column_label: Table 1, substrate row '5α-DHDOC (Red)', AKR1C1 column group: Km cell = 1.2, kcat cell = 0.56, kcat/Km cell = 0.42. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.56 min^-1 normalizes to 0.009333333333333334 s^-1 (divide by 60); Km raw 1.2 uM normalizes to 0.0012 mM (divide by 1000); kcat/Km = 0.009333333333333334 s^-1 / 0.0012 mM = 7.777777777777778 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.42 min^-1 uM^-1 normalizes to 7.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-DHDOC (Red)'; AKR1C1 column group; Km cell = 1.2 uM; kcat cell = 0.56 min^-1; printed kcat/Km cell = 0.42 min^-1 uM^-1.

row_label: 5α-DHDOC (Red) | AKR1C1 column group


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Homo sapiens

substrate_name: Pregnanediol

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C4 column group: Km cell = 0.2, kcat cell = 1.2, kcat/Km cell = 6.0. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.2 min^-1 normalizes to 0.02 s^-1 (divide by 60); Km raw 0.2 uM normalizes to 0.0002 mM (divide by 1000); kcat/Km = 0.02 s^-1 / 0.0002 mM = 100.0 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 6.0 min^-1 uM^-1 normalizes to 100.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C4 column group; Km cell = 0.2 uM; kcat cell = 1.2 min^-1; printed kcat/Km cell = 6.0 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C4 column group

table_label: Table 1. Comparison of kinetic constants for substrate pairs in the reduction and oxidation catalyzed by human AKR1C isoenzymes

data_origin: experimental

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase

substrate: Pregnanediol

status: verified

source: oed


verification_status: corrected

kcat_over_km_origin: calculated

column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C3 column group: Km cell = 27, kcat cell = 1.7, kcat/Km cell = 0.06. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.7 min^-1 normalizes to 0.028333333333333332 s^-1 (divide by 60); Km raw 27 uM normalizes to 0.027 mM (divide by 1000); kcat/Km = 0.028333333333333332 s^-1 / 0.027 mM = 1.0493827160493827 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.06 min^-1 uM^-1 normalizes to 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C3 column group; Km cell = 27 uM; kcat cell = 1.7 min^-1; printed kcat/Km cell = 0.06 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C3 column group

status: corrected


column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C2 column group: Km cell = 1.0, kcat cell = 0.22, kcat/Km cell = 0.22. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.22 min^-1 normalizes to 0.0036666666666666666 s^-1 (divide by 60); Km raw 1.0 uM normalizes to 0.001 mM (divide by 1000); kcat/Km = 0.0036666666666666666 s^-1 / 0.001 mM = 3.6666666666666665 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.22 min^-1 uM^-1 normalizes to 3.6666666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C2 column group; Km cell = 1.0 uM; kcat cell = 0.22 min^-1; printed kcat/Km cell = 0.22 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C2 column group


column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C1 column group: Km cell = 1.5, kcat cell = 9.6, kcat/Km cell = 6.4. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 9.6 min^-1 normalizes to 0.16 s^-1 (divide by 60); Km raw 1.5 uM normalizes to 0.0015 mM (divide by 1000); kcat/Km = 0.16 s^-1 / 0.0015 mM = 106.66666666666667 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 6.4 min^-1 uM^-1 normalizes to 106.66666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C1 column group; Km cell = 1.5 uM; kcat cell = 9.6 min^-1; printed kcat/Km cell = 6.4 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C1 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C4 column group: Km cell = 1.1, kcat cell = 1.3, kcat/Km cell = 1.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.3 min^-1 normalizes to 0.021666666666666667 s^-1 (divide by 60); Km raw 1.1 uM normalizes to 0.0011 mM (divide by 1000); kcat/Km = 0.021666666666666667 s^-1 / 0.0011 mM = 19.696969696969695 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.2 min^-1 uM^-1 normalizes to 20.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C4 column group; Km cell = 1.1 uM; kcat cell = 1.3 min^-1; printed kcat/Km cell = 1.2 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C4 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C3 column group: Km cell = 2.1, kcat cell = 0.52, kcat/Km cell = 0.25. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.52 min^-1 normalizes to 0.008666666666666666 s^-1 (divide by 60); Km raw 2.1 uM normalizes to 0.0021 mM (divide by 1000); kcat/Km = 0.008666666666666666 s^-1 / 0.0021 mM = 4.126984126984127 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.25 min^-1 uM^-1 normalizes to 4.166666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C3 column group; Km cell = 2.1 uM; kcat cell = 0.52 min^-1; printed kcat/Km cell = 0.25 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C3 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C2 column group: Km cell = 0.5, kcat cell = 0.48, kcat/Km cell = 0.96. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.48 min^-1 normalizes to 0.008 s^-1 (divide by 60); Km raw 0.5 uM normalizes to 0.0005 mM (divide by 1000); kcat/Km = 0.008 s^-1 / 0.0005 mM = 16.0 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.96 min^-1 uM^-1 normalizes to 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C2 column group; Km cell = 0.5 uM; kcat cell = 0.48 min^-1; printed kcat/Km cell = 0.96 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C2 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C1 column group: Km cell = 0.7, kcat cell = 0.6, kcat/Km cell = 0.86. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.6 min^-1 normalizes to 0.01 s^-1 (divide by 60); Km raw 0.7 uM normalizes to 0.0007 mM (divide by 1000); kcat/Km = 0.01 s^-1 / 0.0007 mM = 14.285714285714286 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.86 min^-1 uM^-1 normalizes to 14.333333333333334 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C1 column group; Km cell = 0.7 uM; kcat cell = 0.6 min^-1; printed kcat/Km cell = 0.86 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C1 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C4 column group: Km cell = 1.5, kcat cell = 1.4, kcat/Km cell = 0.93. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.4 min^-1 normalizes to 0.02333333333333333 s^-1 (divide by 60); Km raw 1.5 uM normalizes to 0.0015 mM (divide by 1000); kcat/Km = 0.02333333333333333 s^-1 / 0.0015 mM = 15.555555555555554 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.93 min^-1 uM^-1 normalizes to 15.5 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C4 column group; Km cell = 1.5 uM; kcat cell = 1.4 min^-1; printed kcat/Km cell = 0.93 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C4 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C3 column group: Km cell = 0.9, kcat cell = 1.1, kcat/Km cell = 1.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.1 min^-1 normalizes to 0.018333333333333333 s^-1 (divide by 60); Km raw 0.9 uM normalizes to 0.0009 mM (divide by 1000); kcat/Km = 0.018333333333333333 s^-1 / 0.0009 mM = 20.37037037037037 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.2 min^-1 uM^-1 normalizes to 20.0 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C3 column group; Km cell = 0.9 uM; kcat cell = 1.1 min^-1; printed kcat/Km cell = 1.2 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C3 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C2 column group: Km cell = 0.3, kcat cell = 0.65, kcat/Km cell = 2.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.65 min^-1 normalizes to 0.010833333333333334 s^-1 (divide by 60); Km raw 0.3 uM normalizes to 0.0003 mM (divide by 1000); kcat/Km = 0.010833333333333334 s^-1 / 0.0003 mM = 36.111111111111114 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 2.2 min^-1 uM^-1 normalizes to 36.666666666666664 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C2 column group; Km cell = 0.3 uM; kcat cell = 0.65 min^-1; printed kcat/Km cell = 2.2 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C2 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C1 column group: Km cell = 1.3, kcat cell = 2.2, kcat/Km cell = 1.7. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 2.2 min^-1 normalizes to 0.03666666666666667 s^-1 (divide by 60); Km raw 1.3 uM normalizes to 0.0013 mM (divide by 1000); kcat/Km = 0.03666666666666667 s^-1 / 0.0013 mM = 28.205128205128208 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.7 min^-1 uM^-1 normalizes to 28.333333333333332 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C1 column group; Km cell = 1.3 uM; kcat cell = 2.2 min^-1; printed kcat/Km cell = 1.7 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C1 column group


column_label: Table 1, substrate row '3α,5α-THP (Oxi)', AKR1C4 column group: Km cell = 0.2, kcat cell = 4.0, kcat/Km cell = 20. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 4.0 min^-1 normalizes to 0.06666666666666667 s^-1 (divide by 60); Km raw 0.2 uM normalizes to 0.0002 mM (divide by 1000); kcat/Km = 0.06666666666666667 s^-1 / 0.0002 mM = 333.3333333333333 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 20 min^-1 uM^-1 normalizes to 333.3333333333333 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5α-THP (Oxi)'; AKR1C4 column group; Km cell = 0.2 uM; kcat cell = 4.0 min^-1; printed kcat/Km cell = 20 min^-1 uM^-1.

row_label: 3α,5α-THP (Oxi) | AKR1C4 column group


column_label: Table 1, substrate row '3α,5α-THP (Oxi)', AKR1C2 column group: Km cell = 28, kcat cell = 0.28, kcat/Km cell = 0.01. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.28 min^-1 normalizes to 0.004666666666666667 s^-1 (divide by 60); Km raw 28 uM normalizes to 0.028 mM (divide by 1000); kcat/Km = 0.004666666666666667 s^-1 / 0.028 mM = 0.16666666666666669 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.01 min^-1 uM^-1 normalizes to 0.16666666666666666 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5α-THP (Oxi)'; AKR1C2 column group; Km cell = 28 uM; kcat cell = 0.28 min^-1; printed kcat/Km cell = 0.01 min^-1 uM^-1.

row_label: 3α,5α-THP (Oxi) | AKR1C2 column group


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

organism: Sungouiella intermedia

substrate_name: D-xylose

source_db: brenda

verification_status: unverified

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines:
cosubstrate NADPH, pH 7, 25°C
pH 7, 25°C
cosubstrate NADH, pH 7, 25°C

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

substrate: D-xylose

status: unverified

source: brenda


enzyme_display_name: Aldo-keto reductase family 1 member C2

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of

enzyme: Aldo-keto reductase family 1 member C2

source: uniprot


enzyme_display_name: Aldo-keto reductase family 1 member C3

substrate_name: prostaglandin H2

proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.3

enzyme: Aldo-keto reductase family 1 member C3

substrate: prostaglandin H2


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Oryctolagus cuniculus

substrate_name: 5beta-Pregnane-3,20-dione (at pH7.4)

proof_lines: kcat is 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4).

substrate: 5beta-Pregnane-3,20-dione (at pH7.4)


substrate_name: progesterone (reduction)

substrate: progesterone (reduction)


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

organism: Staphylococcus aureus

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

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


column_label: Table 1, substrate row '3α,5α-THP (Oxi)', AKR1C1 column group: Km cell = 3.3, kcat cell = 0.08, kcat/Km cell = 0.02. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.08 min^-1 normalizes to 0.0013333333333333333 s^-1 (divide by 60); Km raw 3.3 uM normalizes to 0.0033 mM (divide by 1000); kcat/Km = 0.0013333333333333333 s^-1 / 0.0033 mM = 0.40404040404040403 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.02 min^-1 uM^-1 normalizes to 0.3333333333333333 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5α-THP (Oxi)'; AKR1C1 column group; Km cell = 3.3 uM; kcat cell = 0.08 min^-1; printed kcat/Km cell = 0.02 min^-1 uM^-1.

row_label: 3α,5α-THP (Oxi) | AKR1C1 column group


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 1, substrate row '3α,5β-THP (Oxi)', AKR1C4 column group: Km cell = 0.4, kcat cell = 1.6, kcat/Km cell = 4.0. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.6 min^-1 normalizes to 0.02666666666666667 s^-1 (divide by 60); Km raw 0.4 uM normalizes to 0.0004 mM (divide by 1000); kcat/Km = 0.02666666666666667 s^-1 / 0.0004 mM = 66.66666666666667 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 4.0 min^-1 uM^-1 normalizes to 66.66666666666667 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5β-THP (Oxi)'; AKR1C4 column group; Km cell = 0.4 uM; kcat cell = 1.6 min^-1; printed kcat/Km cell = 4.0 min^-1 uM^-1.

row_label: 3α,5β-THP (Oxi) | AKR1C4 column group


column_label: Table 1, substrate row '3α,5β-THP (Oxi)', AKR1C2 column group: Km cell = 2.8, kcat cell = 0.27, kcat/Km cell = 0.10. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.27 min^-1 normalizes to 0.0045000000000000005 s^-1 (divide by 60); Km raw 2.8 uM normalizes to 0.0028 mM (divide by 1000); kcat/Km = 0.0045000000000000005 s^-1 / 0.0028 mM = 1.6071428571428574 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.10 min^-1 uM^-1 normalizes to 1.6666666666666667 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5β-THP (Oxi)'; AKR1C2 column group; Km cell = 2.8 uM; kcat cell = 0.27 min^-1; printed kcat/Km cell = 0.10 min^-1 uM^-1.

row_label: 3α,5β-THP (Oxi) | AKR1C2 column group


column_label: Exact Table 1 row 3α,5β-THP (Oxi), AKR1C1 column group: same-row cells 4.5, 0.36, 0.08; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0045 mM and kcat 0.006 s^-1; current stored precision is 0.005 mM and 0.006 s^-1, whose quotient is 1.2; printed efficiency normalizes to 1.3333333333333333.

raw_value_unit_evidence: Table 1 row 3α,5β-THP (Oxi), AKR1C1: Km 4.5 µM, kcat 0.36 min^-1, printed kcat/Km 0.08 min^-1 µM^-1.

row_label: 3α,5β-THP (Oxi) | AKR1C1 column group


column_label: Exact Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C4 column group: same-row cells 0.2, 4.0, 20; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0002 mM and kcat 0.06666666666666667 s^-1; current stored precision is 0.0002 mM and 0.067 s^-1, whose quotient is 335.0; printed efficiency normalizes to 333.3333333333333.

raw_value_unit_evidence: Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C4: Km 0.2 µM, kcat 4.0 min^-1, printed kcat/Km 20 min^-1 µM^-1.

row_label: 5α-Pregnane-3α,20α-diol (Oxi) | AKR1C4 column group


column_label: Exact Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C2 column group: same-row cells 1.8, 0.19, 0.11; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0018 mM and kcat 0.0031666666666666666 s^-1; current stored precision is 0.002 mM and 0.003 s^-1, whose quotient is 1.5; printed efficiency normalizes to 1.8333333333333333.

raw_value_unit_evidence: Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C2: Km 1.8 µM, kcat 0.19 min^-1, printed kcat/Km 0.11 min^-1 µM^-1.

row_label: 5α-Pregnane-3α,20α-diol (Oxi) | AKR1C2 column group


column_label: Exact Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C1 column group: same-row cells 0.9, 2.2, 2.4; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0009 mM and kcat 0.03666666666666667 s^-1; current stored precision is 0.0009 mM and 0.037 s^-1, whose quotient is 41.11111111111111; printed efficiency normalizes to 40.0.

raw_value_unit_evidence: Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C1: Km 0.9 µM, kcat 2.2 min^-1, printed kcat/Km 2.4 min^-1 µM^-1.

row_label: 5α-Pregnane-3α,20α-diol (Oxi) | AKR1C1 column group


column_label: Exact Table 1 row 3α,5α-THDOC (Oxi), AKR1C4 column group: same-row cells 0.3, 4.2, 14; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0003 mM and kcat 0.07 s^-1; current stored values are identical and their quotient is 233.33333333333337; printed efficiency normalizes to 233.33333333333334.

raw_value_unit_evidence: Table 1 row 3α,5α-THDOC (Oxi), AKR1C4: Km 0.3 µM, kcat 4.2 min^-1, printed kcat/Km 14 min^-1 µM^-1.

row_label: 3α,5α-THDOC (Oxi) | AKR1C4 column group


column_label: Exact Table 1 row 3α,5α-THDOC (Oxi), AKR1C2 column group: same-row cells 6.8, 0.13, 0.02; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0068 mM and kcat 0.0021666666666666666 s^-1; current stored precision is 0.007 mM and 0.002 s^-1, whose quotient is 0.2857142857142857; printed efficiency normalizes to 0.3333333333333333.

raw_value_unit_evidence: Table 1 row 3α,5α-THDOC (Oxi), AKR1C2: Km 6.8 µM, kcat 0.13 min^-1, printed kcat/Km 0.02 min^-1 µM^-1.

row_label: 3α,5α-THDOC (Oxi) | AKR1C2 column group


column_label: Exact Table 1 row 3α,5α-THDOC (Oxi), AKR1C1 column group: same-row cells 2.6, 0.22, 0.08; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0026 mM and kcat 0.003666666666666667 s^-1; current stored precision is 0.003 mM and 0.004 s^-1, whose quotient is 1.3333333333333333 s^-1 mM^-1; printed efficiency normalizes to 1.3333333333333333.

raw_value_unit_evidence: Table 1 row 3α,5α-THDOC (Oxi), AKR1C1: Km 2.6 µM, kcat 0.22 min^-1, printed kcat/Km 0.08 min^-1 µM^-1.

row_label: 3α,5α-THDOC (Oxi) | AKR1C1 column group


enzyme_display_name: zerumbone synthase

organism: Zingiber zerumbet

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S142A to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: zerumbone synthase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y155A to reconstruct the assayed variant sequence.


substrate_name: NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

substrate: NAD+


proof_lines:
Table 1
wild-type ZSD1
NAD+


proof_lines:
Table 1
Y155A
NAD+


organism: [Candida] intermedia

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 5,6-Difluoro (4). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 12, K ROm (mM) cell 4.5, kcat/K ROm (M−1:s−1) cell 2667. captured primary segment: 5,6-Difluoro (4) 18p1.9 1.4p0.6 12 857 (1.1) 15.9 (0.1) 12p1 4.5p1.4 2667 (1.7) 17.1 (1.3). metric: kcat; raw value: 12; raw unit: s^-1; normalized value: 12.0 s^(-1); metric: Km; raw value: 4.5; raw unit: mM; normalized value: 4.5 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 2.6666666666666665 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 5,6-Difluoro (4): kcat 12 s^-1 = 12.0 s^(-1) (no conversion, the paper already prints s^-1); Km 4.5 mM = 4.5 mM (no conversion, the paper already prints mM); kcat/Km 2.6666666666666665 s^-1 mM^-1, the same-row quotient 12 s^-1 / 4.5 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 2667 M^-1:s^-1 is 2667 / 1000 = 2.667 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5,6-Difluoro (4) 18p1.9 1.4p0.6 12 857 (` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5,6-Difluoro (4) 18p1.9 1.4p0.6 12 857 (1.1) 15.9 (0.1) 12p1 4.5p1.4 2667 (1.7) 17.1 (1.3) | Candida intermedia II cells read: kcat = 12 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 4.5 mM; kcat/K ROm = 2667 M^-1:s^-1.

row_label: Candida intermedia II | 5,6-Difluoro (4)


column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 6-Deoxy-5-fluoro (6). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 13, K ROm (mM) cell 8.9, kcat/K ROm (M−1:s−1) cell 1461. captured primary segment: 6-Deoxy-5-fluoro (6) 18p0.5 1.2p0.2 15 000 (1.2) 16.3 (0.5) 13p1 8.9p2.2 1461 (0.9) 15.6 (k0.2). metric: kcat; raw value: 13; raw unit: s^-1; normalized value: 13.0 s^(-1); metric: Km; raw value: 8.9; raw unit: mM; normalized value: 8.9 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 1.4606741573033708 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 6-Deoxy-5-fluoro (6): kcat 13 s^-1 = 13.0 s^(-1) (no conversion, the paper already prints s^-1); Km 8.9 mM = 8.9 mM (no conversion, the paper already prints mM); kcat/Km 1.4606741573033708 s^-1 mM^-1, the same-row quotient 13 s^-1 / 8.9 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 1461 M^-1:s^-1 is 1461 / 1000 = 1.461 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `6-Deoxy-5-fluoro (6) 18p0.5 1.2p0.2 15 0` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 6-Deoxy-5-fluoro (6) 18p0.5 1.2p0.2 15 000 (1.2) 16.3 (0.5) 13p1 8.9p2.2 1461 (0.9) 15.6 (k0.2) | Candida intermedia II cells read: kcat = 13 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 8.9 mM; kcat/K ROm = 1461 M^-1:s^-1.

row_label: Candida intermedia II | 6-Deoxy-5-fluoro (6)


column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 5-Deoxy-6-fluoro (7). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 21, K ROm (mM) cell 14.7, kcat/K ROm (M−1:s−1) cell 1428. captured primary segment: 5-Deoxy-6-fluoro (7) 18p2.8 2.6p1.3 6 923 (0.6) 14.4 (k1.4) 21p5 14.7p7.0 1428 (0.9) 15.5 (k0.2). metric: kcat; raw value: 21; raw unit: s^-1; normalized value: 21.0 s^(-1); metric: Km; raw value: 14.7; raw unit: mM; normalized value: 14.7 mM; metric: kcat/Km; raw value: 1428; raw unit: M^-1:s^-1; normalized value: 1.428 s^-1 mM^-1; primary_cell: true; independently_reported: true; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 5-Deoxy-6-fluoro (7): kcat 21 s^-1 = 21.0 s^(-1) (no conversion, the paper already prints s^-1); Km 14.7 mM = 14.7 mM (no conversion, the paper already prints mM); kcat/Km primary printed kcat/Km cell 1428 M^-1:s^-1; direct unit conversion by division by 1000 gives 1.428 s^-1 mM^-1. Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5-Deoxy-6-fluoro (7) 18p2.8 2.6p1.3 6 92` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5-Deoxy-6-fluoro (7) 18p2.8 2.6p1.3 6 923 (0.6) 14.4 (k1.4) 21p5 14.7p7.0 1428 (0.9) 15.5 (k0.2) | Candida intermedia II cells read: kcat = 21 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 14.7 mM; kcat/K ROm = 1428 M^-1:s^-1.

row_label: Candida intermedia II | 5-Deoxy-6-fluoro (7)


column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 5,6-Dideoxy (8). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 14, K ROm (mM) cell 1.7, kcat/K ROm (M−1:s−1) cell 8235. captured primary segment: 5,6-Dideoxy (8) 18p1.3 0.5p0.3 36 000 (3.0) 18.5 (2.7) 14p1 1.7p0.5 8235 (5.3) 19.9 (4.1). metric: kcat; raw value: 14; raw unit: s^-1; normalized value: 14.0 s^(-1); metric: Km; raw value: 1.7; raw unit: mM; normalized value: 1.7 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 8.23529411764706 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 5,6-Dideoxy (8): kcat 14 s^-1 = 14.0 s^(-1) (no conversion, the paper already prints s^-1); Km 1.7 mM = 1.7 mM (no conversion, the paper already prints mM); kcat/Km 8.23529411764706 s^-1 mM^-1, the same-row quotient 14 s^-1 / 1.7 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 8235 M^-1:s^-1 is 8235 / 1000 = 8.235 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5,6-Dideoxy (8) 18p1.3 0.5p0.3 36 000 (3` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5,6-Dideoxy (8) 18p1.3 0.5p0.3 36 000 (3.0) 18.5 (2.7) 14p1 1.7p0.5 8235 (5.3) 19.9 (4.1) | Candida intermedia II cells read: kcat = 14 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 1.7 mM; kcat/K ROm = 8235 M^-1:s^-1.

row_label: Candida intermedia II | 5,6-Dideoxy (8)


column_label: Table label: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR. Row: 5-Deoxy (1). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 13.5, K ROm (mM) cell 1.3, kcat/K ROm (M−1:s−1) cell 10 384. captured primary segment: 5-Deoxy (1) 18p1 0.9p0.3 (1.0) 20 000 (1.2) 11.2 (0.5) 13.5p0.6 1.3p0.3 (2.0) 10 384 (0.7) 9.7 (k1.0). metric: kcat; raw value: 13.5; raw unit: s^-1; normalized value: 13.5 s^(-1); metric: Km; raw value: 1.3; raw unit: mM; normalized value: 1.3 mM; metric: kcat/Km; raw value: 10 384; raw unit: M^-1:s^-1; normalized value: 10.384 s^-1 mM^-1; primary_cell: true; independently_reported: true; assay condition: Table 2 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 2 row 5-Deoxy (1): kcat 13.5 s^-1 = 13.5 s^(-1) (no conversion, the paper already prints s^-1); Km 1.3 mM = 1.3 mM (no conversion, the paper already prints mM); kcat/Km primary printed kcat/Km cell 10 384 M^-1:s^-1; direct unit conversion by division by 1000 gives 10.384 s^-1 mM^-1. Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5-Deoxy (1) 18p1 0.9p0.3 (1.0) 20 000 (1` is the paper's own printed row.

raw_value_unit_evidence: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: kcat (s ) K ROm (mM) kcat/K ROm (M−1:s−1) k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5-Deoxy (1) 18p1 0.9p0.3 (1.0) 20 000 (1.2) 11.2 (0.5) 13.5p0.6 1.3p0.3 (2.0) 10 384 (0.7) 9.7 (k1.0) | Candida intermedia II cells read: kcat = 13.5 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 1.3 mM; kcat/K ROm = 10 384 M^-1:s^-1.

row_label: Candida intermedia II | 5-Deoxy (1)


column_label: Table label: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR. Row: 5-Fluoro (2). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 15.5, K ROm (mM) cell 2.4, kcat/K ROm (M−1:s−1) cell 6 458. captured primary segment: 5-Fluoro (2) 19p1 0.6p0.4 (0.7) 31 667 (1.9) 12.3 (1.6) 15.5p1.9 2.4p0.8 (3.6) 6 458 (0.4) 8.5 (k2.2). metric: kcat; raw value: 15.5; raw unit: s^-1; normalized value: 15.5 s^(-1); metric: Km; raw value: 2.4; raw unit: mM; normalized value: 2.4 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 6.458333333333334 s^-1 mM^-1; assay condition: Table 2 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 2 row 5-Fluoro (2): kcat 15.5 s^-1 = 15.5 s^(-1) (no conversion, the paper already prints s^-1); Km 2.4 mM = 2.4 mM (no conversion, the paper already prints mM); kcat/Km 6.458333333333334 s^-1 mM^-1, the same-row quotient 15.5 s^-1 / 2.4 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 6 458 M^-1:s^-1 is 6458 / 1000 = 6.458 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5-Fluoro (2) 19p1 0.6p0.4 (0.7) 31 667 (` is the paper's own printed row.

raw_value_unit_evidence: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: kcat (s ) K ROm (mM) kcat/K ROm (M−1:s−1) k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5-Fluoro (2) 19p1 0.6p0.4 (0.7) 31 667 (1.9) 12.3 (1.6) 15.5p1.9 2.4p0.8 (3.6) 6 458 (0.4) 8.5 (k2.2) | Candida intermedia II cells read: kcat = 15.5 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 2.4 mM; kcat/K ROm = 6 458 M^-1:s^-1.

row_label: Candida intermedia II | 5-Fluoro (2)


proof_lines: D-xylose L-arabinose L-idose


substrate_name: D-galactose

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

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

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

row_label: Galactose; Candida intermedia II

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

substrate: D-galactose


substrate_name: oenanthaldehyde

column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: Oenanthaldehyde. Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 4.6, K ROm (mM) cell 4.7, kcat/K ROm (M−1:s−1) cell 979. captured primary segment: Oenanthaldehyde 21p3 5.4p0.6 3 888 – 4.6p0.2 4.7p1.1 979 –. metric: kcat; raw value: 4.6; raw unit: s^-1; normalized value: 4.6 s^(-1); metric: Km; raw value: 4.7; raw unit: mM; normalized value: 4.7 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.978723404255319 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row Oenanthaldehyde: kcat 4.6 s^-1 = 4.6 s^(-1) (no conversion, the paper already prints s^-1); Km 4.7 mM = 4.7 mM (no conversion, the paper already prints mM); kcat/Km 0.978723404255319 s^-1 mM^-1, the same-row quotient 4.6 s^-1 / 4.7 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 979 M^-1:s^-1 is 979 / 1000 = 0.979 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `Oenanthaldehyde 21p3 5.4p0.6 3 888 – 4.6` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: Oenanthaldehyde 21p3 5.4p0.6 3 888 – 4.6p0.2 4.7p1.1 979 – | Candida intermedia II cells read: kcat = 4.6 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 4.7 mM; kcat/K ROm = 979 M^-1:s^-1.

row_label: Candida intermedia II | Oenanthaldehyde

substrate: oenanthaldehyde


substrate_name: D-Xylose

column_label: Official PMC PDF page 3 (journal page 103), Table 2, Xylose row under Candida intermedia II, columns kcat, Km, and kcat/Km.

raw_value_unit_evidence: Table 2, Candida intermedia II, Xylose: kcat=10.5 +/- 0.6 s^-1; Km=50 +/- 5 mM; kcat/Km=210 M^-1 s^-1.

row_label: Xylose; Candida intermedia II

table_label: Table 2. Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR

substrate: D-Xylose


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

organism: Moorella thermoacetica

sequence_variant_note: Resolved canonical sequence from ncbi_genpept_accession:ABC19597.1 and applied mutation signature A30C/R31I/T32K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NAD+

column_label: PMID 27587230 DOI 10.1038/srep32644 Table 2; row A30C/R31I/T32K; NAD+ columns under Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

table_label: Table 2. Kinetics parameters of 6PGDH and mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30D/R31I/T32I to reconstruct the assayed variant sequence.

column_label: Table 2, row 'A30D/R31I/T32I', 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.

table_label: Table 2

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30E/R31I/T32D to reconstruct the assayed variant sequence.

column_label: Table 2, row 'A30E/R31I/T32D', 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2, row 'R31I', 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: R31I / NAD+


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+


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.

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+


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+


organism: Thermochaetoides thermophila

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


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


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


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


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

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


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

smiles: CCCCCCCCO


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


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+

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


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

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.


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

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+


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Homo sapiens

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.


organism: Bos taurus

substrate_name: prostaglandin D2

proof_lines:
prostaglandin D2
carbonyl reduction

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


organism: Staphylococcus aureus

substrate_name: diacetyl

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

assay_conditions_summary: pH 6

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

substrate: diacetyl


substrate_name: Methyl pyruvate

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

substrate: Methyl pyruvate


substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


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

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


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


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