sequence_variant_note: Resolved canonical sequence from ncbi_genpept_accession:ABC19597.1 and applied mutation signature R31I/T32G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADP+

column_label: PMID 27587230 DOI 10.1038/srep32644 Table 2; row R31I/T32G; NAD+ columns under Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

row_label: R31I/T32G / NAD+


enzyme_display_name: phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)

organism: Moorella thermoacetica

substrate_name: NAD+

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NAD+

column_label: Table 2, row 'R31T', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31T / NAD+

table_label: Table 2

data_origin: experimental

substrate: NAD+

status: corrected

source: oed


mutation_signature: Unknown

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

column_label: Table 2, row 'WT', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: WT / NAD+

enzyme: phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)


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

organism: Thermochaetoides thermophila

substrate_name: D-galactose

verification_status: verified

kcat_over_km_origin: calculated

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

column_label: Table 4 columns: Substrate | kcat (s^-1) | KM,(Substrate) (mM) | kcat/KM,(Substrate) (mM^-1 min^-1)

normalized_value_unit_evidence: kcat 6.5 s^-1; KM 241.0 mM; normalized kcat/KM 0.026970954356846474 s^-1*mM^-1 from 6.5/241.0; table rounded efficiency 1.6 mM^-1 min^-1 is consistent after unit conversion

raw_value_unit_evidence: D-galactose row: kcat 6.5 +/- 0.4 s^-1; KM(Substrate) 241 +/- 29 mM; kcat/KM(Substrate) 1.6 +/- 0.2 mM^-1 min^-1

row_label: D-galactose

table_label: Table 4

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

substrate: D-galactose

status: verified


substrate_name: D-glucose

normalized_value_unit_evidence: kcat 2.7 s^-1; KM 471.0 mM; normalized kcat/KM 0.0057324840764331215 s^-1*mM^-1 from 2.7/471.0; table rounded efficiency 0.3 mM^-1 min^-1 is consistent after unit conversion

raw_value_unit_evidence: D-glucose row: kcat 2.7 +/- 0.5 s^-1; KM(Substrate) 471 +/- 141 mM; kcat/KM(Substrate) 0.3 +/- 0.1 mM^-1 min^-1

row_label: D-glucose

substrate: D-glucose


substrate_name: NADH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

column_label: Table 3 columns: Cofactor | kcat (s^-1) | KM,(Cofactor) (uM) | kcat/KM,(Cofactor) (uM^-1 min^-1)

normalized_value_unit_evidence: kcat 3.2 s^-1; KM 0.119 mM; normalized kcat/KM 26.890756302521012 s^-1*mM^-1 from 3.2/0.119; table rounded efficiency 1.6 uM^-1 min^-1 is consistent after unit conversion

raw_value_unit_evidence: NADH row: kcat 3.2 +/- 0.1 s^-1; KM(Cofactor) 119 +/- 6 uM; kcat/KM(Cofactor) 1.6 +/- 0.1 uM^-1 min^-1

row_label: NADH

table_label: Table 3

substrate: NADH


substrate_name: NADPH

normalized_value_unit_evidence: kcat 11.4 s^-1; KM 0.135 mM; normalized kcat/KM 84.44444444444444 s^-1*mM^-1 from 11.4/0.135; table rounded efficiency 5.1 uM^-1 min^-1 is consistent after unit conversion

raw_value_unit_evidence: NADPH row: kcat 11.4 +/- 1.1 s^-1; KM(Cofactor) 135 +/- 44 uM; kcat/KM(Cofactor) 5.1 +/- 1.7 uM^-1 min^-1

row_label: NADPH

substrate: NADPH


substrate_name: L-Arabinose

normalized_value_unit_evidence: kcat 8.8 s^-1; KM 62.5 mM; normalized kcat/KM 0.1408 s^-1*mM^-1 from 8.8/62.5; table rounded efficiency 8.4 mM^-1 min^-1 converts to 0.14 s^-1*mM^-1

raw_value_unit_evidence: L-arabinose row: kcat 8.8 +/- 0.4 s^-1; KM(Substrate) 62.5 +/- 7.7 mM; kcat/KM(Substrate) 8.4 +/- 1.1 mM^-1 min^-1

row_label: L-arabinose

substrate: L-Arabinose


substrate_name: D-Xylose

normalized_value_unit_evidence: kcat 9.2 s^-1; KM 22.3 mM; normalized kcat/KM 0.413 s^-1*mM^-1 from 9.2/22.3 rounded; table rounded efficiency 26 mM^-1 min^-1 is consistent after unit conversion

raw_value_unit_evidence: D-xylose row: kcat 9.2 +/- 0.6 s^-1; KM(Substrate) 22.3 +/- 6.1 mM; kcat/KM(Substrate) 26 +/- 7 mM^-1 min^-1

row_label: D-xylose

substrate: D-Xylose


column_label: Table 2 columns: Temperature | kcat (s^-1) | KM,(Xylose) (mM) | kcat/KM,(Xylose) (mM^-1 min^-1)

normalized_value_unit_evidence: kcat 35.2 s^-1; KM 25.4 mM; normalized kcat/KM 1.386 s^-1*mM^-1 from 35.2/25.4; table rounded efficiency 83 mM^-1 min^-1 is consistent after unit conversion


organism: Ensifer adhaerens

verification_status: unverified

status: unverified


substrate_name: D-Glucosone

column_label: Kinetic prose after Table 3 gives D-glucosone as second item for Km and kcat; corresponding efficiency is second item 5,700 M^-1 s^-1.

normalized_value_unit_evidence: D-glucosone normalized paper values: kcat=63.2 s^-1; Km=11.0 mM; kcat/Km=5.7 s^-1 mM^-1 from paper 5,700 M^-1 s^-1.

raw_value_unit_evidence: ASM PDF pmid_16461673_asm_pdf.pdf; text lines 384-389 state: AFR followed Michaelis-Menten kinetics for AF, D-glucosone, and NADPH with apparent Km values 8.4 +/- 0.15 mM, 11.0 +/- 0.10 mM, and 0.2 +/- 0.03 mM, respectively; apparent kcat values for AF and D-glucosone were 286.7 and 63.2 s^-1; corresponding catalytic efficiencies were 34,100 and 5,700 M^-1 s^-1.

row_label: D-glucosone

table_label: Table 3 and kinetic prose immediately following Table 3

substrate: D-Glucosone


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADP+


enzyme_display_name: 1,5-anhydro-D-fructose reductase

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: cofactor NADPH

column_label: Kinetic prose after Table 3 maps the first Km value (8.4 mM) to AF by the stated AF, D-glucosone, NADPH order.

normalized_value_unit_evidence: For AF, normalized paper Km=8.4 mM.

row_label: 1,5-Anhydro-D-fructose / AF

enzyme: 1,5-anhydro-D-fructose reductase

source: uniprot


substrate_name: D-glucosone

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

column_label: Kinetic prose after Table 3 maps the second Km value (11.0 mM) to D-glucosone by the stated AF, D-glucosone, NADPH order.

normalized_value_unit_evidence: For D-glucosone, normalized paper Km=11.0 mM.

substrate: D-glucosone


assay_conditions_summary: cofactor NADP+

column_label: Kinetic prose after Table 3 maps the third Km value (0.2 mM) to NADPH by the stated AF, D-glucosone, NADPH order.

normalized_value_unit_evidence: For NADPH, normalized paper Km=0.2 mM.


organism: Amycolatopsis methanolica

source_db: brenda

smiles: CCCCCCCCO

source: brenda


substrate_name: 12-Hydroxydodecanoic acid

smiles: C(CCCCCC(=O)O)CCCCCO

substrate: 12-Hydroxydodecanoic acid


smiles: CCCCCCO


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


smiles: CCCCCO


smiles: CCCCO


smiles: CCCO


substrate_name: ethanol

smiles: CCO

substrate: ethanol


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Oryctolagus cuniculus

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F217S with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N272T with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


organism: Homo sapiens

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

column_label: Table 3 row AKR1C2 / 20alpha-Hydroxyprogesterone; columns kcat, Km, kcat/Km report normalized values kcat=0.00212 s^-1, Km=0.006 mM, kcat/Km=0.35 s^-1*mM^-1.

raw_value_unit_evidence: AKR1C2 / 20alpha-Hydroxyprogesterone; kcat raw_value=2.12 +/- 0.05 x10^-3 s^-1; Km raw_value=6.0 +/- 0.5 uM; kcat/Km raw_value=3.5 x10^2 M^-1 s^-1.

row_label: AKR1C2 / 20alpha-Hydroxyprogesterone

table_label: Table 3. Kinetic constants for hydroxysteroid oxidation catalyzed by the E120H mutant and AKR1C2


column_label: Table 3 row AKR1C2 / 3alpha-Hydroxy-5beta-androstan-17-one; columns kcat, Km, kcat/Km report normalized values kcat=0.014 s^-1, Km=0.029 mM, kcat/Km=0.49 s^-1*mM^-1.

raw_value_unit_evidence: AKR1C2 / 3alpha-Hydroxy-5beta-androstan-17-one; kcat raw_value=14 +/- 1 x10^-3 s^-1; Km raw_value=29.0 +/- 4.2 uM; kcat/Km raw_value=4.9 x10^2 M^-1 s^-1.


column_label: Table 3 row AKR1C2 / 3beta-Hydroxy-5beta-androstan-17-one; columns kcat, Km, kcat/Km report normalized values kcat=0.000183 s^-1, Km=0.0094 mM, kcat/Km=0.02 s^-1*mM^-1.

raw_value_unit_evidence: AKR1C2 / 3beta-Hydroxy-5beta-androstan-17-one; kcat raw_value=0.183 +/- 0.008 x10^-3 s^-1; Km raw_value=9.4 +/- 1.2 uM; kcat/Km raw_value=0.2 x10^2 M^-1 s^-1.


column_label: Table 3 row AKR1C2 / Androsterone; columns kcat, Km, kcat/Km report normalized values kcat=0.0217 s^-1, Km=0.0093 mM, kcat/Km=2.3 s^-1*mM^-1.

raw_value_unit_evidence: AKR1C2 / Androsterone; kcat raw_value=21.7 +/- 0.8 x10^-3 s^-1; Km raw_value=9.3 +/- 0.9 uM; kcat/Km raw_value=23 x10^2 M^-1 s^-1.

row_label: AKR1C2 / Androsterone


column_label: Table 3 row AKR1C2 / 17beta-Estradiol; columns kcat, Km, kcat/Km report normalized values kcat=0.0016 s^-1, Km=0.0062 mM, kcat/Km=0.26 s^-1*mM^-1.

raw_value_unit_evidence: AKR1C2 / 17beta-Estradiol; kcat raw_value=1.6 +/- 0.1 x10^-3 s^-1; Km raw_value=6.2 +/- 1.2 uM; kcat/Km raw_value=2.6 x10^2 M^-1 s^-1.

row_label: AKR1C2 / 17beta-Estradiol


substrate_name: testosterone

column_label: Table 3 row AKR1C2 / Testosterone; columns kcat, Km, kcat/Km report normalized values kcat=0.000348 s^-1, Km=0.0173 mM, kcat/Km=0.02 s^-1*mM^-1.

raw_value_unit_evidence: AKR1C2 / Testosterone; kcat raw_value=0.348 +/- 0.008 x10^-3 s^-1; Km raw_value=17.3 +/- 1.1 uM; kcat/Km raw_value=0.2 x10^2 M^-1 s^-1.

row_label: AKR1C2 / Testosterone

substrate: testosterone


organism: Yamadazyma tenuis

assay_conditions_summary: pH 7; cofactor NADP+


substrate_name: xylitol

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

assay_conditions_summary: pH 7; buffer 50 mM phosphate; cofactor NADPH

column_label: Table 4; row label: xylitol; constant substrate NAD+ (1 mM); kcat(app) column=0.87 s^-1; Km(app) column=257 mM; kcat/Km column=3.39 M^-1 s^-1.

normalized_value_unit_evidence: normalized: kcat=0.87 s^-1; Km=257 mM; explicit table kcat/Km=0.00339 s^-1 mM^-1; CatLog derived kcat/Km=0.003385214007782101 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row xylitol with NAD+ (1 mM): kcat(app)=0.87 s^-1; Km(app)=257 mM; kcat/Km=3.39 M^-1 s^-1.

row_label: Varied substrate xylitol; constant substrate NAD+ (1 mM)

table_label: Table 4: Apparent kinetic constants of ALR from C. tenuis in D-xylose reduction and xylitol oxidation

substrate: xylitol


column_label: Table 4; row label: NAD+; constant substrate xylitol (500 mM); kcat(app) column=0.89 s^-1; Km(app) column=58.7 uM; kcat/Km column=1.52 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: normalized: kcat=0.89 s^-1; Km=0.0587 mM; explicit table kcat/Km=15.2 s^-1 mM^-1; CatLog derived kcat/Km=15.161839863713798 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row NAD+ with xylitol (500 mM): kcat(app)=0.89 s^-1; Km(app)=58.7 uM; kcat/Km=1.52 x 10^4 M^-1 s^-1.

row_label: Varied substrate NAD+; constant substrate xylitol (500 mM)


sequence_source: multiple

assay_conditions_summary: pH 7; cofactor NADPH

source_databases_merged: brenda uniprot


enzyme_display_name: Malate dehydrogenase

organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

substrate_name: oxaloacetate

enzyme: Malate dehydrogenase

substrate: oxaloacetate


assay_conditions_summary: cofactor NAD+


substrate_name: malate

substrate: malate


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: malate dehydrogenase [NAD(P)+]

organism: Methanothermobacter thermautotrophicus

assay_conditions_summary: pH 7.6; cofactor NADH

enzyme: malate dehydrogenase [NAD(P)+]


assay_conditions_summary: pH 7.6; cofactor NADPH


proof_lines:
pH 7.6
at pH 7.6 and 60°C


substrate_name: NAD+

assay_conditions_summary: pH 7.6; cofactor NAD+

substrate: NAD+


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9WYR9 and applied mutation signature N32D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+

column_label: Table 1 (Kinetics parameters of Tm6PGDH and its mutants.), body row 'N32D'; column 'Km (mM)' under coenzyme NAD+ = 4.0; column 'kcat (s^-1)' under coenzyme NAD+ = 29.3; column 'kcat/Km (mM^-1*s^-1)' under coenzyme NAD+ = 7.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 4.0 mM; the column head prints mM, so no conversion is applied and the exported value is 4.0 mM. kcat: printed Table 1 cell 29.3 s^-1; the column head prints s^-1 and no conversion is applied, and the exported value is 29.3 s^(-1). kcat/Km: printed Table 1 cell 7.3 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 7.3 s^(-1)*mM^(-1), while the exported ratio is 7.325.

raw_value_unit_evidence: Table 1, body row 'N32D', coenzyme NAD+ columns: Km = 4.0 mM; kcat = 29.3 s^-1; printed kcat/Km = 7.3 mM^-1*s^-1.

row_label: Table 1, body row 'N32D', coenzyme NAD+ cell group

table_label: Table 1: Kinetics parameters of Tm6PGDH and its mutants. (Scientific Reports 2016, volume 6, article 36311)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N32D/R33I/T34I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N32D/R33L/T34S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N32E/R33I/T34I to reconstruct the assayed variant sequence.


column_label: Table 1, Wide-type row, NAD+ column block: Km (mM)=4.3 +/- 0.4; kcat (s^-1)=23.3 +/- 2.0; kcat/Km (mM^-1*s^-1)=5.4. The printed efficiency cell, not the quotient 23.3/4.3, is authoritative.

raw_value_unit_evidence: Table 1, Wide-type, NAD+: Km 4.3 +/- 0.4 mM; kcat 23.3 +/- 2.0 s^-1; independently printed kcat/Km 5.4 mM^-1*s^-1.

row_label: Wide-type / NAD+

table_label: Table 1: Kinetics parameters of Tm6PGDH and its mutants


enzyme_display_name: Retinol dehydrogenase 16

enzyme: Retinol dehydrogenase 16


assay_conditions_summary: pH 7.3; cofactor NADH

column_label: JBC Table I, kinetic constants of RoDH-4 for steroid substrates; row Dihydrotestosterone; column Km (uM); raw Km 0.80 +/- 0.17 uM.

normalized_value_unit_evidence: Km normalized_value=0.0008 normalized_unit=mM from 0.80 +/- 0.17 uM.

raw_value_unit_evidence: JBC Table I, kinetic constants of RoDH-4 for steroid substrates row Dihydrotestosterone reports Km = 0.80 +/- 0.17 uM.

row_label: Dihydrotestosterone


substrate_name: NAD

assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: JBC Table II, apparent Km values of RoDH-4 for cofactors; row NAD+; column Km (uM); raw Km 0.13 +/- 0.01 uM.

normalized_value_unit_evidence: Km normalized_value=0.00013 normalized_unit=mM from 0.13 +/- 0.01 uM.

raw_value_unit_evidence: JBC Table II, apparent Km values of RoDH-4 for cofactors row NAD+ reports Km = 0.13 +/- 0.01 uM.

row_label: NAD+

substrate: NAD


substrate_name: NADP

assay_conditions_summary: pH 7.3; cofactor NADP+

column_label: JBC Table II, apparent Km values of RoDH-4 for cofactors; row NADP+; column Km (uM); raw Km 190 +/- 17 uM.

normalized_value_unit_evidence: Km normalized_value=0.19 normalized_unit=mM from 190 +/- 17 uM.

raw_value_unit_evidence: JBC Table II, apparent Km values of RoDH-4 for cofactors row NADP+ reports Km = 190 +/- 17 uM.

row_label: NADP+

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


enzyme_display_name: NADPH-dependent conjugated polyketone reductase C2

organism: Candida parapsilosis

substrate_name: ketopantoyl lactone

column_label: Abstract states ketopantoyl lactone is a good substrate with Km = 333 microM.

raw_value_unit_evidence: Km raw_value=333 microM raw_unit=microM

row_label: Ketopantoyl-lactone reductase / ketopantoyl lactone

table_label: PubMed XML abstract

substrate: ketopantoyl lactone


substrate_name: isatin

column_label: Abstract states the Km and Vmax values for isatin were 14 microM and 306 mumol/min per mg protein.

raw_value_unit_evidence: Km raw_value=14 microM raw_unit=microM

row_label: Ketopantoyl-lactone reductase / isatin

enzyme: NADPH-dependent conjugated polyketone reductase C2

substrate: isatin


substrate_name: camphorquinone

substrate: camphorquinone


substrate_name: NADPH

substrate: NADPH


substrate_name: NADH

substrate: NADH


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

organism: Saccharolobus solfataricus

substrate_name: beta-D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T41A to reconstruct the assayed variant sequence.

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

substrate: beta-D-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T41V to reconstruct the assayed variant sequence.


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-Xylose

substrate: D-Xylose


column_label: Table 2 reports wild-type Xylose with NAD+ kcat 61 s^-1; Km 0.25 mM; kcat/Km 245 s^-1 mM^-1

normalized_value_unit_evidence: kcat normalized_value=61 normalized_unit=s^-1; Km normalized_value=0.25 normalized_unit=mM; kcat/Km normalized_value=245 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=61 raw_unit=s^-1; Km raw_value=0.25 raw_unit=mM; kcat/Km raw_value=245 raw_unit=s^-1 mM^-1

row_label: Wild-type Xylose NAD+ row

table_label: PMID 16556607 Table 2


enzyme_display_name: Retinol dehydrogenase 13

substrate_name: all-trans-retinal

column_label: Table 1 row All-trans-retinaldehyde, column Km (uM), gives 3.2 +/- 0.7

row_label: All-trans-retinaldehyde

table_label: Table 1

enzyme: Retinol dehydrogenase 13

substrate: all-trans-retinal


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

column_label: Table 1 row All-trans-retinol, column Km (uM), gives ~3 with footnote a

raw_value_unit_evidence: Km (uM) = ~3 uM

row_label: All-trans-retinol


column_label: Table 1 row NADPH, column Km (uM), gives 1.5 +/- 0.1

row_label: NADPH


enzyme_display_name: (S)-1-phenylethanol dehydrogenase

organism: Azoarcus sp.

substrate_name: acetophenone

assay_conditions_summary: pH 8

enzyme: (S)-1-phenylethanol dehydrogenase

substrate: acetophenone


assay_conditions_summary: pH 8; cofactor NAD+


organism: Scheffersomyces stipitis

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31867 and applied mutation signature K21A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 308.15 K; buffer 50 mM sodium phosphate; cofactor NADPH

column_label: Table 1 (Kinetic parameters of the Pichia stipitis xylose reductase for NADH and NADPH), NADH block, enzyme-form column 'K21A'; row 'Km [mM]' = 0.03; row 'kcat [min-1]' = 282; row 'kcat/Km [mM-1 min-1]' = 8812.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.03 mM; already in mM, so no unit conversion applies; the exported value is 0.03 mM. kcat: printed Table 1 cell 282 min-1; 1 min-1 is 1/60 s^-1, so 282 / 60 = 4.7 s^-1. kcat/Km: printed Table 1 cell 8812 mM-1 min-1; 1 mM-1 min-1 is 1/60 s^-1 mM^-1, so 8812 / 60 = 146.86666666666667 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value this record carries.

raw_value_unit_evidence: Table 1, NADH block, enzyme-form column 'K21A': Km = 0.03 mM; kcat = 282 min-1; printed kcat/Km = 8812 mM-1 min-1.

table_label: Table 1: Kinetic parameters of the Pichia stipitis xylose reductase for NADH and NADPH (Biotechnol Lett 2009, 31(7):1025-1029)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31867 and applied mutation signature K21A/N272D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 308.15 K; buffer 50 mM sodium phosphate; cofactor NADH

column_label: Table 1 (Kinetic parameters of the Pichia stipitis xylose reductase for NADH and NADPH), NADH block, enzyme-form column 'K21A/N272D'; row 'Km [mM]' = 0.01; row 'kcat [min-1]' = 762; row 'kcat/Km [mM-1 min-1]' = 76230.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.01 mM; already in mM, so no unit conversion applies; the exported value is 0.01 mM. kcat: printed Table 1 cell 762 min-1; 1 min-1 is 1/60 s^-1, so 762 / 60 = 12.7 s^-1. kcat/Km: printed Table 1 cell 76230 mM-1 min-1; 1 mM-1 min-1 is 1/60 s^-1 mM^-1, so 76230 / 60 = 1270.5 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value this record carries.

raw_value_unit_evidence: Table 1, NADH block, enzyme-form column 'K21A/N272D': Km = 0.01 mM; kcat = 762 min-1; printed kcat/Km = 76230 mM-1 min-1.


column_label: Table 1 (Kinetic parameters of the Pichia stipitis xylose reductase for NADH and NADPH), NADH block, enzyme-form column 'WT'; row 'Km [mM]' = 0.02; row 'kcat [min-1]' = 785; row 'kcat/Km [mM-1 min-1]' = 36854.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.02 mM; already in mM, so no unit conversion applies; the exported value is 0.02 mM. kcat: printed Table 1 cell 785 min-1; 1 min-1 is 1/60 s^-1, so 785 / 60 = 13.083333333333334 s^-1. kcat/Km: printed Table 1 cell 36854 mM-1 min-1; 1 mM-1 min-1 is 1/60 s^-1 mM^-1, so 36854 / 60 = 614.2333333333333 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value this record carries.

raw_value_unit_evidence: Table 1, NADH block, enzyme-form column 'WT': Km = 0.02 mM; kcat = 785 min-1; printed kcat/Km = 36854 mM-1 min-1.


column_label: Table 1 (Kinetic parameters of the Pichia stipitis xylose reductase for NADH and NADPH), NADPH block, enzyme-form column 'WT'; row 'Km [mM]' = 0.03; row 'kcat [min-1]' = 2416; row 'kcat/Km [mM-1 min-1]' = 95494.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.03 mM; already in mM, so no unit conversion applies; the exported value is 0.03 mM. kcat: printed Table 1 cell 2416 min-1; 1 min-1 is 1/60 s^-1, so 2416 / 60 = 40.266666666666666 s^-1. kcat/Km: printed Table 1 cell 95494 mM-1 min-1; 1 mM-1 min-1 is 1/60 s^-1 mM^-1, so 95494 / 60 = 1591.5666666666666 s^-1 mM^-1, and that printed catalytic-efficiency cell is the value this record carries.

raw_value_unit_evidence: Table 1, NADPH block, enzyme-form column 'WT': Km = 0.03 mM; kcat = 2416 min-1; printed kcat/Km = 95494 mM-1 min-1.


organism: Aromatoleum aromaticum EbN1

substrate_name: Acetophenone

substrate: Acetophenone


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 303.15 K; cofactor NADH


enzyme_display_name: L-2,3-butanediol dehydrogenase

organism: Corynebacterium glutamicum

substrate_name: NADH (at pH 6.0)

assay_conditions_summary: pH 6; cofactor NADH

column_label: Page 2 paragraph and Table 2; Br. saccharolyticum C-1012 column; K_m row NADH; cell 0.10 mM.

normalized_value_unit_evidence: Km=0.10 mM for NADH at pH 6.0.

raw_value_unit_evidence: PDF page 2 OCR lines 99-103: K_m values report NADH/L-AC at pH 6.0 as 0.10/0.44 mM; Table 2 K_m row NADH under Br. saccharolyticum C-1012 = 0.10 mM.

row_label: NADH at pH 6.0; Table 2 K_m row NADH

table_label: Page 2 kinetic-parameter paragraph and Table 2 Comparison of BDHs Isolated from Several Sources

enzyme: L-2,3-butanediol dehydrogenase

substrate: NADH (at pH 6.0)


substrate_name: (S)-acetoin (at pH 6.0)

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

column_label: Page 2 paragraph and Table 2; Br. saccharolyticum C-1012 column; K_m row AC; cell 0.44 mM.

normalized_value_unit_evidence: Km=0.44 mM for (S)-acetoin at pH 6.0.

raw_value_unit_evidence: PDF page 2 OCR lines 99-103: K_m values report NADH/L-AC at pH 6.0 as 0.10/0.44 mM; Table 2 K_m row AC under Br. saccharolyticum C-1012 = 0.44 mM.

row_label: (S)-acetoin / L-AC at pH 6.0; Table 2 K_m row AC

substrate: (S)-acetoin (at pH 6.0)


assay_conditions_summary: pH 10.5; cofactor NAD+

column_label: Page 2 paragraph and Table 2; Br. saccharolyticum C-1012 column; K_m row NAD*; cell 0.07 mM.

normalized_value_unit_evidence: Km=0.07 mM for NAD(+) at pH 10.5.

raw_value_unit_evidence: PDF page 2 OCR lines 99-103: K_m values report NAD+/L-BD at pH 10.5 as 0.07/0.22 mM; Table 2 K_m row NAD* under Br. saccharolyticum C-1012 = 0.07 mM.

row_label: NAD(+) at pH 10.5; Table 2 K_m row NAD*


substrate_name: (S,S)-butane-2,3-diol (at pH 10.5)

smiles: CC(C(C)O)O

column_label: Page 2 paragraph and Table 2; Br. saccharolyticum C-1012 column; K_m row BD; cell 0.22 mM.

normalized_value_unit_evidence: Km=0.22 mM for (S,S)-butane-2,3-diol at pH 10.5.

raw_value_unit_evidence: PDF page 2 OCR lines 99-103: K_m values report NAD+/L-BD at pH 10.5 as 0.07/0.22 mM; Table 2 K_m row BD under Br. saccharolyticum C-1012 = 0.22 mM.

row_label: (S,S)-butane-2,3-diol / L-BD at pH 10.5; Table 2 K_m row BD

substrate: (S,S)-butane-2,3-diol (at pH 10.5)


organism: Chromohalobacter israelensis

assay_conditions_summary: pH 9; cofactor NADPH


assay_conditions_summary: pH 9


substrate_name: NADP+

assay_conditions_summary: pH 9; cofactor NADP+

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V54L with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: Table 2, WT row, 5alpha-DHT columns; assay identity in Methods 2.6.

row_label: WT / 5alpha-DHT


column_label: Table 2, WT row, progesterone columns; assay identity in Methods 2.6.

raw_value_unit_evidence: WT progesterone: kcat 0.21 min^-1; Km 0.84 +/- 0.01 uM; kcat/Km 0.25 min^-1 uM^-1.

row_label: WT / Progesterone


enzyme_display_name: UniProt Q979W2

organism: Thermoplasma volcanium

substrate_name: D-glucose

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=35°C, pH=6.5
Raw SKiD Env: Temp=55°C, pH=6.5

enzyme: UniProt Q979W2

substrate: D-glucose

source: skid


proof_lines:
Raw SKiD Env: Temp=55°C, pH=6.5
Raw SKiD Env: Temp=35°C, pH=6.5


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4; Km column raw 10.5 uM normalized 0.0105 mM; kcat column raw 2.1 min^-1 normalized 0.035 s^-1; kcat/Km column raw 200 min^-1 mM^-1 normalized 3.3333333333333335 s^-1 mM^-1

raw_value_unit_evidence: Km 10.5 uM; kcat 2.1 min^-1; kcat/Km 200 min^-1 mM^-1


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: Table label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3α-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3α-HSD isoforms. Section row: 5α-DHT reduction. Row: AKR1C4 (S). Columns read: Km (µM) cell 3n4p1n0 = 3.4, Vmax (nmoles/min per mg) cell 53n9p2n8 = 53.9, kcat (min−1) cell 1n99 = 1.99, kcat/Km (min−1 mM−1) cell 586. metric: kcat; raw value: 1.99; raw unit: min^-1; normalized value: 0.033 s^(-1); metric: Km; raw value: 3.4; raw unit: uM; normalized value: 0.0034 mM; metric: kcat/Km; raw value: 586; raw unit: min^-1 mM^-1; normalized value: 9.766666666666667 s^-1 mM^-1; explicit printed primary cell; assay condition: Homogeneous recombinant human AKR1C4; ketosteroid reduction monitored spectrophotometrically in 100 mM potassium phosphate (pH 7n0) containing a constant NADPH concentration (200 µM) and 5α-DHT (3n75–75 µM) dissolved in 4 % acetonitrile; all reactions were followed at 340 nm at 25 mC. In the extract's rendering pH 7n0 is pH 7.0 and 25 mC is 25 degrees Celsius = 298.15 K. Export row conditions: pH 7.4; 298.15 K. The temperature agrees; the exported pH 7.4 does not match the paper's stated assay pH 7.0 and is carried over from the OED source record, not from this paper.

normalized_value_unit_evidence: kcat raw 1.99 min^-1 -> 0.033 s^(-1); Km raw 3.4 uM -> 0.0034 mM; explicit printed kcat/Km raw 586 min^-1 mM^-1 -> 9.766666666666667 s^-1 mM^-1. Conversion: 586 min^-1 mM^-1 / 60 = 293/30 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3α-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3α-HSD isoforms | metric header rows of Table 2 as the extract renders them: `                  Km                   Vmax                     kcat        kcat/Km` and `Enzyme            (µM)                 (nmoles/min per mg)      (min−1)     (min−1 mM−1)` | section header row: `5α-DHT reduction` | data row: `  AKR1C4 (S)        3n4p1n0            53n9p2n8                 1n99          586` | the AKR1C4 (S) cells read: Km = 3.4 +/- 1.0 µM; Vmax = 53.9 +/- 2.8 nmoles/min per mg; kcat = 1.99 min−1; kcat/Km = 586 min−1 mM−1.

row_label: 5α-DHT reduction | AKR1C4 (S)


substrate_name: androsterone

column_label: Table 2; row Androsterone oxidation / AKR1C4; columns kcat (min^-1), kcat/Km (min^-1 mM^-1), and Km (microM).

normalized_value_unit_evidence: Converted: kcat=1.39/60=0.02317 s^-1; Km=0.00504 mM; kcat/Km=276/60=4.6 s^-1 mM^-1. Export values 0.023 and 4.563 are supported by printed-value/derived-rounding tolerance from the explicit table cells.

raw_value_unit_evidence: Table 2 reports androsterone oxidation / AKR1C4: Km=5.04 +/- 1.22 microM, kcat=1.39 min^-1, kcat/Km=276 min^-1 mM^-1.

row_label: Androsterone oxidation; AKR1C4

substrate: androsterone


column_label: Table 2; row 5alpha-Androstane-3,17-dione reduction / AKR1C4; columns kcat (min^-1), kcat/Km (min^-1 mM^-1), and Km (microM).

normalized_value_unit_evidence: Converted: kcat=1.79/60=0.02983 s^-1; Km=0.00144 mM; kcat/Km=1243/60=20.7167 s^-1 mM^-1. Export values 0.03 and 20.833 are supported by printed-value/derived-rounding tolerance from the explicit table cells.

raw_value_unit_evidence: Table 2 reports 5alpha-androstane-3,17-dione reduction / AKR1C4: Km=1.44 +/- 0.10 microM, kcat=1.79 min^-1, kcat/Km=1243 min^-1 mM^-1.


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Bos taurus

substrate_name: prostaglandin D2

proof_lines:
prostaglandin D2
carbonyl reduction

enzyme: Aldo-keto reductase family 1 member C3

substrate: prostaglandin D2


substrate_name: menadione

substrate: menadione


assay_conditions_summary: cofactor NADPH

column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / 4-nitrobenzaldehyde; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS 4-nitrobenzaldehyde Km raw_value=8.3 raw_unit=uM

row_label: PGFS / 4-nitrobenzaldehyde


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

organism: Staphylococcus aureus

substrate_name: diacetyl

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

assay_conditions_summary: pH 6

substrate: diacetyl


substrate_name: Methyl pyruvate

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

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

substrate: Methyl pyruvate


substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


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

assay_conditions_summary: pH 7


substrate_name: cyclohexanecarboxaldehyde

substrate: cyclohexanecarboxaldehyde


substrate_name: oenanthaldehyde

smiles: CCCCCCC=O

substrate: oenanthaldehyde


enzyme_display_name: glucose/galactose 1-dehydrogenase

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

assay_conditions_summary: pH 6.5; 328.15 K; cofactor NADP+

proof_lines: pH 6.5, 55°C, wild-type enzyme or mutant enzyme T277F

enzyme: glucose/galactose 1-dehydrogenase


assay_conditions_summary: pH 6.5; 308.15 K; cofactor NADP+

proof_lines: with D-glucose as cosubstrate, at pH 6.5 and 35°C


substrate_name: D-glucopyranose

substrate: D-glucopyranose


proof_lines: with NADP+ as cosubstrate, at pH 6.5 and 35°C


organism: Pseudomonas putida

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


substrate_name: NADPH

km_display: Not reported

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH


substrate_name: NADH

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: D-glucose 6-phosphate

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

proof_lines: pH 8.0, 30°C, recombinant enzyme, with NADP+

proof_lines: pH 8.0, 30°C, recombinant enzyme, with NAD+

substrate: D-glucose 6-phosphate


assay_conditions_summary: cofactor NADH


substrate_name: D-xylose

proof_lines:
cofactor: NADH
cofactor: NADPH

substrate: D-xylose


organism: Deinococcus radiodurans

assay_conditions_summary: pH 7.5; 305.15 K; cofactor NADP+


assay_conditions_summary: pH 7.5; 305.15 K; cofactor NAD+


enzyme_display_name: D-galacturonate reductase

organism: Euglena gracilis

enzyme: D-galacturonate reductase


substrate_name: D-galacturonate

substrate: D-galacturonate


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH


organism: Picrophilus oshimae

substrate_name: NADP+

substrate: NADP+


substrate_name: D-galactose

substrate: D-galactose


substrate_name: Unknown

ki_unit: mM

assay_conditions_summary: pH 6.5; 328.15 K; cofactor ATP

proof_lines: pH 6.5, 55°C, at saturating glucose concentration (50 mM)

substrate: Unknown


organism: Botrytis cinerea

substrate_name: D-glucuronate

proof_lines: isoform GAR1, 10 mM sodium phosphate, pH 7.0, at 22°C

proof_lines: isoform GAR2, 10 mM sodium phosphate, pH 7.0, at 22°C

substrate: D-glucuronate


organism: Leuconostoc mesenteroides

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H240N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; cofactor NADP+

proof_lines: 25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H240N

proof_lines: 25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H240N


assay_conditions_summary: pH 7.6; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D177N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme D177N

proof_lines: 25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme D177N


sequence_variant_note: Mutation signature H1787N references residue 1787, which is outside the resolved sequence length.

proof_lines: 25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H1787N

proof_lines: 25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H1787N


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Q47E 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 Q47E; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 84 uM; kcat cell = 33 100 min^-1; kcat/Km NADP+ cell = 394. captured primary segment: NADP+ | Q47E G6PD, the site-directed Q47E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 84 uM | Table 3 kcat 33 100 min^-1 | Table 3 kcat/Km NADP+ printed cell 394 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row Q47E: Km NADP+ = 84 uM; kcat = 33 100 min^-1; kcat/Km NADP+ = 394 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row Q47E


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Q47A 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 Q47A; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 234 uM; kcat cell = 34 600 min^-1; kcat/Km NAD+ cell = 148. captured primary segment: NAD+ | Q47A G6PD, the site-directed Q47A single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 234 uM | Table 4 kcat 34 600 min^-1 | Table 4 kcat/Km NAD+ printed cell 148 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Q47A: Km NAD+ = 234 uM; kcat = 34 600 min^-1; kcat/Km NAD+ = 148 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Q47A


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 4, enzyme row T14S; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 199 uM; kcat cell = 35 000 min^-1; kcat/Km NAD+ cell = 176. captured primary segment: NAD+ | T14S G6PD, the site-directed T14S single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 199 uM | Table 4 kcat 35 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 176 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row T14S: Km NAD+ = 199 uM; kcat = 35 000 min^-1; kcat/Km NAD+ = 176 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row T14S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K182R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; cofactor NADP+

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182R

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182R


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14A

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature T14A 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 T14A; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 86 uM; kcat cell = 37 900 min^-1; kcat/Km NADP+ cell = 441. captured primary segment: NADP+ | T14A G6PD, the site-directed T14A single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 86 uM | Table 3 kcat 37 900 min^-1 | Table 3 kcat/Km NADP+ printed cell 441 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row T14A: Km NADP+ = 86 uM; kcat = 37 900 min^-1; kcat/Km NADP+ = 441 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row T14A


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

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme R46E

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme R46E


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature R46E 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 R46E; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 21 000 uM; kcat cell = 38 000 min^-1; kcat/Km NADP+ cell = 1.8. captured primary segment: NADP+ | R46E G6PD, the site-directed R46E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 21 000 uM | Table 3 kcat 38 000 min^-1 | Table 3 kcat/Km NADP+ printed cell 1.8 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row R46E: Km NADP+ = 21 000 uM; kcat = 38 000 min^-1; kcat/Km NADP+ = 1.8 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row R46E


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 R46E; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 986 uM; kcat cell = 39 500 min^-1; kcat/Km NAD+ cell = 40. captured primary segment: NAD+ | R46E G6PD, the site-directed R46E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 986 uM | Table 4 kcat 39 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 40 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row R46E: Km NAD+ = 986 uM; kcat = 39 500 min^-1; kcat/Km NAD+ = 40 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row R46E


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

proof_lines: 25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343Q

proof_lines: 25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K343Q 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 K343Q; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 46 uM; kcat cell = 42 700 min^-1; kcat/Km NADP+ cell = 928. captured primary segment: NADP+ | K343Q G6PD, the site-directed K343Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 46 uM | Table 3 kcat 42 700 min^-1 | Table 3 kcat/Km NADP+ printed cell 928 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K343Q: Km NADP+ = 46 uM; kcat = 42 700 min^-1; kcat/Km NADP+ = 928 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row K343Q


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 4, enzyme row K343R; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 338 uM; kcat cell = 45 000 min^-1; kcat/Km NAD+ cell = 133. captured primary segment: NAD+ | K343R G6PD, the site-directed K343R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 338 uM | Table 4 kcat 45 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 133 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row K343R: Km NAD+ = 338 uM; kcat = 45 000 min^-1; kcat/Km NAD+ = 133 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, 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 T14A; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 2340 uM; kcat cell = 48 500 min^-1; kcat/Km NAD+ cell = 21. captured primary segment: NAD+ | T14A G6PD, the site-directed T14A single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 2340 uM | Table 4 kcat 48 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 21 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row T14A: Km NAD+ = 2340 uM; kcat = 48 500 min^-1; kcat/Km NAD+ = 21 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row T14A


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 Q47E; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 310 uM; kcat cell = 48 500 min^-1; kcat/Km NAD+ cell = 156. captured primary segment: NAD+ | Q47E G6PD, the site-directed Q47E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 310 uM | Table 4 kcat 48 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 156 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Q47E: Km NAD+ = 310 uM; kcat = 48 500 min^-1; kcat/Km NAD+ = 156 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Q47E


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 K343Q; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 503 uM; kcat cell = 51 000 min^-1; kcat/Km NAD+ cell = 101. captured primary segment: NAD+ | K343Q G6PD, the site-directed K343Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 503 uM | Table 4 kcat 51 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 101 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row K343Q: Km NAD+ = 503 uM; kcat = 51 000 min^-1; kcat/Km NAD+ = 101 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row K343Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K182R 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 K182R; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 379 uM; kcat cell = 64 100 min^-1; kcat/Km NAD+ cell = 169. captured primary segment: NAD+ | K182R G6PD, the site-directed K182R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 379 uM | Table 4 kcat 64 100 min^-1 | Table 4 kcat/Km NAD+ printed cell 169 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row K182R: Km NAD+ = 379 uM; kcat = 64 100 min^-1; kcat/Km NAD+ = 169 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row K182R


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

proof_lines: 25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21Q

proof_lines: 25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21Q


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

proof_lines: 25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21R

proof_lines: 25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21R


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

proof_lines: 25°C, pH 7.6, cosubstrate: NADP+, wild-type enzyme

proof_lines: wild type enzyme, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C

proof_lines: 25°C, pH 7.6, cosubstrate: NAD+, wild-type enzyme


proof_lines: wild type enzyme, in 33 mM Tris-HCl, pH 7.6, at 25°C


proof_lines: 25°C, pH 7.6, wild-type enzyme, mutant enzyme K121R


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R46Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R46Q, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C

proof_lines: mutant enzyme R46Q, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C


proof_lines: mutant enzyme R46Q, in 33 mM Tris-HCl, pH 7.6, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R46A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R46A, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C

proof_lines: mutant enzyme R46A, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C


proof_lines: mutant enzyme R46A, in 33 mM Tris-HCl, pH 7.6, at 25°C


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


organism: Trichoderma reesei

assay_conditions_summary: pH 7; cofactor NADP+

proof_lines: in 100 mM sodium phosphate (pH 7.0), at 22°C


assay_conditions_summary: pH 7; cofactor NADPH


substrate_name: L-galactonate

assay_conditions_summary: pH 7

substrate: L-galactonate


substrate_name: DL-glyceraldehyde

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

substrate: DL-glyceraldehyde


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


assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, temperature not specified in the publication


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

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADP+

source_databases_merged: brenda skid uniprot


organism: Sphingomonas sp. PAMC 26621

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


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


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


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


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.

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

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


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.

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


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.

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

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+

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)


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

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


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


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.


substrate_name: D-glucose 6-phosphate

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: NAD+


substrate_name: NADP+


enzyme_display_name: UniProt K7ZP76

organism: Paracoccus laeviglucosivorans

enzyme: UniProt K7ZP76


substrate_name: myo-inositol

substrate: myo-inositol


enzyme_display_name: UniProt P0A9V8

organism: Escherichia coli

enzyme: UniProt P0A9V8


enzyme_display_name: sulfolactaldehyde 3-reductase

substrate_name: NADH

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

enzyme: sulfolactaldehyde 3-reductase

substrate: NADH


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

assay_conditions_summary: cofactor NAD+

enzyme: 2-hydroxymethylglutarate dehydrogenase

substrate: NAD+


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

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)