-Malate; NADP+; MJ0490 (MdhII); column/metric MJ0490 (MdhII), Km (mM)

raw_value_unit_evidence: Table 2 reports Km 0.025 +/- 0.005 mM for (S)-malate with NADP+ in the MJ0490 (MdhII) column.

row_label: (S)-Malate; NADP+; MJ0490 (MdhII)

substrate: (S)-malate


organism: Thauera aromatica

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH 7.4, 37°C, calculated as kcat number per subunit


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

proof_lines: kcat is 3.0 sec(-1) for D,L glyceraldehyde as substrate (PubMed:22820017). kcat is 3.0 sec(-1) for methylglyoxal as substrate (PubMed:22820017). kcat is 3.4 sec(-1) for 3-deoxyglucosone as substrate (PubMed:22820017). kcat is 3.1 sec(-1) fo


substrate_name: prostaglandin H2

substrate: prostaglandin H2


enzyme_display_name: UDP-N-acetylglucosamine 3-dehydrogenase

organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)

substrate_name: UDP-GalNAc

proof_lines: kcat is 0.9 sec(-) with UDP-GalNAc. kcat is 0.99 sec(-1) with NAD(+).

enzyme: UDP-N-acetylglucosamine 3-dehydrogenase

substrate: UDP-GalNAc


substrate_name: NAD(+)

column_label: PMC Table 1 row MMP0352 / NAD+, column Km (uM), reports 180 +/- 20.

normalized_value_unit_evidence: Km normalized 0.18 mM.

raw_value_unit_evidence: Km raw 180 +/- 20 uM for NAD+.

row_label: MMP0352; NAD+

table_label: Table 1. Apparent kinetic parameters for the UDP-GlcNAc oxidoreductases

substrate: NAD(+)


organism: Bos taurus

substrate_name: S-nitroso-CoA

proof_lines: kcat is 627 min(-1) for S-nitroso-CoA as substrate (PubMed:25512491). kcat is 471 min(-1) for S-nitroso-glutathione as substrate (PubMed:31649033).

substrate: S-nitroso-CoA


organism: Mus musculus

column_label: Table 1 lists DL-Glyceraldehyde with Km column value 0.044 mM.

raw_value_unit_evidence: Km raw_value=0.044 raw_unit=mM

row_label: DL-Glyceraldehyde row

table_label: Table 1. Substrate specificity of mouse aldose reductase expressed in E. coli


substrate_name: D-xylose

column_label: Table 1 lists D-Xylose with Km column value 5.03 mM, not the queued 5.0 mM.

raw_value_unit_evidence: Km raw_value=5.03 raw_unit=mM

row_label: D-Xylose row

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-glucuronate

column_label: Table 1 lists D-Glucuronate with Km column value 1.04 mM.

raw_value_unit_evidence: Km raw_value=1.04 raw_unit=mM

row_label: D-Glucuronate row

substrate: D-glucuronate


substrate_name: S-nitroso-glutathione

substrate: S-nitroso-glutathione


substrate_name: mevaldate

substrate: mevaldate


enzyme_display_name: D/L-glyceraldehyde reductase

organism: Trichoderma reesei

substrate_name: methylglyoxal

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD1 / methylglyoxal; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=0.4 raw_unit=mM

row_label: GLD1 / methylglyoxal

enzyme: D/L-glyceraldehyde reductase

substrate: methylglyoxal


substrate_name: L-glyceraldehyde

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD1 / L-glyceraldehyde; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=0.9 raw_unit=mM

row_label: GLD1 / L-glyceraldehyde

substrate: L-glyceraldehyde


substrate_name: diacetyl

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

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD1 / diacetyl; column(s) Km (mM)

row_label: GLD1 / diacetyl

substrate: diacetyl


substrate_name: Glyoxal

smiles: C(=O)C=O

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD1 / Glyoxal; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=2.4 raw_unit=mM

row_label: GLD1 / Glyoxal

substrate: Glyoxal


substrate_name: dihydroxyacetone

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

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD1 / dihydroxyacetone; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=5.8 raw_unit=mM

row_label: GLD1 / dihydroxyacetone

substrate: dihydroxyacetone


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase

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

substrate_name: glucose 6-phosphate (with NADP)

assay_conditions_summary: cofactor NADP+

column_label: The abstract reports estimated Km values for purified G6PDH acting on glucose-6-phosphate, NADP+, and NAD+ were 530, 57, and 333 microM, respectively.

raw_value_unit_evidence: Km raw_value=530 microM raw_unit=microM

row_label: Prose segment: glucose-6-phosphate Km

table_label: PubMed PMID 9537370 abstract

enzyme: Glucose-6-phosphate 1-dehydrogenase

substrate: glucose 6-phosphate (with NADP)


substrate_name: NADP

raw_value_unit_evidence: Km raw_value=57 microM raw_unit=microM

row_label: Prose segment: NADP+ Km

substrate: NADP


substrate_name: NAD

raw_value_unit_evidence: Km raw_value=333 microM raw_unit=microM

row_label: Prose segment: NAD+ Km

substrate: NAD


organism: Paracoccus laeviglucosivorans

assay_conditions_summary: pH 6; 298.15 K; cofactor NADH

column_label: PMID 29799855 DOI 10.1371/journal.pone.0198010, Table 3, row L-epi-2-inosose, columns Km, kcat, and kcat/Km. Unlike the starred comparator rows, this row is measured in the current paper.

table_label: Table 3. Kinetic parameters of Pl-scyllo-IDH with L-2-epi-inosose and substrates


substrate_name: myo-inositol

assay_conditions_summary: pH 9; 298.15 K; buffer is 100 mM Tris-HCl pH 8; cofactor NAD+

column_label: PMID 23038265 DOI 10.1074/jbc.M112.403055, Table 1, LgdA row myo-inositol, columns Km, kcat, and kcat/Km; footnote a fixes 10 mM NAD+.

raw_value_unit_evidence: Table 1 myo-inositol: Km 53.3 +/- 8.6 mM; kcat 572 +/- 30 min^-1; kcat/Km 10.7 min^-1 mM^-1.

row_label: LgdA / myo-inositol

table_label: Table 1. Kinetic parameters of the L-glucose catabolic enzymes

substrate: myo-inositol


substrate_name: scyllo-Inositol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H318A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

column_label: PMID 29799855 DOI 10.1371/journal.pone.0198010, Table 4, row H318A, scyllo-inositol column block, metrics Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 4 H318A with scyllo-inositol: Km 154 +/- 43 mM; kcat 85.6 +/- 21 min^-1; kcat/Km 0.56 min^-1 mM^-1.

row_label: H318A / scyllo-inositol

table_label: Table 4. Kinetic parameters of Pl-scyllo-IDH mutants with scyllo-inositol and L-glucose

substrate: scyllo-Inositol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R178A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: PMID 29799855 DOI 10.1371/journal.pone.0198010, Table 4, row R178A, scyllo-inositol column block, metrics Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 4 R178A with scyllo-inositol: Km 40.6 +/- 7.2 mM; kcat 486 +/- 39 min^-1; kcat/Km 12.0 min^-1 mM^-1.

row_label: R178A / scyllo-inositol


column_label: PMID 23038265 DOI 10.1074/jbc.M112.403055, Table 1, LgdA row scyllo-inositol, columns Km, kcat, and kcat/Km; footnote a fixes 10 mM NAD+.

raw_value_unit_evidence: Table 1 scyllo-inositol: Km 3.70 +/- 0.4 mM; kcat 705 +/- 12 min^-1; kcat/Km 190 min^-1 mM^-1.

row_label: LgdA / scyllo-inositol


enzyme_display_name: UniProt D0WGK0

organism: Slackia exigua

substrate_name: NADH

enzyme: UniProt D0WGK0

substrate: NADH


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: UniProt P05793

organism: Escherichia coli

assay_conditions_summary: pH 7

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7

enzyme: UniProt P05793


enzyme_display_name: diacetyl reductase [(S)-acetoin forming]

organism: Mycobacterium sp.

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


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

enzyme: diacetyl reductase [(S)-acetoin forming]


organism: Bacillus subtilis (strain 168)

substrate_name: NADH (in the presence of 5 mM 2-inosose at 25 degrees Celsius and pH 7)

assay_conditions_summary: pH 7; cofactor NADH


substrate_name: NAD (in the presence of 40 mM myo-inositol at 25 degrees Celsius and pH 9)

assay_conditions_summary: pH 9


substrate_name: 2-inosose (in the presence of 0.1 mM NADH at 25 degrees Celsius and pH 7)


substrate_name: myo-inositol (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)


substrate_name: alpha-D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)


substrate_name: D-xylose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NAD+)

organism: Bacillus subtilis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

column_label: Table 4 reports IolX-(His)6, varied substrate NADH, constant substrate 10 mM SIS, K m = 0.019 +/- 0.007 mM; normalized Km = 0.019 mM.

normalized_value_unit_evidence: Km=0.019 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate NADH / K m column

table_label: Table 4 / Km and Vmax values for purified IolX-(His)6 and IolW-(His)6

enzyme: scyllo-inositol 2-dehydrogenase (NAD+)


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

column_label: Table 4 reports IolX-(His)6, varied substrate NAD+, constant substrate 60 mM SI, K m = 0.15 +/- 0.01 mM; normalized Km = 0.15 mM.

normalized_value_unit_evidence: Km=0.15 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate NAD+ / K m column

substrate: NAD+


substrate_name: scyllo-inosose

column_label: Table 4 reports IolX-(His)6, varied substrate SIS, constant substrate 0.5 mM NADH, K m = 2.85 +/- 0.48 mM; normalized Km = 2.85 mM.

normalized_value_unit_evidence: Km=2.85 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate SIS / K m column

substrate: scyllo-inosose


column_label: Table 4 reports IolX-(His)6, varied substrate SI, constant substrate 0.5 mM NAD+, K m = 17.1 +/- 0.24 mM; normalized Km = 17.1 mM.

normalized_value_unit_evidence: Km=17.1 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate SI / K m column


organism: Carpoglyphus lactis

substrate_name: geraniol

substrate: geraniol


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+

column_label: Abstract reports Km values for geraniol and NAD+ were 51.0 microM and 59.5 microM respectively.

raw_value_unit_evidence: Km raw_value=59.5 microM raw_unit=microM

row_label: Carpoglyphus lactis geraniol dehydrogenase / NAD+

table_label: PubMed XML abstract PMID 18422649


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NADP(+)) IolW

substrate_name: NADP(+)

column_label: Table 4 reports IolW-(His)6, varied substrate NADP+, constant substrate 60 mM SI, K m = 0.096 +/- 0.015 mM; normalized Km = 0.096 mM.

normalized_value_unit_evidence: Km=0.096 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate NADP+ / K m column

substrate: NADP(+)


assay_conditions_summary: cofactor NADPH

column_label: Table 4 reports IolW-(His)6, varied substrate NADPH, constant substrate 10 mM SIS, K m = 0.027 +/- 0.008 mM; normalized Km = 0.027 mM.

normalized_value_unit_evidence: Km=0.027 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate NADPH / K m column

enzyme: scyllo-inositol 2-dehydrogenase (NADP(+)) IolW


enzyme_display_name: UniProt P77398

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt P77398


enzyme_display_name: (R)-mandelate dehydrogenase

organism: Schleiferilactobacillus harbinensis

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

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+

enzyme: (R)-mandelate dehydrogenase


substrate_name: (R)-mandelate

substrate: (R)-mandelate


enzyme_display_name: ketol-acid reductoisomerase [NAD(P)+]

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

proof_lines: mutant A71S/R76D/S78D/Q110A, pH 7.0, temperature not specified in the publication

enzyme: ketol-acid reductoisomerase [NAD(P)+]


proof_lines: mutant S78D/Q110V, pH 7.0, temperature not specified in the publication


proof_lines: mutant S78D, pH 7.0, temperature not specified in the publication


proof_lines: mutant Q110A, pH 7.0, temperature not specified in the publication


proof_lines: mutant Q110V, pH 7.0, temperature not specified in the publication


proof_lines: mutant A71S/R76D/S78D/Q110V, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant A71S/R76D/S78D/Q110V, pH 7.0, temperature not specified in the publication


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

proof_lines: wild-type, pH 7.0, temperature not specified in the publication


proof_lines: mutant A71S/R76D/S78D/Q110V/D146G/G185R/K433E , pH not specified in the publication, temperature not specified in the publication


assay_conditions_summary: cofactor NADH


organism: Shewanella sp.

proof_lines: mutant R76D/Ser78D, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant A71S/R76D/S78AD/Q110V, pH not specified in the publication, temperature not specified in the publication


organism: Rhodotorula graminis

substrate_name: Unknown

ki_unit: mM

proof_lines: pH 5.9, temperature not specified in the publication

substrate: Unknown


assay_conditions_summary: pH 9.5; 300.15 K; cofactor NADH


substrate_name: phenylglyoxylate

substrate: phenylglyoxylate


assay_conditions_summary: pH 9.5; 300.15 K; cofactor NAD+


enzyme_display_name: L-rhamnose 1-dehydrogenase [NAD(P)+]

organism: Azotobacter vinelandii

substrate_name: L-Mannose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F99Y to reconstruct the assayed variant sequence.

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

enzyme: L-rhamnose 1-dehydrogenase [NAD(P)+]

substrate: L-Mannose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F99A to reconstruct the assayed variant sequence.


substrate_name: L-rhamnose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q156A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

substrate: L-rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature I196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T191F with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


substrate_name: L-Lyxose

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

substrate: L-Lyxose


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

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


substrate_name: NADP+

assay_conditions_summary: pH 9; cofactor NADP+

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D200H to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 9; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S37H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D200A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R15T to reconstruct the assayed variant sequence.


enzyme_display_name: L-arabinose 1-dehydrogenase [NAD(P)+]

organism: Azospirillum brasilense

substrate_name: L-arabinose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173S to reconstruct the assayed variant sequence.

proof_lines:
pH 9.0, 30°C, mutant enzyme N173S
30°C, pH 9.0, mutant enzyme N173S

enzyme: L-arabinose 1-dehydrogenase [NAD(P)+]

substrate: L-arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme N173A
pH 9.0, 30°C, mutant enzyme N173A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173Q to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme N173Q
pH 9.0, 30°C, mutant enzyme N173Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S37D/R38A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme S37D/R38A
pH 9.0, 30°C, mutant enzyme S37D/R38A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173G to reconstruct the assayed variant sequence.

proof_lines:
pH 9.0, 30°C, mutant enzyme N173G
30°C, pH 9.0, mutant enzyme N173G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173V to reconstruct the assayed variant sequence.

proof_lines:
pH 9.0, 30°C, mutant enzyme N173V
30°C, pH 9.0, mutant enzyme N173V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152Y to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152Y
pH 9.0, 30°C, mutant enzyme W152Y


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H119N to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme H119N
pH 9.0, 30°C, mutant enzyme H119N


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152F to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152F
pH 9.0, 30°C, mutant enzyme W152F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S37D to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme S37D
pH 9.0, 30°C, mutant enzyme S37D


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152H to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152H
pH 9.0, 30°C, mutant enzyme W152H


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R38A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme R38A
pH 9.0, 30°C, mutant enzyme R38A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152A
pH 9.0, 30°C, mutant enzyme W152A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W231A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W231A
pH 9.0, 30°C, mutant enzyme W231A


enzyme_display_name: ketol-acid reductoisomerase (NAD+)

organism: Archaeoglobus fulgidus

substrate_name: NADH

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

proof_lines: pH 7, temperature not specified in the publication, cosubstrate: (2S)-2-hydroxy-2-methyl-3-oxobutanoate

enzyme: ketol-acid reductoisomerase (NAD+)


enzyme_display_name: L-rhamnose 1-dehydrogenase (NADP+)

organism: Thermoplasma acidophilum

proof_lines: kcat is 1.341 min(-1) for dehydrogenase activity with L-rhamnose as substrate (at pH 7 and 60 degrees Celsius). kcat is 1.426 min(-1) for dehydrogenase activity with L-lyxose as substrate (at pH 7 and 60 degrees Celsius). kcat is 892.9 min(

enzyme: L-rhamnose 1-dehydrogenase (NADP+)


assay_conditions_summary: pH 7; cofactor NADP+

proof_lines:
pH 7.0, 60°C, cosubstrate: L-lyxose
pH 7.0, 60°C, cosubstrate: L-rhamnose
pH 7.0, 60°C, cosubstrate: L-mannose


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase YdfG

organism: Escherichia coli (strain K12)

substrate_name: NADP(+) (at pH 9 and at 30 degrees Celsius)

proof_lines: The highest catalytic efficiency was observed with L-allo-threonine.


substrate_name: L-serine (at pH 9 and at 30 degrees Celsius)

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

enzyme: NADP-dependent 3-hydroxy acid dehydrogenase YdfG


substrate_name: D-threonine (at pH 9 and at 30 degrees Celsius)

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


substrate_name: L-glycerate (at pH 9 and at 30 degrees Celsius)

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


substrate_name: D-glycerate (at pH 9 and at 30 degrees Celsius)


enzyme_display_name: Ketol-acid reductoisomerase (NAD(+))

organism: Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)

substrate_name: NADH (at pH 7 with S2AL as substrate)

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.

proof_lines: kcat is 0.46 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate). kcat is 0.25 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate).

enzyme: Ketol-acid reductoisomerase (NAD(+))

substrate: NADH (at pH 7 with S2AL as substrate)


substrate_name: NADPH (at pH 7 with S2AL as substrate)

assay_conditions_summary: pH 7; cofactor NADPH

substrate: NADPH (at pH 7 with S2AL as substrate)


organism: Haloferax volcanii

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

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: pH 8.0, temperature not specified in the publication


substrate_name: D-galactose

assay_conditions_summary: pH 8

substrate: D-galactose


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession:D0WGK0 and applied mutation signature S61D/S63D to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Se_KARI DD / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Se_KARI DD / NADPH: KM 880 uM; kcat 0.10 s^-1; kcat/KM 0.11 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.88 mM; kcat=0.10 s^-1; kcat/Km=0.11 s^-1*mM^-1.

row_label: Se_KARI DD / NADPH


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

proof_lines: mutant S61D/S63D/I95V, pH not specified in the publication, temperature not specified in the publication


column_label: Table 1 row Se_KARI / mutations column dash; K_M for cofactors [uM] / NADH = 45; kcat for cofactors [s^-1] / NADH = 0.41; kcat/K_M [mM^-1 s^-1] / NADH = 9.

normalized_value_unit_evidence: Km normalized_value=0.045 normalized_unit=mM; kcat normalized_value=0.41 normalized_unit=s^-1; kcat/Km normalized_value=9 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=45 raw_unit=uM for NADH; kcat raw_value=0.41 raw_unit=s^-1 for NADH; kcat/Km raw_value=9 raw_unit=mM^-1 s^-1 for NADH.

row_label: Se_KARI / mutations column dash

table_label: PMC3704004 Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and variants

substrate: NADH


column_label: Table 1 row Se_KARI / mutations column dash; K_M for cofactors [uM] / NADPH = 1; kcat for cofactors [s^-1] / NADPH = 0.8; kcat/K_M [mM^-1 s^-1] / NADPH = 800.

normalized_value_unit_evidence: Km normalized_value=0.001 normalized_unit=mM; kcat normalized_value=0.8 normalized_unit=s^-1; kcat/Km normalized_value=800 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=1 raw_unit=uM for NADPH; kcat raw_value=0.8 raw_unit=s^-1 for NADPH; kcat/Km raw_value=800 raw_unit=mM^-1 s^-1 for NADPH.

substrate: NADPH


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Se_KARI DD / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Se_KARI DD / NADH: KM 113 uM; kcat 0.97 s^-1; kcat/KM 9 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.113 mM; kcat=0.97 s^-1; kcat/Km=9 s^-1*mM^-1.

row_label: Se_KARI DD / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession:D0WGK0 and applied mutation signature S61D/S63D/I95V to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Se_KARI DDV / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Se_KARI DDV / NADH: KM 47 uM; kcat 1.01 s^-1; kcat/KM 22 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.047 mM; kcat=1.01 s^-1; kcat/Km=22 s^-1*mM^-1.

row_label: Se_KARI DDV / NADH


organism: Hydrogenobaculum sp. Y04AAS1

assay_conditions_summary: pH 7; cofactor NADH


enzyme_display_name: L-rhamnose 1-dehydrogenase (NAD(P)(+))

organism: Azotobacter vinelandii (strain DJ / ATCC BAA-1303)

substrate_name: NAD(+)

proof_lines: kcat is 2230 min(-1) with L-rhamnose as substrate (in the presence of NAD(+)) (PubMed:18505728). kcat is 4490 min(-1) with L-rhamnose as substrate (in the presence of NADP(+)) (PubMed:18505728). kcat is 5010 min(-1) with L-rhamnose as subst

enzyme: L-rhamnose 1-dehydrogenase (NAD(P)(+))

substrate: NAD(+)


substrate_name: NADP(+)


enzyme_display_name: Ketol-acid reductoisomerase (NAD(P)(+))

organism: Hydrogenobaculum sp. (strain Y04AAS1)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: kcat is 0.12 sec(-1) for isomerase activity with NADPH (at pH 7 with S2AL as substrate). kcat is 0.12 sec(-1) for isomerase activity with NADH (at pH 7 with S2AL as substrate).

enzyme: Ketol-acid reductoisomerase (NAD(P)(+))


organism: Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)

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

proof_lines: kcat is 0.28 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate). kcat is 0.22 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N172A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A

proof_lines: pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A


substrate_name: D-talose

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines: pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense

proof_lines: pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense

source_databases_merged: brenda skid

substrate: D-talose


substrate_name: D-xylose

substrate: D-xylose


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

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


organism: Slackia exigua

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

proof_lines: mutant S61D/S63D, pH not specified in the publication, 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.

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


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

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A to reconstruct the assayed variant sequence.

proof_lines: kcat is 0.07 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate). kcat is 0.06 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate).


organism: uncultured archaeon

proof_lines: pH 7, temperature not specified in the publication, cosubstrate: (2S)-2-hydroxy-2-methyl-3-oxobutanoate


substrate_name: L-fucose

substrate: L-fucose


substrate_name: L-Mannose


substrate_name: L-Lyxose


enzyme_display_name: 3-hydroxy acid dehydrogenase

organism: Saccharomyces cerevisiae

substrate_name: D-serine

assay_conditions_summary: pH 9

proof_lines: The highest catalytic efficiency was observed with L-allo-threonine.

enzyme: 3-hydroxy acid dehydrogenase

substrate: D-serine


substrate_name: L-allo-threonine

substrate: L-allo-threonine


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

proof_lines: kcat is 0.1 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate). kcat is 0.04 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate).


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADP(+) (at pH 9 and at 30 degrees Celsius)


organism: Desulfosudis oleivorans

substrate_name: NADH


organism: Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: kcat is 0.25 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate).


enzyme_display_name: L-arabinose 1-dehydrogenase [NAD(P)(+)]

organism: Azospirillum brasilense

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R38A to reconstruct the assayed variant sequence.

enzyme: L-arabinose 1-dehydrogenase [NAD(P)(+)]

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S37D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S37D/R38A to reconstruct the assayed variant sequence.


substrate_name: NADP+


substrate_name: L-Arabinose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H119N to reconstruct the assayed variant sequence.

substrate: L-Arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173Q to reconstruct the assayed variant sequence.


organism: Thermacetogenium phaeum

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


organism: Lactococcus lactis subsp. lactis

sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q02138 and applied mutation signature V48L/R49P/K52E/S53D to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPED / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Ll_KARI LPED / NADPH: KM 1,180 uM; kcat 0.06 s^-1; kcat/KM 0.05 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=1.18 mM; kcat=0.06 s^-1; kcat/Km=0.05 s^-1*mM^-1.

row_label: Ll_KARI LPED / NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q02138 and applied mutation signature V48L/R49P/K52L/S53D to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPLD / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Ll_KARI LPLD / NADPH: KM 1,000 uM; kcat 0.08 s^-1; kcat/KM 0.08 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=1.0 mM; kcat=0.08 s^-1; kcat/Km=0.08 s^-1*mM^-1.

row_label: Ll_KARI LPLD / NADPH


column_label: Table 1 row Ll_KARI / mutations column dash; K_M for cofactors [uM] / NADH = 285; kcat for cofactors [s^-1] / NADH = 0.1; kcat/K_M [mM^-1 s^-1] / NADH = 0.43.

normalized_value_unit_evidence: Km normalized_value=0.285 normalized_unit=mM; kcat normalized_value=0.1 normalized_unit=s^-1; kcat/Km normalized_value=0.43 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=285 raw_unit=uM for NADH; kcat raw_value=0.1 raw_unit=s^-1 for NADH; kcat/Km raw_value=0.43 raw_unit=mM^-1 s^-1 for NADH.

row_label: Ll_KARI / mutations column dash


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPED / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Ll_KARI LPED / NADH: KM 128 uM; kcat 0.35 s^-1; kcat/KM 2.7 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.128 mM; kcat=0.35 s^-1; kcat/Km=2.7 s^-1*mM^-1.

row_label: Ll_KARI LPED / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q02138 and applied mutation signature V48L/R49P/K52L/S53D/E59K/T182S/E320K to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI 2G6 / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Ll_KARI 2G6 / NADPH: KM 749 uM; kcat 0.35 s^-1; kcat/KM 0.47 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.749 mM; kcat=0.35 s^-1; kcat/Km=0.47 s^-1*mM^-1.

row_label: Ll_KARI 2G6 / NADPH


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPLD / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Ll_KARI LPLD / NADH: KM 108 uM; kcat 0.40 s^-1; kcat/KM 3.7 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.108 mM; kcat=0.40 s^-1; kcat/Km=3.7 s^-1*mM^-1.

row_label: Ll_KARI LPLD / NADH


column_label: Table 1 row Ll_KARI / mutations column dash; K_M for cofactors [uM] / NADPH = 13; kcat for cofactors [s^-1] / NADPH = 0.8; kcat/K_M [mM^-1 s^-1] / NADPH = 65.

normalized_value_unit_evidence: Km normalized_value=0.013 normalized_unit=mM; kcat normalized_value=0.8 normalized_unit=s^-1; kcat/Km normalized_value=65 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=13 raw_unit=uM for NADPH; kcat raw_value=0.8 raw_unit=s^-1 for NADPH; kcat/Km raw_value=65 raw_unit=mM^-1 s^-1 for NADPH.


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI 2G6 / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Ll_KARI 2G6 / NADH: KM 15 uM; kcat 1.07 s^-1; kcat/KM 71 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.015 mM; kcat=1.07 s^-1; kcat/Km=71 s^-1*mM^-1.

row_label: Ll_KARI 2G6 / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W231A to reconstruct the assayed variant sequence.


organism: Escherichia coli

proof_lines: D-serine YdfG


substrate_name: D-Threonine

substrate: D-Threonine


substrate_name: L-Glycerate

substrate: L-Glycerate


substrate_name: L-serine

substrate: L-serine


substrate_name: L-allo-Threonine

substrate: L-allo-Threonine


substrate_name: D-Glycerate

substrate: D-Glycerate


organism: Bacillus subtilis (strain 168)

substrate_name: scyllo-inositol

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

column_label: Table 4 reports IolW-(His)6, varied substrate SI, constant substrate 0.5 mM NADP+, K m = 34.3 +/- 4.4 mM; normalized Km = 34.3 mM.

normalized_value_unit_evidence: Km=34.3 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate SI / K m column

substrate: scyllo-inositol


substrate_name: scyllo-inosose

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

column_label: Table 4 reports IolW-(His)6, varied substrate SIS, constant substrate 0.5 mM NADPH, K m = 1.68 +/- 0.16 mM; normalized Km = 1.68 mM.

normalized_value_unit_evidence: Km=1.68 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate SIS / K m column

substrate: scyllo-inosose


substrate_name: NADP(+)

column_label: Table 4 reports IolW-(His)6, varied substrate NADP+, constant substrate 60 mM SI, K m = 0.096 +/- 0.015 mM; normalized Km = 0.096 mM.

substrate: NADP(+)


substrate_name: NADPH

column_label: Table 4 reports IolW-(His)6, varied substrate NADPH, constant substrate 10 mM SIS, K m = 0.027 +/- 0.008 mM; normalized Km = 0.027 mM.

substrate: NADPH


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=8


substrate_name: D-Galactose

substrate: D-Galactose


enzyme_display_name: L-arabinose 1-dehydrogenase (NAD(P)(+))

substrate_name: NADP(+) (at 30 degrees Celsius and pH 9.0)

assay_conditions_summary: cofactor NADP+

enzyme: L-arabinose 1-dehydrogenase (NAD(P)(+))


organism: Mycolicibacterium smegmatis

substrate_name: mycothiol

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

column_label: Table 2, formaldehyde dehydrogenase (a), reports K MSH (uM) = 17.3 +/- 0.8.

raw_value_unit_evidence: Km raw_value=17.3 raw_unit=uM

row_label: Formaldehyde dehydrogenase (a)

table_label: Table 2 - Kinetic parameters for the formaldehyde dehydrogenase (a) and MSNO (b) reductase reactions

substrate: mycothiol


assay_conditions_summary: pH 8.7; cofactor NAD+

column_label: Table 2, formaldehyde dehydrogenase (a), reports K NAD (uM) = 354 +/- 16.

raw_value_unit_evidence: Km raw_value=354 raw_unit=uM


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Sungouiella intermedia

substrate_name: oenanthaldehyde

smiles: CCCCCCC=O

column_label: Official PMC PDF page 5 (journal page 105), Table 4, Oenanthaldehyde row under Candida intermedia II, columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat=4.6 s^-1; Km=4.7 mM; printed kcat/Km=0.979 s^-1 mM^-1. The exported 0.978723404255319 is the same-row 4.6/4.7 quotient before table rounding.

raw_value_unit_evidence: Table 4, Candida intermedia II, Oenanthaldehyde: kcat=4.6 +/- 0.2 s^-1; Km=4.7 +/- 1.1 mM; kcat/Km=979 M^-1 s^-1.

row_label: Oenanthaldehyde; Candida intermedia II

table_label: Table 4. Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR

enzyme: D-xylose reductase [NAD(P)H]

substrate: oenanthaldehyde


substrate_name: D-galactose

column_label: Official PMC PDF page 5 (journal page 105), Table 4, Galactose row under Candida intermedia II, columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat=5.9 s^-1; Km=74 mM; printed kcat/Km=0.080 s^-1 mM^-1. The exported 0.07972972972972973 is the same-row 5.9/74 quotient before table rounding.

raw_value_unit_evidence: Table 4, Candida intermedia II, Galactose: kcat=5.9 +/- 0.1 s^-1; Km=74 +/- 4 mM; kcat/Km=80 M^-1 s^-1.

row_label: Galactose; Candida intermedia II

substrate: D-galactose


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: NAD(+)-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose


substrate_name: UDP-glucuronate

substrate: UDP-glucuronate


substrate_name: NADP+

substrate: NADP+


proof_lines:
preferred NADP+ to NAD+ as a coenzyme
purified enzyme
Azospirillum brasilense

substrate: NAD+


substrate_name: D-serine

column_label: Official ScienceDirect HTML Table 4 row d-Serine gives YMR226C (B) kcat 7.84 s^-1, Km 71 mM, and Vmax/Km 110 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=7.84 normalized_unit=s^-1; Km normalized_value=71.0 normalized_unit=mM; kcat/Km normalized_value=0.1104225352112676 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=7.84 raw_unit=s^-1; Km raw_value=71 raw_unit=mM; Vmax/Km raw_value=110 raw_unit=s^-1 M^-1

row_label: d-Serine; YMR226C column group (B)

table_label: Table 4. Kinetic parameters of YdfG (A) and YMR226C (B)

substrate: D-serine


column_label: Official ScienceDirect HTML Table 4 row l-3-Hydroxybutyrate gives YMR226C (B) kcat 9.38 s^-1, Km 95 mM, and Vmax/Km 99 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=9.38 normalized_unit=s^-1; Km normalized_value=95.0 normalized_unit=mM; kcat/Km normalized_value=0.09873684210526316 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=9.38 raw_unit=s^-1; Km raw_value=95 raw_unit=mM; Vmax/Km raw_value=99 raw_unit=s^-1 M^-1

row_label: l-3-Hydroxybutyrate; YMR226C column group (B)


column_label: Official ScienceDirect HTML Table 4 row l-Serine gives YMR226C (B) kcat 11.0 s^-1, Km 95 mM, and Vmax/Km 116 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=11.0 normalized_unit=s^-1; Km normalized_value=95.0 normalized_unit=mM; kcat/Km normalized_value=0.11578947368421053 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=11.0 raw_unit=s^-1; Km raw_value=95 raw_unit=mM; Vmax/Km raw_value=116 raw_unit=s^-1 M^-1

row_label: l-Serine; YMR226C column group (B)


column_label: Official ScienceDirect HTML Table 4 row l-allo-Threonine gives YMR226C (B) kcat 43.8 s^-1, Km 3 mM, and Vmax/Km 14,600 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=43.8 normalized_unit=s^-1; Km normalized_value=3.0 normalized_unit=mM; kcat/Km normalized_value=14.6 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=43.8 raw_unit=s^-1; Km raw_value=3 raw_unit=mM; Vmax/Km raw_value=14,600 raw_unit=s^-1 M^-1

row_label: l-allo-Threonine; YMR226C column group (B)


substrate_name: D-Threonine

column_label: Official ScienceDirect HTML Table 4 row d-Threonine gives YMR226C (B) kcat 52.8 s^-1, Km 7 mM, and Vmax/Km 7540 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=52.8 normalized_unit=s^-1; Km normalized_value=7.0 normalized_unit=mM; kcat/Km normalized_value=7.542857142857143 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=52.8 raw_unit=s^-1; Km raw_value=7 raw_unit=mM; Vmax/Km raw_value=7540 raw_unit=s^-1 M^-1

row_label: d-Threonine; YMR226C column group (B)

substrate: D-Threonine


enzyme_display_name: L-rhamnose 1-dehydrogenase (NADP(+))

organism: Thermoplasma acidophilum

substrate_name: L-Lyxose

enzyme: L-rhamnose 1-dehydrogenase (NADP(+))

substrate: L-Lyxose


substrate_name: L-Mannose

substrate: L-Mannose


assay_conditions_summary: pH 7; 333.15 K; cofactor NADP+

proof_lines:
L-rhamnose
NADP(+)
Thermoplasma acidophilum


substrate_name: L-Rhamnose

substrate: L-Rhamnose


enzyme_display_name: sulfoacetaldehyde reductase (NADPH)

organism: Klebsiella oxytoca

substrate_name: isethionate

smiles: O=S(=O)(O)CCO

enzyme: sulfoacetaldehyde reductase (NADPH)

substrate: isethionate


assay_conditions_summary: pH 10; 295.15 K; cofactor NADP+


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: NAD (with CHMS as substrate at 25 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 3 row NAD+ (200) lists Km 20.6 +/- 1.0 uM with CHMS in parentheses; table footnote states Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=20.6 +/- 1.0 raw_unit=uM for CHMS with NAD+.

row_label: LigC / CHMS Km with NAD+ (200 uM cofactor)

table_label: PMC111406 Table 3, kinetic constants of CHMS dehydrogenases


substrate_name: NADP (with CHMS as substrate at 25 degrees Celsius and pH 8)

column_label: Table 3 row NADP+ (200) lists Km 26.0 +/- 0.5 uM with CHMS in parentheses; table footnote states Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=26.0 +/- 0.5 raw_unit=uM for CHMS with NADP+.

row_label: LigC / CHMS Km with NADP+ (200 uM cofactor)


enzyme_display_name: L-serine 3-dehydrogenase (NAD+)

organism: Pseudomonas aeruginosa

substrate_name: L-serine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature S122A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 11; 310.15 K; buffer a 1 ml reaction mixture containing 50 mM diethanolamine; cofactor NAD+

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block S122A, variable substrate row L-Serine; column Km (mM) = 10.6; column kcat (s^-1) = 0.4; column kcat/Km (M^-1 s^-1) = 0.4 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.4 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 0.4 s^(-1). Km: printed Table 1 cell 10.6 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 10.6 mM. kcat/Km: printed Table 1 cell 0.4 x 10^2 M^-1 s^-1, that is 40 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 40 / 1000 = 0.04 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block S122A, variable substrate row L-Serine: Km = 10.6 mM; kcat = 0.4 s^-1; printed kcat/Km = 0.4 x 10^2 M^-1 s^-1.

table_label: Table 1: Kinetic parameters of PA0743 with various substrates (J. Biol. Chem. 2012, 287(3):1874-1883)

enzyme: L-serine 3-dehydrogenase (NAD+)

substrate: L-serine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature Y219A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block Y219A, variable substrate row L-Serine; column Km (mM) = 11.0; column kcat (s^-1) = 0.8; column kcat/Km (M^-1 s^-1) = 0.7 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.8 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 0.8 s^(-1). Km: printed Table 1 cell 11.0 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 11.0 mM. kcat/Km: printed Table 1 cell 0.7 x 10^2 M^-1 s^-1, that is 70 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 70 / 1000 = 0.07 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Y219A, variable substrate row L-Serine: Km = 11.0 mM; kcat = 0.8 s^-1; printed kcat/Km = 0.7 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature T96A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block T96A, variable substrate row L-Serine; column Km (mM) = 12.3; column kcat (s^-1) = 1.4; column kcat/Km (M^-1 s^-1) = 0.1 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.4 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 1.4 s^(-1). Km: printed Table 1 cell 12.3 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 12.3 mM. kcat/Km: printed Table 1 cell 0.1 x 10^3 M^-1 s^-1, that is 100 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 100 / 1000 = 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block T96A, variable substrate row L-Serine: Km = 12.3 mM; kcat = 1.4 s^-1; printed kcat/Km = 0.1 x 10^3 M^-1 s^-1.


assay_conditions_summary: pH 11; 310.15 K; buffer a reaction mixture (1 ml) containing 50 mM diethanolamine; cofactor NAD+

column_label: Table 1, PA0743 wild type NAD+ row: Km 3.4 ± 0.2 mM; kcat 1.6 ± 0.1 s^-1; printed kcat/Km 0.5 × 10^3 M^-1 s^-1 = 0.5 s^-1 mM^-1. The current quotient 0.4705882352941177 lies in both the uncertainty quotient interval [1.5/3.6, 1.7/3.2] = [0.4166666666666667, 0.53125] and the printed-efficiency interval [0.45, 0.55).

normalized_value_unit_evidence: The printed same-row central cells are kcat=1.6 s^-1 and Km=3.4 mM. Their stored-precision quotient is 1.6 / 3.4 = 0.4705882352941177 s^-1 mM^-1. The independently printed efficiency 0.5 × 10^3 M^-1 s^-1 normalizes separately to 0.5 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=3.4 ± 0.2 raw_unit=mM; kcat raw_value=1.6 ± 0.1 raw_unit=s^-1; kcat/Km printed_raw_value=0.5 × 10^3 raw_unit=M^-1 s^-1

row_label: Wild type / NAD+

table_label: Table 1. Kinetic parameters of PA0743 with various substrates


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature N175A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block N175A, variable substrate row L-Serine; column Km (mM) = 4.2; column kcat (s^-1) = 2.7; column kcat/Km (M^-1 s^-1) = 0.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.7 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 2.7 s^(-1). Km: printed Table 1 cell 4.2 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 4.2 mM. kcat/Km: printed Table 1 cell 0.6 x 10^3 M^-1 s^-1, that is 600 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 600 / 1000 = 0.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block N175A, variable substrate row L-Serine: Km = 4.2 mM; kcat = 2.7 s^-1; printed kcat/Km = 0.6 x 10^3 M^-1 s^-1.


substrate_name: D-glycerate

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block Wild type, variable substrate row DL-Glyceric acid; column Km (mM) = 19.8; column kcat (s^-1) = 5.8; column kcat/Km (M^-1 s^-1) = 0.3 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.8 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 5.8 s^(-1). Km: printed Table 1 cell 19.8 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 19.8 mM. kcat/Km: printed Table 1 cell 0.3 x 10^3 M^-1 s^-1, that is 300 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300 / 1000 = 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Wild type, variable substrate row DL-Glyceric acid: Km = 19.8 mM; kcat = 5.8 s^-1; printed kcat/Km = 0.3 x 10^3 M^-1 s^-1.

substrate: D-glycerate


substrate_name: DL-threonine

assay_conditions_summary: pH 11

substrate: DL-threonine


assay_conditions_summary: pH 11; 310.15 K; buffer a reaction mixture (1 ml) containing 50 mM diethanolamine; cofactor NADP+

column_label: Table 1, PA0743 wild type L-serine row: Km 2.5 ± 0.1 mM; kcat 10.4 ± 0.2 s^-1; printed kcat/Km 0.4 × 10^4 M^-1 s^-1 = 4.0 s^-1 mM^-1. The current quotient 4.16 lies in both the uncertainty quotient interval [10.2/2.6, 10.6/2.4] = [3.923076923076923, 4.416666666666667] and the printed-efficiency interval [3.5, 4.5).

normalized_value_unit_evidence: The printed same-row central cells are kcat=10.4 s^-1 and Km=2.5 mM. Their stored-precision quotient is 10.4 / 2.5 = 4.16 s^-1 mM^-1. The independently printed efficiency 0.4 × 10^4 M^-1 s^-1 normalizes separately to 4.0 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=2.5 ± 0.1 raw_unit=mM; kcat raw_value=10.4 ± 0.2 raw_unit=s^-1; kcat/Km printed_raw_value=0.4 × 10^4 raw_unit=M^-1 s^-1

row_label: Wild type / L-serine


substrate_name: methyl 2,2-dimethyl-3-hydroxypropionate

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

normalized_value_unit_evidence: The printed same-row central cells are kcat=11.6 s^-1 and Km=17.4 mM. Their stored-precision quotient is 11.6 / 17.4 = 0.6666666666666667 s^-1 mM^-1. The independently printed efficiency 0.7 × 10^3 M^-1 s^-1 normalizes separately to 0.7 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=17.4 ± 1.2 raw_unit=mM; kcat raw_value=11.6 ± 0.4 raw_unit=s^-1; kcat/Km printed_raw_value=0.7 × 10^3 raw_unit=M^-1 s^-1

row_label: Wild type / MDHP

substrate: methyl 2,2-dimethyl-3-hydroxypropionate


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: glucose 6-phosphate

proof_lines: The catalytic efficiency with NAD(+) is about 230-fold higher than with NADP(+), indicating that NAD(+) is the physiological electron acceptor.

substrate: glucose 6-phosphate


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: NAD(P)H-dependent D-xylose reductase

organism: Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)

substrate_name: DL-Glyceraldehyde

proof_lines: The enzyme was active with various aldose substrates, such as D-galactose and D-glucose.

enzyme: NAD(P)H-dependent D-xylose reductase

substrate: DL-Glyceraldehyde


substrate_name: D-Galactose

substrate: D-Galactose


enzyme_display_name: sulfoquinovose 1-dehydrogenase

organism: Pseudomonas putida

substrate_name: sulfoquinovose

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication

proof_lines: with NAD+ as cosubstrate, in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication

proof_lines: kcat is 33.8 sec(-1) for sulfoquinovose oxidation with NAD(+). kcat is 1.4 sec(-1) for sulfoquinovose oxidation with NADP(+).

enzyme: sulfoquinovose 1-dehydrogenase

substrate: sulfoquinovose


organism: Homo sapiens

substrate_name: 3beta-hydroxy-5beta-cholan-24-oic acid

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

substrate: 3beta-hydroxy-5beta-cholan-24-oic acid


enzyme_display_name: NAD-dependent L-serine dehydrogenase

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

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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / L-serine: Km=2.5 mM.

normalized_value_unit_evidence: Km=2.5 mM

raw_value_unit_evidence: Km=2.5 mM

row_label: Table 1 / Wild type / L-serine

enzyme: NAD-dependent L-serine dehydrogenase


substrate_name: NAD

assay_conditions_summary: cofactor NAD+

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / NAD+: Km=3.4 mM.

normalized_value_unit_evidence: Km=3.4 mM

raw_value_unit_evidence: Km=3.4 mM

row_label: Table 1 / Wild type / NAD+

substrate: NAD


enzyme_display_name: 3beta-hydroxysteroid dehydrogenase 2

organism: Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B)

proof_lines: kcat is 1750 min(-1) with 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate as substrate.

enzyme: 3beta-hydroxysteroid dehydrogenase 2


enzyme_display_name: 3beta-hydroxysteroid dehydrogenase 1

proof_lines: kcat is 584 min(-1) with 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate as substrate.

enzyme: 3beta-hydroxysteroid dehydrogenase 1


organism: Pyrobaculum calidifontis

substrate_name: NADP+

assay_conditions_summary: pH 10; 323.15 K; cofactor NADP+

proof_lines: pH 10.0, 50°C, recombinant wild-type enzyme

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 10; 323.15 K; cofactor NAD+

substrate: NAD+


substrate_name: DL-glycerate

substrate: DL-glycerate


enzyme_display_name: L-serine 3-dehydrogenase (NAD(+))

substrate_name: D-Glycerate

assay_conditions_summary: pH 11; 310.15 K; cofactor NAD+

proof_lines:
PA0743
NAD+-dependent L-serine dehydrogenase
l-serine

enzyme: L-serine 3-dehydrogenase (NAD(+))

substrate: D-Glycerate


enzyme_display_name: 2-oxoglutarate reductase

organism: Micrococcus aerogenes

enzyme: 2-oxoglutarate reductase


substrate_name: NADH

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


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


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines:
NADPH
coenzyme specificities
Candida intermedia

substrate: NADPH


proof_lines:
NADH
coenzyme specificities
Candida intermedia


organism: Fusobacterium nucleatum

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / Methyl-DL-serine: Km=2.4 mM; Vmax=17.2 umol/min/mg protein; kcat=9.6 s^-1; kcat/Km=0.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km=2.4 mM; Vmax=17.2 umol/min/mg protein; kcat=9.6 s^-1; kcat/Km=4.0 s^-1 mM^-1

row_label: Table 1 / Wild type / Methyl-DL-serine


substrate_name: Glycerate

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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / DL-glyceric acid: Km=19.8 mM; Vmax=10.4 umol/min/mg protein; kcat=5.8 s^-1; kcat/Km=0.3 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km=19.8 mM; Vmax=10.4 umol/min/mg protein; kcat=5.8 s^-1; kcat/Km=0.3 s^-1 mM^-1

row_label: Table 1 / Wild type / DL-glyceric acid

substrate: Glycerate


substrate_name: L-Serine

row_label: Table 1, enzyme block N175A, variable substrate row L-Serine

substrate: L-Serine


row_label: Table 1, enzyme block S122A, variable substrate row L-Serine


row_label: Table 1, enzyme block T96A, variable substrate row L-Serine


column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / L-serine: Km=2.5 mM; Vmax=18.7 umol/min/mg protein; kcat=10.4 s^-1; kcat/Km=0.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km=2.5 mM; Vmax=18.7 umol/min/mg protein; kcat=10.4 s^-1; kcat/Km=4.0 s^-1 mM^-1


row_label: Table 1, enzyme block Y219A, variable substrate row L-Serine


substrate_name: DL-threonine

substrate: DL-threonine


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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / MDHP: Km=17.4 mM; Vmax=20.9 umol/min/mg protein; kcat=11.6 s^-1; kcat/Km=0.7 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km=17.4 mM; Vmax=20.9 umol/min/mg protein; kcat=11.6 s^-1; kcat/Km=0.7 s^-1 mM^-1

row_label: Table 1 / Wild type / MDHP


column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / NAD+: Km=3.4 mM; Vmax=2.8 umol/min/mg protein; kcat=1.6 s^-1; kcat/Km=0.5 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km=3.4 mM; Vmax=2.8 umol/min/mg protein; kcat=1.6 s^-1; kcat/Km=0.5 s^-1 mM^-1


organism: Eggerthella lenta


enzyme_display_name: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 2

organism: Clostridium scindens (strain JCM 10418 / VPI 12708)

substrate_name: choloyl-CoA (at pH 8.7 and 37 degrees Celsius)

assay_conditions_summary: pH 8.7; cofactor CoA

proof_lines: kcat is 10 min(-1) with choloyl-CoA as substrate. kcat is 12 min(-1) with chenodeoxycholoyl-CoA as substrate. kcat is 11 min(-1) with lithocholoyl-CoA as substrate. kcat is 9.5 min(-1) with deoxycholoyl-CoA as substrate. kcat is 8.3 min(-1)


substrate_name: chenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)

enzyme: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 2


substrate_name: lithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: deoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxochenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxolithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: NAD(+) (at pH 8.7 and 37 degrees Celsius)


substrate_name: NADP(+) (at pH 8.7 and 37 degrees Celsius)