substrate_name: geraniol

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

column_label: Table II, row 'Geraniol', AKR1C34 column group, columns Km, kcat and kcat/Km. All three cells are read from that one printed row: Km 4.1 uM = 0.0041 mM, kcat 1.4 min^-1 = 0.023333333333333334 s^-1, and the row's own printed kcat/Km cell 0.34 min^-1 uM^-1 = 5.666666666666667 s^-1 mM^-1. The exported km 0.0041 mM matches the printed Km cell; the exported kcat 0.023 s^-1 is that printed kcat cell rounded, and the exported kcat_over_km 5.609756097560975 s^-1 mM^-1 is the quotient of the exported rounded cells rather than the paper's own printed ratio cell. Captured paper table segment: Geraniol                                  76               0.92        0.012*             4.1            1.4             0.34

raw_value_unit_evidence: Table II row Geraniol, AKR1C34 column group: Km 4.1 uM; kcat 1.4 min^-1; kcat/Km 0.34 min^-1 uM^-1.

row_label: Geraniol | AKR1C34

substrate: geraniol


organism: Mesocricetus auratus

substrate_name: geranylgeraniol

source_db: oed

verification_status: corrected

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.

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

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table II, row 'Geranylgeraniol', AKR1C34 column group, columns Km, kcat and kcat/Km. All three cells are read from that one printed row: Km 1.0 uM = 0.001 mM, kcat 0.46 min^-1 = 0.007666666666666666 s^-1, and the row's own printed kcat/Km cell 0.46 min^-1 uM^-1 = 7.666666666666667 s^-1 mM^-1. The exported km 0.001 mM matches the printed Km cell; the exported kcat 0.008 s^-1 is that printed kcat cell rounded, and the exported kcat_over_km 8.0 s^-1 mM^-1 is the quotient of the exported rounded cells rather than the paper's own printed ratio cell. Captured paper table segment: Geranylgeraniol                            1.2             2.3         2.0                1.0            0.46            0.46*

raw_value_unit_evidence: Table II row Geranylgeraniol, AKR1C34 column group: Km 1.0 uM; kcat 0.46 min^-1; kcat/Km 0.46 min^-1 uM^-1.

row_label: Geranylgeraniol | AKR1C34

table_label: Table II. Substrate specificity for non-steroidal alcohols

data_origin: experimental

substrate: geranylgeraniol

status: corrected

source: oed


substrate_name: nerol

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

column_label: Table II, row 'Nerol', AKR1C34 column group, columns Km, kcat and kcat/Km. All three cells are read from that one printed row: Km 11 uM = 0.011 mM, kcat 1.4 min^-1 = 0.023333333333333334 s^-1, and the row's own printed kcat/Km cell 0.13 min^-1 uM^-1 = 2.1666666666666665 s^-1 mM^-1. The exported km 0.011 mM matches the printed Km cell; the exported kcat 0.023 s^-1 is that printed kcat cell rounded, and the exported kcat_over_km 2.090909090909091 s^-1 mM^-1 is the quotient of the exported rounded cells rather than the paper's own printed ratio cell. Captured paper table segment: Nerol                                   162*               0.69*       0.004*            11              1.4             0.13

raw_value_unit_evidence: Table II row Nerol, AKR1C34 column group: Km 11 uM; kcat 1.4 min^-1; kcat/Km 0.13 min^-1 uM^-1.

row_label: Nerol | AKR1C34

substrate: nerol


column_label: Table II, row 'R-Tetralol', AKR1C34 column group, columns Km, kcat and kcat/Km. All three cells are read from that one printed row: Km 28 uM = 0.028 mM, kcat 1.3 min^-1 = 0.021666666666666667 s^-1, and the row's own printed kcat/Km cell 0.047 min^-1 uM^-1 = 0.7833333333333333 s^-1 mM^-1. The exported km 0.028 mM matches the printed Km cell; the exported kcat 0.022 s^-1 is that printed kcat cell rounded, and the exported kcat_over_km 0.7857142857142857 s^-1 mM^-1 is the quotient of the exported rounded cells rather than the paper's own printed ratio cell. Captured paper table segment: R-Tetralol                                95               0.45        0.005             28              1.3             0.047

raw_value_unit_evidence: Table II row R-Tetralol, AKR1C34 column group: Km 28 uM; kcat 1.3 min^-1; kcat/Km 0.047 min^-1 uM^-1.

row_label: R-Tetralol | AKR1C34


verification_status: verified

assay_conditions_summary: pH 7.4; 298.15 K; buffer pH 7; cofactor NAD+

column_label: Table II, row 'S-Tetralol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.5 min^-1; kcat/Km 1.0 min^-1 uM^-1; Km 1.5 uM

row_label: S-Tetralol / AKR1C34

table_label: Table II

status: verified


column_label: Table III, row '5beta-Androstane-3alpha,17beta-diol', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

table_label: Table III


column_label: Table III, row '5beta-Androstane-3beta,17beta-diol', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 2.2 min^-1; kcat/Km 0.15 min^-1 uM^-1; Km 15 uM


column_label: Table III, row '5beta-DHT', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

row_label: 5beta-DHT / AKR1C35


column_label: Table III, row '5beta-Pregnane-3beta,21-diol-20-one', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.


kcat_over_km_origin: calculated

column_label: Table III, row '5beta-Pregnan-3beta-ol-20-one', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

row_label: 5beta-Pregnan-3beta-ol-20-one / AKR1C35


column_label: Table II, row 'alpha-3-Hydroxyhexobarbital', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.1 min^-1; kcat/Km 0.078 min^-1 uM^-1; Km 14 uM

row_label: alpha-3-Hydroxyhexobarbital / AKR1C34


column_label: Table II, row 'beta-3-Hydroxyhexobarbital', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.5 min^-1; kcat/Km 0.038 min^-1 uM^-1; Km 40 uM

row_label: beta-3-Hydroxyhexobarbital / AKR1C34


substrate_name: beta-ionol

column_label: Table II, row 'beta-Ionol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.3 min^-1; kcat/Km 1.3 min^-1 uM^-1; Km 1.0 uM

row_label: beta-Ionol / AKR1C34

substrate: beta-ionol


substrate_name: cis-benzene dihydrodiol

column_label: Table II, row 'cis-Benzene dihydrodiol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.5 min^-1; kcat/Km 0.15 min^-1 uM^-1; Km 9.7 uM

row_label: cis-Benzene dihydrodiol / AKR1C34

substrate: cis-benzene dihydrodiol


substrate_name: Cyclohexanol

column_label: Table II, row 'Cyclohexanol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

row_label: Cyclohexanol / AKR1C34

substrate: Cyclohexanol


organism: Rattus norvegicus

substrate_name: Isatin

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, TBER1 column group: Km = 2.2 uM (normalized 0.0022 mM); kcat = 105 min-1 (normalized 1.75 s^-1); kcat/Km = 48 min-1 uM-1 (normalized 800.0 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 105 min-1 / 60 = 1.75 s^-1; the catalog holds 1.75 s^(-1). Km: printed cell 2.2 uM / 1000 = 0.0022 mM; the catalog holds 0.002 mM. kcat/Km: the paper prints the cell 48 min-1 uM-1, which is 48 x 1000 / 60 = 800.0 s^-1 mM^-1; the catalog holds 875.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, TBER1 column group: Km = 2.2 uM; kcat = 105 min-1; kcat/Km = 48 min-1 uM-1.

table_label: Table 1 (journal page 1058) 'Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5', decoded plain-numeral transcription

substrate: Isatin


column_label: table label: Table 2. Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: (E) 16-Ketoestrone (section (E), steroids with dicarbonyl structures); column label: TBER1 Km (uM), TBER1 kcat (min-1) and TBER1 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the Rat 17HSD5 column group and no cell is taken from any other row; raw value: Km 0.4 uM, kcat 113 min-1, kcat/Km 283 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.0004 mM, kcat 1.883 s^-1, kcat/Km 4707.5 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined in the oxidation of (A) 17b-hydroxysteroids and (B) 3a- and 20a-hydroxysteroids, and in the reduction of (C) 3- and 17-ketosteroids, (D) 3- and 20-ketosteroids, and (E) steroids with dicarbonyl structures, using the coenzymes listed in Table 1; this row reads the TBER1 columns, so the coenzyme is NAD(H). Exported assay conditions: pH 7.4, 298.15 K.

normalized_value_unit_evidence: Km 0.4 uM divided by 1000 gives 0.0004 mM at the export's stored precision; exported Km 0.0004 mM. kcat 113 min-1 divided by 60 gives 1.883 s^-1 at the export's stored precision; exported kcat 1.883 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 1.883 s^-1 divided by 0.0004 mM giving 4707.5 s^-1 mM^-1, and of nothing else; exported kcat/Km 4707.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, section (E), steroids with dicarbonyl structures, row (E) 16-Ketoestrone, TBER1 column group: Km 0.4 uM; kcat 113 min-1; kcat/Km 283 min-1 uM-1.

row_label: (E) 16-Ketoestrone


column_label: table label: Table 2. Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: (B) 4-Pregenene-17a,20a-diol-3-one (section (B), oxidation of 3a- and 20a-hydroxysteroids); column label: TBER1 Km (uM), TBER1 kcat (min-1) and TBER1 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the Rat 17HSD5 column group and no cell is taken from any other row; raw value: Km 12 uM, kcat 7.9 min-1, kcat/Km 0.66 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.012 mM, kcat 0.132 s^-1, kcat/Km 11.0 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined in the oxidation of (A) 17b-hydroxysteroids and (B) 3a- and 20a-hydroxysteroids, and in the reduction of (C) 3- and 17-ketosteroids, (D) 3- and 20-ketosteroids, and (E) steroids with dicarbonyl structures, using the coenzymes listed in Table 1; this row reads the TBER1 columns, so the coenzyme is NAD(H). Exported assay conditions: pH 7.4, 298.15 K.

normalized_value_unit_evidence: Km 12 uM divided by 1000 gives 0.012 mM at the export's stored precision; exported Km 0.012 mM. kcat 7.9 min-1 divided by 60 gives 0.132 s^-1 at the export's stored precision; exported kcat 0.132 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.132 s^-1 divided by 0.012 mM giving 11.0 s^-1 mM^-1, and of nothing else; exported kcat/Km 11.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, section (B), oxidation of 3a- and 20a-hydroxysteroids, row (B) 4-Pregenene-17a,20a-diol-3-one, TBER1 column group: Km 12 uM; kcat 7.9 min-1; kcat/Km 0.66 min-1 uM-1.

row_label: (B) 4-Pregenene-17a,20a-diol-3-one


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (D), printed row 1, substrate `17a-Hydroxyprogesterone`, TBER1 column group: Km = 2.5 uM (normalized 0.0025 mM); kcat = 2.5 min-1 (normalized 0.041666666666666664 s^-1); kcat/Km = 1.0 min-1 uM-1 (normalized 16.666666666666668 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 2.5 min-1 / 60 = 0.041666666666666664 s^-1; the catalog holds 0.042 s^(-1). Km: printed cell 2.5 uM / 1000 = 0.0025 mM; the catalog holds 0.003 mM. kcat/Km: the paper prints the cell 1.0 min-1 uM-1, which is 1.0 x 1000 / 60 = 16.666666666666668 s^-1 mM^-1; the catalog holds 14.0 s^(-1)*mM^(-1).

table_label: Table 2 (journal page 1058) 'Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5', decoded plain-numeral transcription


column_label: table label: Table 2. Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: 4-Pregenen-20a-ol-3-one (section (B), oxidation of 3a- and 20a-hydroxysteroids); column label: TBER1 Km (uM), TBER1 kcat (min-1) and TBER1 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the Rat 17HSD5 column group and no cell is taken from any other row; raw value: Km 8.1 uM, kcat 3.2 min-1, kcat/Km 0.39 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.008 mM, kcat 0.053 s^-1, kcat/Km 6.625 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined in the oxidation of (A) 17b-hydroxysteroids and (B) 3a- and 20a-hydroxysteroids, and in the reduction of (C) 3- and 17-ketosteroids, (D) 3- and 20-ketosteroids, and (E) steroids with dicarbonyl structures, using the coenzymes listed in Table 1; this row reads the TBER1 columns, so the coenzyme is NAD(H). Exported assay conditions: pH 7.4, 298.15 K.

normalized_value_unit_evidence: Km 8.1 uM divided by 1000 gives 0.008 mM at the export's stored precision; exported Km 0.008 mM. kcat 3.2 min-1 divided by 60 gives 0.053 s^-1 at the export's stored precision; exported kcat 0.053 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.053 s^-1 divided by 0.008 mM giving 6.625 s^-1 mM^-1, and of nothing else; exported kcat/Km 6.625 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, section (B), oxidation of 3a- and 20a-hydroxysteroids, row 4-Pregenen-20a-ol-3-one, TBER1 column group: Km 8.1 uM; kcat 3.2 min-1; kcat/Km 0.39 min-1 uM-1.


column_label: table label: Table 2. Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: 5a-Pregnan-20a-ol-3-one (section (B), oxidation of 3a- and 20a-hydroxysteroids); column label: TBER1 Km (uM), TBER1 kcat (min-1) and TBER1 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the Rat 17HSD5 column group and no cell is taken from any other row; raw value: Km 5.1 uM, kcat 2.4 min-1, kcat/Km 0.47 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.005 mM, kcat 0.04 s^-1, kcat/Km 8.0 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined in the oxidation of (A) 17b-hydroxysteroids and (B) 3a- and 20a-hydroxysteroids, and in the reduction of (C) 3- and 17-ketosteroids, (D) 3- and 20-ketosteroids, and (E) steroids with dicarbonyl structures, using the coenzymes listed in Table 1; this row reads the TBER1 columns, so the coenzyme is NAD(H). Exported assay conditions: pH 7.4, 298.15 K.

normalized_value_unit_evidence: Km 5.1 uM divided by 1000 gives 0.005 mM at the export's stored precision; exported Km 0.005 mM. kcat 2.4 min-1 divided by 60 gives 0.04 s^-1 at the export's stored precision; exported kcat 0.04 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.04 s^-1 divided by 0.005 mM giving 8.0 s^-1 mM^-1, and of nothing else; exported kcat/Km 8.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, section (B), oxidation of 3a- and 20a-hydroxysteroids, row 5a-Pregnan-20a-ol-3-one, TBER1 column group: Km 5.1 uM; kcat 2.4 min-1; kcat/Km 0.47 min-1 uM-1.


column_label: table label: Table 2. Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: 5b-Pregnan-20a-ol-3-one (section (D), reduction of 3- and 20-ketosteroids); column label: TBER1 Km (uM), TBER1 kcat (min-1) and TBER1 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the Rat 17HSD5 column group and no cell is taken from any other row; raw value: Km 19 uM, kcat 1.0 min-1, kcat/Km 0.05 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.019 mM, kcat 0.017 s^-1, kcat/Km 0.8947368421052633 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined in the oxidation of (A) 17b-hydroxysteroids and (B) 3a- and 20a-hydroxysteroids, and in the reduction of (C) 3- and 17-ketosteroids, (D) 3- and 20-ketosteroids, and (E) steroids with dicarbonyl structures, using the coenzymes listed in Table 1; this row reads the TBER1 columns, so the coenzyme is NAD(H). Exported assay conditions: pH 7.4, 298.15 K.

normalized_value_unit_evidence: Km 19 uM divided by 1000 gives 0.019 mM at the export's stored precision; exported Km 0.019 mM. kcat 1.0 min-1 divided by 60 gives 0.017 s^-1 at the export's stored precision; exported kcat 0.017 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.017 s^-1 divided by 0.019 mM giving 0.8947368421052633 s^-1 mM^-1, and of nothing else; exported kcat/Km 0.8947368421052633 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, section (D), reduction of 3- and 20-ketosteroids, row 5b-Pregnan-20a-ol-3-one, TBER1 column group: Km 19 uM; kcat 1.0 min-1; kcat/Km 0.05 min-1 uM-1.


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (E), printed row 2, substrate `21-Dehydrocortisol`, TBER1 column group: Km = 4.5 uM (normalized 0.0045000000000000005 mM); kcat = 23 min-1 (normalized 0.3833333333333333 s^-1); kcat/Km = 5.1 min-1 uM-1 (normalized 85.0 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 23 min-1 / 60 = 0.3833333333333333 s^-1; the catalog holds 0.383 s^(-1). Km: printed cell 4.5 uM / 1000 = 0.0045000000000000005 mM; the catalog holds 0.005 mM. kcat/Km: the paper prints the cell 5.1 min-1 uM-1, which is 5.1 x 1000 / 60 = 85.0 s^-1 mM^-1; the catalog holds 76.6 s^(-1)*mM^(-1).


smiles: CCC(C)=O

column_label: table label: Table 1. Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: 2,3-Pentanedione (Reduction block); column label: TBER1 Km (uM), TBER1 kcat (min-1) and TBER1 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the Rat 17HSD5 column group and no cell is taken from any other row; raw value: Km 385 uM, kcat 29 min-1, kcat/Km 0.08 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.385 mM, kcat 0.483 s^-1, kcat/Km 1.2545454545454544 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined at pH 7.4 with NAD(H) for TBER1 and with NADP(H) for rat 17HSD5 as the coenzyme; this row reads the TBER1 columns, so the coenzyme is NAD(H). Exported assay conditions: pH 7.4, 298.15 K.

normalized_value_unit_evidence: Km 385 uM divided by 1000 gives 0.385 mM at the export's stored precision; exported Km 0.385 mM. kcat 29 min-1 divided by 60 gives 0.483 s^-1 at the export's stored precision; exported kcat 0.483 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.483 s^-1 divided by 0.385 mM giving 1.2545454545454544 s^-1 mM^-1, and of nothing else; exported kcat/Km 1.2545454545454544 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Reduction block, row 2,3-Pentanedione, TBER1 column group: Km 385 uM; kcat 29 min-1; kcat/Km 0.08 min-1 uM-1.


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 3, substrate `5b-Androstan-3a-ol-17-one`, TBER1 column group: Km = 42 uM (normalized 0.042 mM); kcat = 6.6 min-1 (normalized 0.10999999999999999 s^-1); kcat/Km = 0.16 min-1 uM-1 (normalized 2.666666666666667 s^-1 mM^-1).


column_label: PMID 16788056 Table 2, steroid substrates; row 5b-Pregnan-3a-ol-20-one; TBER1 Km/kcat/kcat/Km columns; raw Km 8.4 uM, kcat 0.83 min^-1, kcat/Km 0.10 min^-1 uM^-1.

row_label: 5b-Pregnan-3a-ol-20-one / TBER1


column_label: PMID 16788056 Table 2, steroid substrates; row 4-Androsten-3a-ol-17-one; TBER1 Km/kcat/kcat/Km columns; raw Km 14 uM, kcat 3.6 min^-1, kcat/Km 0.25 min^-1 uM^-1.

raw_value_unit_evidence: Km 14 uM; kcat 3.6 min^-1; kcat/Km 0.25 min^-1 uM^-1

row_label: 4-Androsten-3a-ol-17-one / TBER1


verification_status: unverified

status: unverified


column_label: PMID 16788056 Table 2, steroid substrates; row 5a-Dihydrotestosterone; TBER1 Km/kcat/kcat/Km columns; raw Km 9.1 uM, kcat 12 min^-1, kcat/Km 1.30 min^-1 uM^-1.

raw_value_unit_evidence: Km 9.1 uM; kcat 12 min^-1; kcat/Km 1.30 min^-1 uM^-1

row_label: 5a-Dihydrotestosterone / TBER1


column_label: PMID 16788056 Table 2, steroid substrates; row 5a-Androstane-3a,17b-diol; TBER1 Km/kcat/kcat/Km columns; raw Km 17 uM, kcat 4.2 min^-1, kcat/Km 0.25 min^-1 uM^-1.

raw_value_unit_evidence: Km 17 uM; kcat 4.2 min^-1; kcat/Km 0.25 min^-1 uM^-1

row_label: 5a-Androstane-3a,17b-diol / TBER1


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (D), printed row 2, substrate `5b-Pregnane-3,20-dione`, TBER1 column group: Km = 1.6 uM (normalized 0.0016 mM); kcat = 0.78 min-1 (normalized 0.013 s^-1); kcat/Km = 0.49 min-1 uM-1 (normalized 8.166666666666668 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 0.78 min-1 / 60 = 0.013 s^-1; the catalog holds 0.013 s^(-1). Km: printed cell 1.6 uM / 1000 = 0.0016 mM; the catalog holds 0.002 mM. kcat/Km: the paper prints the cell 0.49 min-1 uM-1, which is 0.49 x 1000 / 60 = 8.166666666666668 s^-1 mM^-1; the catalog holds 6.5 s^(-1)*mM^(-1).


column_label: PMID 16788056 Table 1, non-steroidal substrates; row TBE; TBER1 Km/kcat/kcat/Km columns; raw Km 180 uM, kcat 75 min^-1, kcat/Km 0.42 min^-1 uM^-1.

raw_value_unit_evidence: Km 180 uM; kcat 75 min^-1; kcat/Km 0.42 min^-1 uM^-1

row_label: TBE / TBER1


enzyme_display_name: TBER1 / novel rat cytoplasmic 17beta-hydroxysteroid dehydrogenase

substrate_name: 9alpha,11beta-Prostaglandin F2

column_label: PMID 16788056 Table 1, non-steroidal substrates; row 9a,11b-PGF2; TBER1 Km/kcat/kcat/Km columns; raw Km 24 uM, kcat 0.15 min^-1, kcat/Km 0.006 min^-1 uM^-1.

row_label: 9a,11b-PGF2 / TBER1

substrate: 9alpha,11beta-Prostaglandin F2


column_label: PMID 16788056 Table 1, non-steroidal substrates; row a-3-Hydroxyhexobarbital; TBER1 Km/kcat/kcat/Km columns; raw Km 420 uM, kcat 17 min^-1, kcat/Km 0.04 min^-1 uM^-1.

raw_value_unit_evidence: Km 420 uM; kcat 17 min^-1; kcat/Km 0.04 min^-1 uM^-1

row_label: a-3-Hydroxyhexobarbital / TBER1

enzyme: TBER1 / novel rat cytoplasmic 17beta-hydroxysteroid dehydrogenase


column_label: PMID 16788056 Table 1, non-steroidal substrates; row b-3-Hydroxyhexobarbital; TBER1 Km/kcat/kcat/Km columns; raw Km 1180 uM, kcat 7.2 min^-1, kcat/Km 0.006 min^-1 uM^-1.

row_label: b-3-Hydroxyhexobarbital / TBER1


column_label: PMID 16788056 Table 1, non-steroidal substrates; row 2-Cyclohexen-1-ol; TBER1 Km/kcat/kcat/Km columns; raw Km 1500 uM, kcat 26 min^-1, kcat/Km 0.02 min^-1 uM^-1.

raw_value_unit_evidence: Km 1500 uM; kcat 26 min^-1; kcat/Km 0.02 min^-1 uM^-1

row_label: 2-Cyclohexen-1-ol / TBER1


substrate_name: Dimethylglyoxal

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

column_label: PMID 16788056 Table 1, non-steroidal substrates; row 2,3-Butanedione; TBER1 Km/kcat/kcat/Km columns; raw Km 4800 uM, kcat 100 min^-1, kcat/Km 0.02 min^-1 uM^-1.

row_label: 2,3-Butanedione / TBER1

substrate: Dimethylglyoxal


column_label: PMID 16788056 Table 2, steroid substrates; row 17b-Estradiol; TBER1 Km/kcat/kcat/Km columns; raw Km 33 uM, kcat 9.0 min^-1, kcat/Km 0.27 min^-1 uM^-1.

raw_value_unit_evidence: Km 33 uM; kcat 9.0 min^-1; kcat/Km 0.27 min^-1 uM^-1

row_label: 17b-Estradiol / TBER1


substrate_name: p-Nitrobenzaldehyde

column_label: PMID 16788056 Table 1, non-steroidal substrates; row 4-Nitrobenzaldehyde; TBER1 Km/kcat/kcat/Km columns; raw Km 96 uM, kcat 18 min^-1, kcat/Km 0.20 min^-1 uM^-1.

raw_value_unit_evidence: Km 96 uM; kcat 18 min^-1; kcat/Km 0.20 min^-1 uM^-1

row_label: 4-Nitrobenzaldehyde / TBER1

substrate: p-Nitrobenzaldehyde


column_label: PMID 16788056 Table 1, non-steroidal substrates; row S-Tetralol; TBER1 Km/kcat/kcat/Km columns; raw Km 168 uM, kcat 45 min^-1, kcat/Km 0.27 min^-1 uM^-1.

raw_value_unit_evidence: Km 168 uM; kcat 45 min^-1; kcat/Km 0.27 min^-1 uM^-1

row_label: S-Tetralol / TBER1


column_label: PMID 16788056 Table 1, non-steroidal substrates; row S-Indan-1-ol; TBER1 Km/kcat/kcat/Km columns; raw Km 134 uM, kcat 25 min^-1, kcat/Km 0.19 min^-1 uM^-1.

raw_value_unit_evidence: Km 134 uM; kcat 25 min^-1; kcat/Km 0.19 min^-1 uM^-1

row_label: S-Indan-1-ol / TBER1


column_label: PMID 16788056 Table 1, non-steroidal substrates; row trans-Benzene dihydrodiol; TBER1 Km/kcat/kcat/Km columns; raw Km 215 uM, kcat 38 min^-1, kcat/Km 0.18 min^-1 uM^-1.

raw_value_unit_evidence: Km 215 uM; kcat 38 min^-1; kcat/Km 0.18 min^-1 uM^-1

row_label: trans-Benzene dihydrodiol / TBER1


organism: Leuconostoc mesenteroides

substrate_name: NADP+

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

mutation_type: substitution

assay_conditions_summary: pH 7.6; 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 Y415F; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 6.3 uM; kcat cell = 11 000 min^-1; kcat/Km NADP+ cell = 1750. captured primary segment: NADP+ | Y415F G6PD, the site-directed Y415F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 6.3 uM | Table 3 kcat 11 000 min^-1 | Table 3 kcat/Km NADP+ printed cell 1750 under the column head kcat/Km NADP+ (min^-1 uM^-1)

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

row_label: Table 3, enzyme row Y415F

substrate: NADP+


substrate_name: glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R46E with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines:
R46E
D-glucose 6-phosphate
Leuconostoc mesenteroides

substrate: glucose 6-phosphate


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


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

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row K182Q; columns Km G6P (uM), kcat (min^-1) and kcat/Km G6P (min^-1 uM^-1); Km G6P cell = 13 100 uM; kcat cell = 18 500 min^-1; kcat/Km G6P cell = 1.4. captured primary segment: glucose 6-phosphate | K182Q G6PD, the site-directed K182Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km G6P 13 100 uM | Table 3 kcat 18 500 min^-1 | Table 3 kcat/Km G6P printed cell 1.4 under the column head kcat/Km G6P (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K182Q: Km G6P = 13 100 uM; kcat = 18 500 min^-1; kcat/Km G6P = 1.4 under the printed column head kcat/Km G6P (min^-1 uM^-1).

row_label: Table 3, enzyme row K182Q


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K343Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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


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

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row P149V; columns Km G6P (uM), kcat (min^-1) and kcat/Km G6P (min^-1); Km G6P cell = 1730 uM; kcat cell = 166 min^-1; kcat/Km G6P cell = 0.10. captured primary segment: glucose 6-phosphate | P149V G6PD, the site-directed P149V single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km G6P 1730 uM | Table 4 kcat 166 min^-1 | Table 4 kcat/Km G6P printed cell 0.10 under the column head kcat/Km G6P (min^-1), whose uM^-1 the printed head omits although every cell of the column is a kcat/Km in min^-1 uM^-1 (section 6)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row P149V: Km G6P = 1730 uM; kcat = 166 min^-1; kcat/Km G6P = 0.10 under the printed column head kcat/Km G6P (min^-1).

row_label: Table 4, enzyme row P149V


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 7.6; 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 (printed with footnote marker d: apparent kinetic values); Table 4, columns Km G6P (uM), kcat (min^-1) and kcat/Km G6P (min^-1); Km G6P cell = 96 uM; kcat cell = 34 600 min^-1; kcat/Km G6P cell = 360. captured primary segment: glucose 6-phosphate | 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 G6P 96 uM | Table 4 kcat 34 600 min^-1 | Table 4 kcat/Km G6P printed cell 360 under the column head kcat/Km G6P (min^-1), whose uM^-1 the printed head omits although every cell of the column is a kcat/Km in min^-1 uM^-1 (section 6)

normalized_value_unit_evidence: Km: printed Km G6P cell 96 uM; 1 uM = 1/1000 mM, so 96 / 1000 = 0.096 mM; the export stores 0.096 mM, the same value. kcat: printed cell 34 600 min^-1; the printed turnover column is per MINUTE, so 34 600 / 60 = 576.6666666666666 s^(-1); the export stores 0.567 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km G6P cell 360 under the column head kcat/Km G6P (min^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 360 x 16.666666666666668 = 6000.0 s^(-1)*mM^(-1). The export stores 6000.0 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Q47A (printed with footnote marker d: apparent kinetic values): Km G6P = 96 uM; kcat = 34 600 min^-1; kcat/Km G6P = 360 under the printed column head kcat/Km G6P (min^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T14A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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

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

normalized_value_unit_evidence: Km: printed Km NADP+ cell 8.0 uM; 1 uM = 1/1000 mM, so 8.0 / 1000 = 0.008 mM; the export stores 0.008 mM, the same value. kcat: printed cell 24 200 min^-1; the printed turnover column is per MINUTE, so 24 200 / 60 = 403.3333333333333 s^(-1); the export stores 0.4 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 2030 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 2030 x 16.666666666666668 = 33833.333333333336 s^(-1)*mM^(-1). The export stores 33833.333333333336 s^(-1)*mM^(-1), the same value.

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

row_label: Table 3, enzyme row K343R


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

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

normalized_value_unit_evidence: Km: printed Km NADP+ cell 14 uM; 1 uM = 1/1000 mM, so 14 / 1000 = 0.014 mM; the export stores 0.014 mM, the same value. kcat: printed cell 22 700 min^-1; the printed turnover column is per MINUTE, so 22 700 / 60 = 378.3333333333333 s^(-1); the export stores 0.367 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 1620 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 1620 x 16.666666666666668 = 27000.000000000004 s^(-1)*mM^(-1). The export stores 27000.0 s^(-1)*mM^(-1), the same value.

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

row_label: Table 3, enzyme row T14S


substrate_name: NAD+

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

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

normalized_value_unit_evidence: Km: printed Km NAD+ cell 571 uM; 1 uM = 1/1000 mM, so 571 / 1000 = 0.571 mM; the export stores 0.571 mM, the same value. kcat: printed cell 12 500 min^-1; the printed turnover column is per MINUTE, so 12 500 / 60 = 208.33333333333334 s^(-1); the export stores 0.2 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NAD+ cell 22 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 22 x 16.666666666666668 = 366.6666666666667 s^(-1)*mM^(-1). The export stores 366.6666666666667 s^(-1)*mM^(-1), the same value.

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

row_label: Table 4, enzyme row D374Q

substrate: NAD+


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


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; Table 4, 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)

normalized_value_unit_evidence: Km: printed Km NAD+ cell 379 uM; 1 uM = 1/1000 mM, so 379 / 1000 = 0.379 mM; the export stores 0.379 mM, the same value. kcat: printed cell 64 100 min^-1; the printed turnover column is per MINUTE, so 64 100 / 60 = 1068.3333333333333 s^(-1); the export stores 1.067 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NAD+ cell 169 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 169 x 16.666666666666668 = 2816.666666666667 s^(-1)*mM^(-1). The export stores 2816.6666666666665 s^(-1)*mM^(-1), the same value.

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_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 4, enzyme row K343Q; Table 4, 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)

normalized_value_unit_evidence: Km: printed Km NAD+ cell 503 uM; 1 uM = 1/1000 mM, so 503 / 1000 = 0.503 mM; the export stores 0.503 mM, the same value. kcat: printed cell 51 000 min^-1; the printed turnover column is per MINUTE, so 51 000 / 60 = 850.0 s^(-1); the export stores 0.85 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NAD+ cell 101 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 101 x 16.666666666666668 = 1683.3333333333335 s^(-1)*mM^(-1). The export stores 1683.3333333333333 s^(-1)*mM^(-1), the same value.

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


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; Table 4, 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)

normalized_value_unit_evidence: Km: printed Km NAD+ cell 338 uM; 1 uM = 1/1000 mM, so 338 / 1000 = 0.338 mM; the export stores 0.338 mM, the same value. kcat: printed cell 45 000 min^-1; the printed turnover column is per MINUTE, so 45 000 / 60 = 750.0 s^(-1); the export stores 0.75 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NAD+ cell 133 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 133 x 16.666666666666668 = 2216.666666666667 s^(-1)*mM^(-1). The export stores 2216.6666666666665 s^(-1)*mM^(-1), the same value.

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


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.

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; Table 3, 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)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 84 uM; 1 uM = 1/1000 mM, so 84 / 1000 = 0.084 mM; the export stores 0.084 mM, the same value. kcat: printed cell 33 100 min^-1; the printed turnover column is per MINUTE, so 33 100 / 60 = 551.6666666666666 s^(-1); the export stores 0.55 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 394 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 394 x 16.666666666666668 = 6566.666666666667 s^(-1)*mM^(-1). The export stores 6566.666666666667 s^(-1)*mM^(-1), the same value.

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 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


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.


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

proof_lines: PMID 11106479 names T14A, not the row's T14S substitution

proof_lines: The row context warns T14S cannot be applied safely to the resolved sequence


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

proof_lines: PMID 11106479 explicitly includes Y415F in the mutant panel

proof_lines: The row context flags the Y415F sequence mapping as unsafe


organism: Homo sapiens

substrate_name: chenodeoxycholate

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

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table 2, row Chenodeoxycholic acid / DD4, columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 2 Chenodeoxycholic acid / DD4 reports kcat 1.9 min^-1 and Km 1.1 uM; kcat/Km is not printed as a column and is derived from those same-row cells.

row_label: Chenodeoxycholic acid / DD4

table_label: Table 2. Stereospecificity in the oxidation of xenobiotic alcohols and steroids by the two human liver dehydrogenases

substrate: chenodeoxycholate


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: Table 3. Substrate specificity for carbonyl compounds, row 5beta-Androstane-3,17-dione, columns DD4 kcat (min^-1) and DD4 Km (uM); both metrics are taken from the one same printed row and the one same DD4 column pair; kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 3. Substrate specificity for carbonyl compounds, printed row 5beta-Androstane-3,17-dione, DD4 columns: kcat 4.8 min^-1 and Km 0.6 uM; kcat/Km is derived from those same-row DD4 cells.

row_label: 5beta-Androstane-3,17-dione / DD4


column_label: Table 2, row 5beta-Androstane-3alpha,17beta-diol / DD4, columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 2 5beta-Androstane-3alpha,17beta-diol / DD4 reports kcat 7.6 min^-1 and Km 1.3 uM; kcat/Km is not printed as a column and is derived from those same-row cells.


substrate_name: Benzene dihydrodiol

substrate: Benzene dihydrodiol


substrate_name: Camphorquinone

column_label: Table 3. Substrate specificity for carbonyl compounds, row Camphorquinone, columns DD4 kcat (min^-1) and DD4 Km (uM); both metrics are taken from the one same printed row and the one same DD4 column pair; kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 3. Substrate specificity for carbonyl compounds, printed row Camphorquinone, DD4 columns: kcat 8.1 min^-1 and Km 0.6 uM; kcat/Km is derived from those same-row DD4 cells.

row_label: Camphorquinone / DD4

substrate: Camphorquinone


column_label: Table 3, row Butane-2,3-dione / DD4, columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 3 Butane-2,3-dione / DD4 reports kcat 4.0 min^-1 and Km 6.5 uM; kcat/Km is not printed as a column and is derived from those same-row cells.

row_label: Butane-2,3-dione / DD4

table_label: Table 3. Substrate specificity for carbonyl compounds


substrate_name: m-Nitrobenzaldehyde

column_label: Table 3. Substrate specificity for carbonyl compounds, row 3-Nitrobenzaldehyde, columns DD4 kcat (min^-1) and DD4 Km (uM); both metrics are taken from the one same printed row and the one same DD4 column pair; kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 3. Substrate specificity for carbonyl compounds, printed row 3-Nitrobenzaldehyde, DD4 columns: kcat 2.1 min^-1 and Km 17 uM; kcat/Km is derived from those same-row DD4 cells.

row_label: 3-Nitrobenzaldehyde / DD4

substrate: m-Nitrobenzaldehyde


column_label: Table 3, row Pyridine-3-aldehyde / DD4, columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 3 Pyridine-3-aldehyde / DD4 reports kcat 10 min^-1 and Km 330 uM; kcat/Km is not printed as a column and is derived from those same-row cells.

row_label: Pyridine-3-aldehyde / DD4


column_label: Table 2, row (R)-(-)-Indan-1-ol / DD4, columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 2 (R)-(-)-Indan-1-ol / DD4 reports kcat 16 min^-1 and Km 300 uM; kcat/Km is not printed as a column and is derived from those same-row cells.


column_label: Table 2, row (S)-(+)-Indan-1-ol, DD4 columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2 (S)-(+)-Indan-1-ol / DD4 reports kcat 19 min^-1 and Km 450 uM; kcat/Km is derived from those same-row same-column cells.


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Oxidation, printed row 7, substrate `9a,11b-PGF2`, TBER1 column group: Km = 24 uM (normalized 0.024 mM); kcat = 0.15 min-1 (normalized 0.0025 s^-1); kcat/Km = 0.006 min-1 uM-1 (normalized 0.1 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 0.15 min-1 / 60 = 0.0025 s^-1; the catalog holds 0.003 s^(-1). Km: printed cell 24 uM / 1000 = 0.024 mM; the catalog holds 0.024 mM. kcat/Km: the paper prints the cell 0.006 min-1 uM-1, which is 0.006 x 1000 / 60 = 0.1 s^-1 mM^-1; the catalog holds 0.125 s^(-1)*mM^(-1).


column_label: PMID 16788056 Table 1. Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5; row 2,3-Butanedione / TBER1 (Table 1, Reduction); TBER1 column group, sub-columns Km, kcat and kcat/Km; printed cells Km 4,800 uM, kcat 100 min^-1, kcat/Km 0.02 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (1.667 s^-1 / 4.8 mM = 0.34729166666666667 s^-1 mM^-1), not as the paper's two-significant-figure printed kcat/Km cell (0.02 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 4.8 mM; metric: kcat; normalized value: 1.667 s^-1; metric: kcat/Km; normalized value: 0.34729166666666667 s^-1 mM^-1; assay condition: pH 7.4; TBER1 column group; NAD(H) coenzyme per the Table 1 footnote; reduction reaction; wild-type recombinant enzyme; no mutation

raw_value_unit_evidence: Table row as printed: Km 4,800 uM; kcat 100 min^-1; kcat/Km 0.02 min^-1 uM^-1 (TBER1 column group).


column_label: PMID 16788056 Table 2. Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5; row 17b-Estradiol / TBER1 (Table 2, (A) oxidation of 17b-hydroxysteroids); TBER1 column group, sub-columns Km, kcat and kcat/Km; printed cells Km 33 uM, kcat 9.0 min^-1, kcat/Km 0.27 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.15 s^-1 / 0.033 mM = 4.545454545454545 s^-1 mM^-1), not as the paper's two-significant-figure printed kcat/Km cell (0.27 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.033 mM; metric: kcat; normalized value: 0.15 s^-1; metric: kcat/Km; normalized value: 4.545454545454545 s^-1 mM^-1; assay condition: pH 7.4; TBER1 column group; NAD(H) coenzyme per the Table 1 footnote; oxidation reaction; wild-type recombinant enzyme; no mutation

raw_value_unit_evidence: Table row as printed: Km 33 uM; kcat 9.0 min^-1; kcat/Km 0.27 min^-1 uM^-1 (TBER1 column group).


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 7, substrate `4-Nitrobenzaldehyde`, TBER1 column group: Km = 96 uM (normalized 0.096 mM); kcat = 18 min-1 (normalized 0.3 s^-1); kcat/Km = 0.20 min-1 uM-1 (normalized 3.333333333333334 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 18 min-1 / 60 = 0.3 s^-1; the catalog holds 0.3 s^(-1). Km: printed cell 96 uM / 1000 = 0.096 mM; the catalog holds 0.096 mM. kcat/Km: the paper prints the cell 0.20 min-1 uM-1, which is 0.20 x 1000 / 60 = 3.333333333333334 s^-1 mM^-1; the catalog holds 3.125 s^(-1)*mM^(-1).


column_label: PMID 16788056 Table 1. Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5; row S-Indan-1-ol / TBER1 (Table 1, Oxidation); TBER1 column group, sub-columns Km, kcat and kcat/Km; printed cells Km 134 uM, kcat 25 min^-1, kcat/Km 0.19 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.417 s^-1 / 0.134 mM = 3.1119402985074625 s^-1 mM^-1), not as the paper's two-significant-figure printed kcat/Km cell (0.19 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.134 mM; metric: kcat; normalized value: 0.417 s^-1; metric: kcat/Km; normalized value: 3.1119402985074625 s^-1 mM^-1; assay condition: pH 7.4; TBER1 column group; NAD(H) coenzyme per the Table 1 footnote; oxidation reaction; wild-type recombinant enzyme; no mutation

raw_value_unit_evidence: Table row as printed: Km 134 uM; kcat 25 min^-1; kcat/Km 0.19 min^-1 uM^-1 (TBER1 column group).


column_label: PMID 16788056 Table 1. Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5; row trans-Benzene dihydrodiol / TBER1 (Table 1, Oxidation); TBER1 column group, sub-columns Km, kcat and kcat/Km; printed cells Km 215 uM, kcat 38 min^-1, kcat/Km 0.18 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.633 s^-1 / 0.215 mM = 2.944186046511628 s^-1 mM^-1), not as the paper's two-significant-figure printed kcat/Km cell (0.18 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.215 mM; metric: kcat; normalized value: 0.633 s^-1; metric: kcat/Km; normalized value: 2.944186046511628 s^-1 mM^-1; assay condition: pH 7.4; TBER1 column group; NAD(H) coenzyme per the Table 1 footnote; oxidation reaction; wild-type recombinant enzyme; no mutation

raw_value_unit_evidence: Table row as printed: Km 215 uM; kcat 38 min^-1; kcat/Km 0.18 min^-1 uM^-1 (TBER1 column group).


column_label: Table 2. Stereospecificity in the oxidation of xenobiotic alcohols and steroids by the two human liver dehydrogenases, row (S)-(+)-Tetralol / DD4, columns kcat (min^-1) and Km (uM); calculated kcat/Km is derived from those exact cells because no kcat/Km column is printed.

normalized_value_unit_evidence: current kcat 0.583 s^-1; paper kcat 0.583333333333 s^-1; current Km 0.35 mM; paper Km 0.35 mM; current kcat/Km 1.66571428571 s^-1 mM^-1; calculated from exact paper kcat and Km cells 1.66666666667 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.583 s^-1; paper kcat 35 min^-1; current Km 0.35 mM; paper Km 350 uM; current kcat/Km 1.66571428571 s^-1 mM^-1; paper does not print kcat/Km as a separate column

row_label: (S)-(+)-Tetralol / DD4


column_label: Table 2, row Naphthalene dihydrodiol, DD4 columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2 Naphthalene dihydrodiol / DD4 reports kcat 5.4 min^-1 and Km 420 uM; kcat/Km is derived from those same-row same-column cells.

row_label: Naphthalene dihydrodiol / DD4


column_label: Table 3. Substrate specificity for carbonyl compounds, row 20alpha-Hydroxy-5beta-pregnan-3-one / DD4, columns kcat (min^-1) and Km (uM); calculated kcat/Km is derived from those exact cells because no kcat/Km column is printed.

normalized_value_unit_evidence: current kcat 0.01 s^-1; paper kcat 0.0283333333333 s^-1; current Km 0.002 mM; paper Km 0.0006 mM; current kcat/Km 5 s^-1 mM^-1; calculated from exact paper kcat and Km cells 47.2222222222 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.01 s^-1; paper kcat 1.7 min^-1; current Km 0.002 mM; paper Km 0.6 uM; current kcat/Km 5 s^-1 mM^-1; paper does not print kcat/Km as a separate column


column_label: Table 3, row 2-Nitrobenzaldehyde, DD4 kcat and Km columns.

raw_value_unit_evidence: DD4 kcat 11 min^-1; DD4 Km 1.1 uM.

row_label: 2-Nitrobenzaldehyde; DD4 columns


column_label: Table 2. Stereospecificity in the oxidation of xenobiotic alcohols and steroids by the two human liver dehydrogenases, row Deoxycholic acid / DD4, columns kcat (min^-1) and Km (uM); calculated kcat/Km is derived from those exact cells because no kcat/Km column is printed.

normalized_value_unit_evidence: current kcat 0.052 s^-1; paper kcat 0.0516666666667 s^-1; current Km 0.006 mM; paper Km 0.0063 mM; current kcat/Km 8.66666666667 s^-1 mM^-1; calculated from exact paper kcat and Km cells 8.20105820106 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.052 s^-1; paper kcat 3.1 min^-1; current Km 0.006 mM; paper Km 6.3 uM; current kcat/Km 8.66666666667 s^-1 mM^-1; paper does not print kcat/Km as a separate column

row_label: Deoxycholic acid / DD4


column_label: Table 2, row Cholic acid / DD4, columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row cells.

raw_value_unit_evidence: Table 2 Cholic acid / DD4 reports kcat 15 min^-1 and Km 24 uM; kcat/Km is derived from those same-row cells.

row_label: Cholic acid / DD4


column_label: Table 2, row 3alpha-Hydroxy-5beta-androstan-17-one, DD4 kcat and Km columns.

raw_value_unit_evidence: DD4 kcat 4.7 min^-1; DD4 Km 1.4 uM.


column_label: Table 2. Stereospecificity in the oxidation of xenobiotic alcohols and steroids by the two human liver dehydrogenases, row Lithocholic acid / DD4, columns kcat (min^-1) and Km (uM); calculated kcat/Km is derived from those exact cells because no kcat/Km column is printed.

normalized_value_unit_evidence: current kcat 0.028 s^-1; paper kcat 0.0283333333333 s^-1; current Km 0.0007 mM; paper Km 0.0007 mM; current kcat/Km 40 s^-1 mM^-1; calculated from exact paper kcat and Km cells 40.4761904762 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.028 s^-1; paper kcat 1.7 min^-1; current Km 0.0007 mM; paper Km 0.7 uM; current kcat/Km 40 s^-1 mM^-1; paper does not print kcat/Km as a separate column

row_label: Lithocholic acid / DD4


column_label: Table 2, row 3alpha-Hydroxy-5beta-pregnan-20-one, DD4 columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2 3alpha-Hydroxy-5beta-pregnan-20-one / DD4 reports kcat 2.0 min^-1 and Km 1.6 uM; kcat/Km is derived from those same-row same-column cells.


column_label: Table 3. Substrate specificity for carbonyl compounds, row Dehydrolithocholic acid / DD4, columns kcat (min^-1) and Km (uM); calculated kcat/Km is derived from those exact cells because no kcat/Km column is printed.

normalized_value_unit_evidence: current kcat 0.015 s^-1; paper kcat 0.0145 s^-1; current Km 0.0001 mM; paper Km 0.0001 mM; current kcat/Km 150 s^-1 mM^-1; calculated from exact paper kcat and Km cells 145 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.015 s^-1; paper kcat 0.87 min^-1; current Km 0.0001 mM; paper Km 0.1 uM; current kcat/Km 150 s^-1 mM^-1; paper does not print kcat/Km as a separate column

row_label: Dehydrolithocholic acid / DD4


substrate_name: trans-benzene dihydrodiol

column_label: Table II, row 'trans-Benzene dihydrodiol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 2.0 min^-1; kcat/Km 0.18 min^-1 uM^-1; Km 11 uM

row_label: trans-Benzene dihydrodiol / AKR1C34

substrate: trans-benzene dihydrodiol


column_label: Table II, row 'alpha-3-Hydroxyhexobarbital', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.1 min^-1; kcat/Km 0.078 min^-1 uM^-1; Km 14 uM

row_label: alpha-3-Hydroxyhexobarbital / AKR1C34


column_label: Table II, row 'beta-3-Hydroxyhexobarbital', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.5 min^-1; kcat/Km 0.038 min^-1 uM^-1; Km 40 uM

row_label: beta-3-Hydroxyhexobarbital / AKR1C34


column_label: Table II, row 'beta-Ionol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.3 min^-1; kcat/Km 1.3 min^-1 uM^-1; Km 1.0 uM

row_label: beta-Ionol / AKR1C34


column_label: Table II, row 'cis-Benzene dihydrodiol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.5 min^-1; kcat/Km 0.15 min^-1 uM^-1; Km 9.7 uM

row_label: cis-Benzene dihydrodiol / AKR1C34


substrate_name: testosterone

substrate: testosterone


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Drosophila melanogaster

substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: pH 9.3; cofactor CoA

proof_lines: 17beta-hydroxysteroid dehydrogenase type 10

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2

source: uniprot


substrate_name: 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor NADH


substrate_name: 17-beta-estradiol (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 5alpha-pregnan-20beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

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


substrate_name: NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius)


organism: Trypanosoma cruzi

substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:Q1WBU6 and applied mutation signature L80G to reconstruct the assayed variant sequence.

column_label: Table 1 paired substrate columns KM, kcat, and kcat/KM; kcat/KM converted from s^-1 uM^-1 to s^-1 mM^-1 by multiplying by 1000.

normalized_value_unit_evidence: Km 0.074 mM; kcat 2.0 s^-1; explicit kcat/Km 27.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row L80G / G6P columns reports KM D-glucose 6-phosphate 74 uM; kcat 2.0 s^-1; kcat/KM 0.027 s^-1 uM^-1.

row_label: L80G / G6P columns

table_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and epiandrosterone

substrate: D-glucose 6-phosphate


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:Q1WBU6 and applied mutation signature K84A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: Km 0.618 mM; kcat 24.6 s^-1; explicit kcat/Km 40.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row K84A / G6P columns reports KM D-glucose 6-phosphate 618 uM; kcat 24.6 s^-1; kcat/KM 0.04 s^-1 uM^-1.

row_label: K84A / G6P columns


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:Q1WBU6 and applied mutation signature R408A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: Km 0.168 mM; kcat 15.0 s^-1; explicit kcat/Km 89.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row R408A / G6P columns reports KM D-glucose 6-phosphate 168 uM; kcat 15.0 s^-1; kcat/KM 0.089 s^-1 uM^-1.

row_label: R408A / G6P columns


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

organism: Sulfolobus solfataricus

substrate_name: D-Xylose

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

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

substrate: D-Xylose


substrate_name: D-Galactose

sequence_variant_note: Mutation signature T41A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: D-Galactose


assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+

column_label: Table 2, T41V block, Galactose/NAD+ row, columns Km for sugar, kcat, and kcat/Km.

normalized_value_unit_evidence: Km=204 mM; kcat=8 s^-1; explicit kcat/Km=0.04 s^-1 mM^-1.

row_label: T41V; Galactose; NAD+

table_label: PMID 16556607 Table 2


substrate_name: D-Glucose

substrate: D-Glucose


column_label: Table 2, T41V block, Glucose/NAD+ row, columns Km for sugar, kcat, and kcat/Km.

normalized_value_unit_evidence: Km=72.5 mM; kcat=6 s^-1; explicit kcat/Km=0.09 s^-1 mM^-1.

row_label: T41V; Glucose; NAD+


column_label: Table 2, Wild-type block, Xylose/NAD+ row, columns Km for sugar, kcat, and kcat/Km.

normalized_value_unit_evidence: Km=0.25 mM; kcat=61 s^-1; explicit kcat/Km=245 s^-1 mM^-1.

row_label: Wild-type; Xylose; NAD+


proof_lines:
17beta-HSD10
Drosophila melanogaster
sex steroids

substrate: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate: 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)


substrate: 17-beta-estradiol (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


proof_lines:
17beta-HSD10
Drosophila melanogaster
C21 steroids

substrate: 5alpha-pregnan-20beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


proof_lines:
17beta-HSD10
Drosophila melanogaster
isoursodeoxycholate

substrate: 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines:
17beta-HSD10
Drosophila melanogaster
hydroxyacyl-CoA dehydrogenase


substrate: NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius)


enzyme_display_name: GDH/6PGL endoplasmic bifunctional protein

organism: Mus musculus

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


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

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

enzyme: GDH/6PGL endoplasmic bifunctional protein


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


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


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


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


organism: Priestia megaterium

substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM PBS; cofactor NADP+

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 1, enzyme row 'BmGDHM0' with mutation column 'Q252L/E170K'; column 'Specific activity [U mg^-1]' = 172; column 'Km [mM]' = 17.4; column 'kcat [s^-1]' = 84.4; column 'kcat/Km [s^-1 mM^-1]' = 4.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 17.4 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 17.4 mM. kcat: printed Table 1 cell 84.4 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 84.4 s^(-1). kcat/Km: printed Table 1 cell 4.9 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 4.9 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 84.4 / 17.4 = 4.850574712643679 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 1, enzyme row 'BmGDHM0', mutation column 'Q252L/E170K': specific activity = 172 U mg^-1; Km = 17.4 mM; kcat = 84.4 s^-1; printed kcat/Km = 4.9 s^-1 mM^-1.

table_label: Table 1: Kinetic parameters for purified BmGDHM0 and its variants (ChemBioChem 2020, 21, 2680-2688)

substrate: D-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K/K166R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 3, enzyme row 'BmGDHM2' with mutation column 'Q252L/E170K/K166R'; column 'Specific activity [U mg^-1]' = 167; column 'Km [mM]' = 16.4; column 'kcat [s^-1]' = 81.9; column 'kcat/Km [s^-1 mM^-1]' = 5.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 16.4 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 16.4 mM. kcat: printed Table 1 cell 81.9 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 81.9 s^(-1). kcat/Km: printed Table 1 cell 5.0 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 5.0 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 81.9 / 16.4 = 4.993902439024391 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 3, enzyme row 'BmGDHM2', mutation column 'Q252L/E170K/K166R': specific activity = 167 U mg^-1; Km = 16.4 mM; kcat = 81.9 s^-1; printed kcat/Km = 5.0 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K/S100P to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 2, enzyme row 'BmGDHM1' with mutation column 'Q252L/E170K/S100P'; column 'Specific activity [U mg^-1]' = 167; column 'Km [mM]' = 14.8; column 'kcat [s^-1]' = 82.6; column 'kcat/Km [s^-1 mM^-1]' = 5.6.

normalized_value_unit_evidence: Km: printed Table 1 cell 14.8 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 14.8 mM. kcat: printed Table 1 cell 82.6 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 82.6 s^(-1). kcat/Km: printed Table 1 cell 5.6 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 5.6 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 82.6 / 14.8 = 5.581081081081081 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 2, enzyme row 'BmGDHM1', mutation column 'Q252L/E170K/S100P': specific activity = 167 U mg^-1; Km = 14.8 mM; kcat = 82.6 s^-1; printed kcat/Km = 5.6 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K/S100P/K166R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 4, enzyme row 'BmGDHM3' with mutation column 'Q252L/E170K/S100P/K166R'; column 'Specific activity [U mg^-1]' = 172; column 'Km [mM]' = 16.0; column 'kcat [s^-1]' = 89.6; column 'kcat/Km [s^-1 mM^-1]' = 5.6.

normalized_value_unit_evidence: Km: printed Table 1 cell 16.0 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 16.0 mM. kcat: printed Table 1 cell 89.6 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 89.6 s^(-1). kcat/Km: printed Table 1 cell 5.6 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 5.6 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 89.6 / 16.0 = 5.6 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 4, enzyme row 'BmGDHM3', mutation column 'Q252L/E170K/S100P/K166R': specific activity = 172 U mg^-1; Km = 16.0 mM; kcat = 89.6 s^-1; printed kcat/Km = 5.6 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K/S100P/K166R/K137R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 6, enzyme row 'BmGDHM5' with mutation column 'Q252L/E170K/S100P/K166R/K137R'; column 'Specific activity [U mg^-1]' = 169; column 'Km [mM]' = 17.5; column 'kcat [s^-1]' = 82.4; column 'kcat/Km [s^-1 mM^-1]' = 4.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 17.5 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 17.5 mM. kcat: printed Table 1 cell 82.4 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 82.4 s^(-1). kcat/Km: printed Table 1 cell 4.7 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 4.7 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 82.4 / 17.5 = 4.708571428571429 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 6, enzyme row 'BmGDHM5', mutation column 'Q252L/E170K/S100P/K166R/K137R': specific activity = 169 U mg^-1; Km = 17.5 mM; kcat = 82.4 s^-1; printed kcat/Km = 4.7 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K/S100P/K166R/V72I to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 5, enzyme row 'BmGDHM4' with mutation column 'Q252L/E170K/S100P/K166R/V72I'; column 'Specific activity [U mg^-1]' = 227; column 'Km [mM]' = 17.2; column 'kcat [s^-1]' = 112; column 'kcat/Km [s^-1 mM^-1]' = 6.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 17.2 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 17.2 mM. kcat: printed Table 1 cell 112 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 112.0 s^(-1). kcat/Km: printed Table 1 cell 6.5 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 6.5 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 112 / 17.2 = 6.511627906976744 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 5, enzyme row 'BmGDHM4', mutation column 'Q252L/E170K/S100P/K166R/V72I': specific activity = 227 U mg^-1; Km = 17.2 mM; kcat = 112 s^-1; printed kcat/Km = 6.5 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K/S100P/K166R/V72I/K137R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 7, enzyme row 'BmGDHM6' with mutation column 'Q252L/E170K/S100P/K166R/V72I/K137R'; column 'Specific activity [U mg^-1]' = 239; column 'Km [mM]' = 17.3; column 'kcat [s^-1]' = 119; column 'kcat/Km [s^-1 mM^-1]' = 6.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 17.3 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 17.3 mM. kcat: printed Table 1 cell 119 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 119.0 s^(-1). kcat/Km: printed Table 1 cell 6.9 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 6.9 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 119 / 17.3 = 6.878612716763006 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 7, enzyme row 'BmGDHM6', mutation column 'Q252L/E170K/S100P/K166R/V72I/K137R': specific activity = 239 U mg^-1; Km = 17.3 mM; kcat = 119 s^-1; printed kcat/Km = 6.9 s^-1 mM^-1.


organism: Bacillus megaterium

proof_lines: PMID 1629157 separates NAD-linked and NADP-linked isozyme measurements.


proof_lines: PMID 1629157 distinguishes GlcDH-II NAD and NADP assay contexts.


proof_lines: PMID 1629157 separates GlcDH-IV NAD and NADP assay contexts.


substrate_name: NADP+

column_label: Table 2: Kinetic constants of glucose dehydrogenases (J. Bacteriol. 1992, 174(15):5013-5020), row 'GlcDH-III', column 'Coenzyme' = 'NADP'; column 'kcat (s-1)' = 802; column 'Ka (mM)' = 18.9.

normalized_value_unit_evidence: kcat: printed cell 802 s^-1; already in s^-1, no unit conversion applies; the exported value is 802.0 s^(-1). km: printed Ka (mM) cell 18.9 mM; already in mM, no unit conversion applies; the exported value is 18.9 mM. kcat_over_km: this paper prints no kcat/Km efficiency column, so the value is derived from this row's own two printed cells: 802 / 18.9 = 42.43386243386244 s^-1 mM^-1, which is the exported value; the paper itself does not report an independent efficiency figure for this row.

raw_value_unit_evidence: Table 2, row 'GlcDH-III', coenzyme column 'NADP': kcat = 802 s^-1; Ka (mM) = 18.9 mM.

substrate: NADP+


organism: Comamonas testosteroni

substrate_name: Fusidic acid

source_db: brenda

sequence_source: multiple

column_label: PDF page 4, Table 1, row Fusidic acid, column Km (umol/l): 6.1; 6.1 uM = 0.0061 mM.

raw_value_unit_evidence: Km raw_value=6.1 raw_unit=umol/l

row_label: Fusidic acid

table_label: Table 1: Kinetic Constants for 3alpha-HSD/CR from C. testosteroni with Steroids

source_databases_merged: brenda uniprot

substrate: Fusidic acid

source: brenda


substrate_name: cholic acid

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

column_label: PDF page 4, Table 1, row Cholic acid, column Km (umol/l): 18.4; 18.4 uM = 0.0184 mM.

raw_value_unit_evidence: Km raw_value=18.4 raw_unit=umol/l

row_label: Cholic acid

substrate: cholic acid


substrate_name: androstanedione

assay_conditions_summary: pH 7

column_label: PDF page 4, Table 1, row Androstanedione, column Km (umol/l): 42.2; 42.2 uM = 0.0422 mM.

raw_value_unit_evidence: Km raw_value=42.2 raw_unit=umol/l

row_label: Androstanedione

substrate: androstanedione


substrate_name: metyrapone

column_label: PDF page 5, Table 2, row Metyrapone, column Km (umol/l): 1882; 1882 uM = 1.882 mM.

raw_value_unit_evidence: Km raw_value=1882 raw_unit=umol/l

row_label: Metyrapone

table_label: Table 2: Kinetic Constants for 3alpha-HSD/CR from C. testosteroni with Non-Steroidal Aldehydes and Ketones

substrate: metyrapone


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase 1, chloroplastic

organism: Arabidopsis thaliana

substrate_name: NADP

substrate: NADP


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase 3, chloroplastic


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase 6, cytoplasmic


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase 2, chloroplastic


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase 5, cytoplasmic


column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation row 5alpha-DHT reduction / AKR1C4 (S); columns Km (uM), Vmax (nmol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation row 5alpha-DHT reduction / AKR1C4 (S): Km 3.4 uM; Vmax 53.9 +/- 2.8; kcat 1.99 min^-1; kcat/Km 586 min^-1 mM^-1.

row_label: 5alpha-DHT reduction / AKR1C4 (S)


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 2; row 5alpha-Androstane-3,17-dione reduction / AKR1C4; expected Km and kcat/Km are not the table values.

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.

row_label: 5alpha-androstane-3,17-dione reduction; AKR1C4 closest kcat row

table_label: Table 2


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 2; 3alpha-Androstanediol oxidation section; no explicit row/column combination matches expected metrics.

normalized_value_unit_evidence: Closest AKR1C4 conversion: kcat=0.035 s^-1, Km=0.0105 mM, kcat/Km=3.333 s^-1 mM^-1; expected row has kcat=0.113, Km=0.002, kcat/Km=56.5.

raw_value_unit_evidence: Closest explicit Table 2 row, 3alpha-androstanediol oxidation / AKR1C4, reports Km=10.5 +/- 2.4 microM, kcat=2.1 min^-1, kcat/Km=200 min^-1 mM^-1; AKR1C2 and AKR1C3 are also far lower than expected.

row_label: 3alpha-androstanediol oxidation; closest relevant rows are AKR1C2, AKR1C3, and AKR1C4


column_label: Table 2; Androsterone oxidation section; no explicit row/column combination matches all required expected metrics.

normalized_value_unit_evidence: Closest AKR1C4 conversion: kcat=0.02317 s^-1, Km=0.00504 mM, kcat/Km=4.6 s^-1 mM^-1; expected row has kcat=0.09, Km=0.001, kcat/Km=90.

raw_value_unit_evidence: Closest explicit Table 2 row, androsterone oxidation / AKR1C4, reports Km=5.04 +/- 1.22 microM, kcat=1.39 min^-1, kcat/Km=276 min^-1 mM^-1; other androsterone oxidation rows are AKR1C1 41.7 microM/0.060 min^-1/1.4 and AKR1C2 9.73 microM/0.42 min^-1/43.

row_label: Androsterone oxidation; closest relevant rows are AKR1C1, AKR1C2, and AKR1C4


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K159A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


proof_lines:
wild type
Tyr-155/Lys-159 mutant series


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y155F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y155F/K159A to reconstruct the assayed variant sequence.


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.


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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

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

row_label: WT / 5alpha-DHT


enzyme_display_name: Galactose 1-dehydrogenase

organism: Pseudomonas fluorescens

substrate_name: NAD(+)

assay_conditions_summary: pH 9.1; buffer while varying NAD+ and D-galactose; cofactor NAD+

column_label: PDF text lines 26-29 state the limiting Michaelis constant for NAD+ is Ka = 0.24 mM at pH 9.1 and 30 C.

normalized_value_unit_evidence: Km/Ka normalized_value=0.24 normalized_unit=mM; raw value is already reported in mM.

raw_value_unit_evidence: The paper reports: at pH 9.1 and 30 C, the limiting Michaelis constant for NAD+ is Ka = 0.24 mM.

row_label: D-galactose dehydrogenase from Pseudomonas fluorescens / NAD+ cosubstrate

table_label: Kinetic constants prose summary and initial-rate results section

enzyme: Galactose 1-dehydrogenase

substrate: NAD(+)


substrate_name: NADP(+)

assay_conditions_summary: pH 9.1; buffer while varying NADP+ and D-galactose; cofactor NADP+

column_label: PDF text lines 26-29 state the limiting Michaelis constant for NADP+ is Ka = 2.3 mM at pH 9.1 and 30 C.

normalized_value_unit_evidence: Km/Ka normalized_value=2.3 normalized_unit=mM; raw value is already reported in mM.

raw_value_unit_evidence: The paper reports: at pH 9.1 and 30 C, the limiting Michaelis constant for NADP+ is Ka = 2.3 mM.

row_label: D-galactose dehydrogenase from Pseudomonas fluorescens / NADP+ cosubstrate

substrate: NADP(+)


substrate_name: D-galactose

substrate: D-galactose


assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


substrate_name: NAD+

substrate: NAD+


organism: Aspergillus nidulans

substrate_name: NADPH

assay_conditions_summary: cofactor NADP+

substrate: NADPH


substrate_name: D-glucose 6-phosphate

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Table 2 lists the A. nidulans row with K(G6P)=92+10 uM.

raw_value_unit_evidence: Km raw_value=92+10 raw_unit=uM

row_label: A. nidulans row

table_label: Table 2. Kinetic parameters for A. nidulans and A. niger G6PD enzymes

substrate: D-glucose 6-phosphate


km_display: Not reported

ki_unit: mM

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 2 lists the A. nidulans row with Ki(NADPH)=20+5 uM.

raw_value_unit_evidence: Ki raw_value=20+5 raw_unit=uM


organism: Escherichia coli

substrate_name: D-Glucose 6-phosphate

proof_lines:
specificity constants for NADP and NAD
Escherichia coli G6PDH

substrate: D-Glucose 6-phosphate


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines:
wild-type E. coli G6PDH
7.5 uM
174 s^-1


substrate_name: glucose 6-phosphate

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

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+

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

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

substrate: glucose 6-phosphate


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

column_label: Table 2. Kinetic data for the NAD-linked reactions (Protein Science 1992, 1:329-334, journal page 331). Row K21R; column Km G6P (uM) = 96.5; column Km NAD+ (uM) = 240; column kcat (min^-1) = 66,100; column kcat/Km (G6P) (min^-1 uM^-1) = 685.

raw_value_unit_evidence: Journal page 331, Table 2, row K21R, varied substrate glucose 6-phosphate: Km G6P = 96.5 uM; kcat = 66,100 min^-1; kcat/Km G6P = 685 min^-1 uM^-1.


proof_lines:
wild-type enzyme
Leuconostoc mesenteroides
glucose 6-phosphate


organism: Pseudomonas sp

substrate_name: androsterone

sequence: QVIAITGSASGIGAA

wild_type_sequence: QVIAITGSASGIGAA

proof_lines:
Pseudomonas strain
3alpha-HSD/carbonyl reductase
broad steroid activity

substrate: androsterone


substrate_name: fusidic acid

proof_lines:
Pseudomonas strain
broad substrate specificity
xenobiotic carbonyl compounds

substrate: fusidic acid


proof_lines:
metyrapone-based insecticides
xenobiotic carbonyl compounds
Pseudomonas strain


substrate_name: (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor NADH

column_label: Table 3; Drosophila species columns; row β-Hydroxybutyryl-CoA/NAD+; Km column

normalized_value_unit_evidence: Km=0.101 mM converted from 101 uM

raw_value_unit_evidence: Table 3 Drosophila β-Hydroxybutyryl-CoA/NAD+ Km 101 +/- 8 ×10^-6 M

row_label: β-Hydroxybutyryl-CoA/NAD+

table_label: Table 3


enzyme_display_name: Lambda-crystallin homolog

substrate_name: NAD

proof_lines:
human lambda-crystallin homolog
L-gulonate 3-dehydrogenase
NAD-linked dehydrogenation

enzyme: Lambda-crystallin homolog

substrate: NAD


substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
human lambda-crystallin homolog
L-gulonate 3-dehydrogenase
NAD(H)-complex kinetics

substrate: NADH


enzyme_display_name: Lambda-crystallin

organism: Oryctolagus cuniculus

assay_conditions_summary: cofactor NAD+

proof_lines: PMID 15809331 supports rabbit L-gulonate 3-dehydrogenase and NAD-linked chemistry, but not the exact Km value preserved here.

enzyme: Lambda-crystallin


proof_lines: PMID 15809331 supports rabbit L-gulonate 3-dehydrogenase and NAD(H)-linked chemistry, but not the exact Km value preserved here.


substrate_name: D-Galactose

assay_conditions_summary: pH 7.5; 343.15 K; buffer 10 mM NAD+ in 100 mM HEPES; cofactor NAD+

column_label: Table II - Kinetic parameters of glucose dehydrogenase from S. solfataricus at 70 C; row d-Galactose / NAD+

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.

row_label: d-Galactose / NAD+

substrate: D-Galactose