substrate_name: D-Glucose

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

row_label: d-Glucose / NAD+

substrate: D-Glucose


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

organism: Sulfolobus solfataricus

substrate_name: D-Galactose

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.

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+

column_label: Table II row D-Galactose / NAD+ gives Km 0.57, kcat 61.3, kcat/Km 107.5.

row_label: D-Galactose / NAD+

table_label: TABLE II. Kinetic parameters of glucose dehydrogenase from S. solfataricus at 70 C

data_origin: experimental

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

substrate: D-Galactose

status: corrected

source: oed


column_label: Table II row D-Glucose / NAD+ gives Km 1.50, kcat 74.9, kcat/Km 49.9.

row_label: D-Glucose / NAD+


enzyme_display_name: Glucose 1-dehydrogenase

organism: Saccharolobus solfataricus

substrate_name: NAD(+) (at 70 degrees Celsius and pH 8)

source_db: uniprot

verification_status: verified

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+

column_label: Table 4 / Apparent Km values for substrates and coenzymes of glucose dehydrogenase from Sulfolobus solfataricus; Glucose-NAD+ row; coenzyme Km column = 1.2 mM.

normalized_value_unit_evidence: Km=1.2 mM directly reported in Table 4; no unit conversion required.

raw_value_unit_evidence: Glucose-NAD+ / coenzyme Km column reports coenzyme Km = 1.2 mM.

row_label: Glucose-NAD+ / coenzyme Km column

enzyme: Glucose 1-dehydrogenase

substrate: NAD(+) (at 70 degrees Celsius and pH 8)

status: verified

source: uniprot


substrate_name: NADP(+) (at 70 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

column_label: Table 4 / Apparent Km values for substrates and coenzymes of glucose dehydrogenase from Sulfolobus solfataricus; Glucose-NADP+ row; coenzyme Km column = 0.03 mM.

normalized_value_unit_evidence: Km=0.03 mM directly reported in Table 4; no unit conversion required.

raw_value_unit_evidence: Glucose-NADP+ / coenzyme Km column reports coenzyme Km = 0.03 mM.

row_label: Glucose-NADP+ / coenzyme Km column


verification_status: unverified

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: The enzyme utilizes both NAD+ and NADP+ as coenzyme

proof_lines: Saccharolobus solfataricus glucose dehydrogenase

status: unverified


substrate: NADP(+) (at 70 degrees Celsius and pH 8)


organism: Trypanosoma cruzi

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:Q1WBU6 and applied mutation signature K83A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

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 0.021 mM; kcat 3.0 s^-1; explicit kcat/Km 140.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row K83A / NADP+ columns reports KM NADP+ 21 uM; kcat 3.0 s^-1; kcat/KM 0.14 s^-1 uM^-1.

row_label: K83A / NADP+ columns

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

substrate: NADP+


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

raw_value_unit_evidence: Table 1 row K84A / NADP+ columns reports KM NADP+ 17 uM; kcat 58.0 s^-1; kcat/KM 3.4 s^-1 uM^-1.

row_label: K84A / NADP+ columns


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

raw_value_unit_evidence: Table 1 row R408A / NADP+ columns reports KM NADP+ 17 uM; kcat 19.0 s^-1; kcat/KM 1.1 s^-1 uM^-1.

row_label: R408A / NADP+ columns


assay_conditions_summary: pH 7.5; 298.15 K; buffer B (50 mM Tris pH 7; cofactor NADP+

column_label: Table 1; row WT; columns KM NADP+ (uM), kcat (NADP+ series), kcat/KM NADP+ (s^-1 uM^-1)

raw_value_unit_evidence: Table 1 WT NADP+ series: Km 16 uM; kcat 52 s^-1; kcat/Km 3.2 s^-1 uM^-1

row_label: WT

table_label: Table 1


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Drosophila melanogaster

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor NADH

column_label: Table 3; Drosophila species columns; row Acetoacetyl-CoA/NADH; Km column

normalized_value_unit_evidence: Km=0.0337 mM converted from 33.7 uM

raw_value_unit_evidence: Table 3 Drosophila Acetoacetyl-CoA/NADH Km 33.7 +/- 8 ×10^-6 M

row_label: Acetoacetyl-CoA/NADH

table_label: Table 3

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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 NAD+

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 4 / Apparent Km values for substrates and coenzymes of glucose dehydrogenase from Sulfolobus solfataricus


assay_conditions_summary: 343.15 K; cofactor NADP+


assay_conditions_summary: pH 6.4; cofactor NAD+

substrate: (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA) (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: cofactor NAD+


organism: Mesocricetus auratus

substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M potassium phosphate; cofactor NAD+

column_label: Table I (Kinetic constants for coenzymes), enzyme block 'AKR1C35', coenzyme row 'NADH'; column 'Km (uM)' = 17 with a standard deviation of 2; column 'kcat (min^-1)' = 6.2 with a standard deviation of 0.9; column 'kcat/Km (min^-1 uM^-1)' = 0.36. The AKR1C34 block of the same coenzyme row prints Km 13, kcat 10 and kcat/Km 0.76.

normalized_value_unit_evidence: Km: printed Table I cell 17 uM; 17 / 1000 = 0.017 mM, which is the exported value. kcat: printed Table I cell 6.2 min^-1; 6.2 / 60 = 0.10333333333333333 s^-1. kcat/Km: Printed kcat/Km cell 0.36 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.36 x 1000 / 60 = 6.0 s^-1 mM^-1. Closure disclosure: the quotient of this row's own printed component cells is 6.2 / 17 = 0.3647058823529412 min^-1 uM^-1, against the printed efficiency cell 0.36 carried at the precision of the printed column.

raw_value_unit_evidence: Table I, AKR1C35 enzyme block, coenzyme row 'NADH': Km = 17 uM; kcat = 6.2 min^-1; kcat/Km = 0.36 min^-1 uM^-1.

row_label: Table I, coenzyme row NADH of the AKR1C35 enzyme block

table_label: Table I: Kinetic constants for coenzymes (J. Biochem. 2015, 158(5):425-434)

substrate: NADH


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

organism: Halobacterium salinarum

substrate_name: NADPH

source_db: brenda

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

assay_conditions_summary: pH 8.2; cofactor NADP+

column_label: Primary-paper PDF Table 2 lists NADPH as varied substrate with Km (mM) = 0.49.

raw_value_unit_evidence: NADPH Km 0.49 mM

row_label: NADPH varied-substrate row

table_label: Table 2: Product inhibition study of H. salinarum glucose dehydrogenase reaction in the reverse direction

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

substrate: NADPH

source: brenda


substrate: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)


assay_conditions_summary: pH 9.3; cofactor CoA


assay_conditions_summary: pH 7; cofactor NADH

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


substrate_name: NAD+

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

column_label: Table I, row 'NAD+', 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 6.8 min^-1; kcat/Km 0.30 min^-1 uM^-1; Km 23 uM

row_label: NAD+ / AKR1C35

table_label: Table I

substrate: NAD+


column_label: Primary-paper PDF Table I lists NADP+ as varied substrate with Km (mM) = 0.19.

raw_value_unit_evidence: NADP+ Km 0.19 mM

row_label: NADP+ varied-substrate row

table_label: Table I: Product inhibition study of H. salinarum glucose dehydrogenase reaction in the forward direction


assay_conditions_summary: pH 8.2; cofactor NADPH


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


assay_conditions_summary: pH 7.4; 298.15 K; buffer pH 7; cofactor NADH

column_label: Table I, row 'NADH', 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 6.2 min^-1; kcat/Km 0.36 min^-1 uM^-1; Km 17 uM

row_label: NADH / AKR1C35


assay_conditions_summary: 343.15 K; cofactor NAD+


assay_conditions_summary: pH 6.4; cofactor CoA

proof_lines:
hydroxyacyl-CoA dehydrogenase
17beta-HSD10
Drosophila


organism: Comamonas testosteroni

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S114A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Homo sapiens

substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


organism: Rattus norvegicus

assay_conditions_summary: cofactor NADPH

column_label: The abstract reports the Km for NADPH was 0.71 microM.

raw_value_unit_evidence: Km raw_value=0.71 microM raw_unit=microM

row_label: Prose segment: NADPH Km

table_label: PubMed PMID 2268552 abstract


assay_conditions_summary: cofactor NADP+

column_label: The abstract reports the Km for NADP+ was 1.6 microM.

raw_value_unit_evidence: Km raw_value=1.6 microM raw_unit=microM

row_label: Prose segment: NADP+ Km


organism: Neurospora crassa


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


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

organism: Azospirillum brasilense

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

assay_conditions_summary: pH 9; cofactor NADP+

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


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


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: glucose-6-phosphate (at 25 degrees Celsius)

assay_conditions_summary: pH 8; cofactor NADP+

column_label: Table 1 section PfGluPho's G6PD activity reports G6P Km (uM) = 19.2 +/- 3.9.

raw_value_unit_evidence: Km raw_value=19.2 +/- 3.9 raw_unit=uM

row_label: PfGluPho's G6PD activity row G6P

table_label: Biochemical Journal Table 1, Kinetic characteristics of PfGluPho, G6PDPfGluPho, hG6PD and h6PGL


substrate_name: NADP(+) (at 25 degrees Celsius)

column_label: Table 1 section PfGluPho's G6PD activity reports NADP+ Km (uM) = 6.5 +/- 2.2.

raw_value_unit_evidence: Km raw_value=6.5 +/- 2.2 raw_unit=uM

row_label: PfGluPho's G6PD activity row NADP+

substrate: NADP(+) (at 25 degrees Celsius)


assay_conditions_summary: buffer pH was 9; cofactor NAD+

column_label: Table 4; Glucose-NAD+ row; coenzyme K_m (mM) column; raw value 1.2 mM.

raw_value_unit_evidence: Table 4 Glucose-NAD+ row reports coenzyme K_m = 1.2 mM.

row_label: Glucose-NAD+ row

table_label: PMID 3827812, Table 4: Apparent Km values for substrates and coenzymes of glucose dehydrogenase from Sulfolobus solfataricus


assay_conditions_summary: buffer pH was 9; cofactor NADP+

column_label: Table 4; Glucose-NADP+ row; coenzyme K_m (mM) column; raw value 0.03 mM.

raw_value_unit_evidence: Table 4 Glucose-NADP+ row reports coenzyme K_m = 0.03 mM.

row_label: Glucose-NADP+ row


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 1

column_label: Table 1, Purified Enzymes / Wild type row, Estradiol to Estrone Km column reports 2.11 +/- 0.56 uM.

raw_value_unit_evidence: Km raw_value=2.11 +/- 0.56 raw_unit=uM

row_label: Purified Enzymes / Wild type

table_label: Oxford Academic full text Table 1: Activity Measurements of 17-HSD Type 1 Enzymes in Vitro


substrate_name: estrone

column_label: Table 1, Purified Enzymes / Wild type row, Estrone to Estradiol Km column reports 0.90 +/- 0.13 uM.

raw_value_unit_evidence: Km raw_value=0.90 +/- 0.13 raw_unit=uM

enzyme: 17-beta-hydroxysteroid dehydrogenase type 1

substrate: estrone


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51857 and applied mutation signature E120H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; buffer 1-ml systems containing 100 mM potassium phosphate; cofactor NAD+

column_label: Table 3: Kinetic constants for hydroxysteroid oxidation catalyzed by the E120H mutant and AKR1C2 (J. Biol. Chem. 2012, 287(20):16609-16622), enzyme block E120H, substrate row '5beta-DHT'; column 'Substrate stereospecificity' = 17beta; column 'kcat (x 10^-3 s^-1)' = 0.85; column 'Km (uM)' = 5.7; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 1.5. Column 'Ki (uM)' is empty for this row.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.85 with the column head x 10^-3 s^-1, so the cell reads 0.85 x 10^-3 s^-1; the paper value is 0.00085 s^(-1); the exported value is 0.0008 s^(-1). Km: printed Table 3 cell 5.7 uM; 1 uM is 0.001 mM, so 5.7 / 1000 = 0.0057 mM; the paper value is 0.0057 mM; the exported value is 0.006 mM. kcat/Km: printed Table 3 cell 1.5 with the column head x 10^2 M^-1 s^-1, so the cell reads 150 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150 / 1000 = 0.15 s^-1 mM^-1; the paper value is 0.15 s^(-1)*mM^(-1); the exported value is 0.13333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row '5beta-DHT': kcat = 0.85 s-1 under the column multiplier x 10^-3; Km = 5.7 uM; printed kcat/Km = 1.5 M-1 s-1 under the column multiplier x 10^2.


proof_lines:
AKR1D1 E120H
comparator kinetics
P52895


organism: Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)

substrate_name: NADP(+) (at 70 degrees Celsius and pH 7)

assay_conditions_summary: pH 7; cofactor NADP+


organism: Aspergillus nidulans


substrate_name: beta-D-glucose

substrate: beta-D-glucose


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase

substrate_name: glucose 6-phosphate

enzyme: Glucose-6-phosphate 1-dehydrogenase

substrate: glucose 6-phosphate


column_label: Table 2; row 4-Androstene-3,17-dione; TBER1 Km/kcat/kcat/Km columns; raw 17 uM, 1.0 min^-1, 0.06 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 TBER1 cells: Km 17 uM; kcat 1.0 min^-1; kcat/Km 0.06 min^-1 uM^-1.

row_label: 4-Androstene-3,17-dione / TBER1

table_label: PMID 16788056 Table 2, steroid substrates


substrate_name: testosterone

column_label: Table 2; row Testosterone; TBER1 Km/kcat/kcat/Km columns; raw 25 uM, 16 min^-1, 0.62 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 TBER1 cells: Km 25 uM; kcat 16 min^-1; kcat/Km 0.62 min^-1 uM^-1.

row_label: Testosterone / TBER1

substrate: testosterone


organism: Priestia megaterium

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


substrate_name: NADP+


assay_conditions_summary: cofactor NAD+


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

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl; cofactor NADP+

proof_lines:
wild type, coenzyme NADP+
wild type, coenzyme NAD+
wild-type enzyme, pH 8.0, 25°C


substrate_name: NAADP

substrate: NAADP


column_label: Table I column K m (unit microM) for row Rat RoDH1 - Testosterone gives 2.8

normalized_value_unit_evidence: Table I K m normalized_value=0.0028 normalized_unit=mM

raw_value_unit_evidence: Table I K m raw_value=2.8 raw_unit=microM

row_label: Rat RoDH1 / Testosterone / Androstenedione / Ox 17beta-HSD

table_label: Table I: Kinetic constants of steroid metabolizing enzymes


assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl; cofactor NAD+

proof_lines: apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table I, row 'AKR1C35', AKR1C35 column group, columns Km, kcat and kcat/Km. The Table I column headers print Km, kcat and kcat/Km; the PDF glyph loss drops the Greek mu, so the columns are Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Every other AKR1C34/AKR1C35 row of Table I reproduces its own printed ratio under that reading. Normalizing the two printed primary cells gives Km 2.4 mM and kcat 0.15 s^-1; the kcat/Km entry is the quotient of those same two cells, 0.0625 s^-1 mM^-1, recorded as derived rather than transcribed. Conversion arithmetic, disclosed separately from the stored values: 9.0 min^-1 / 60 = 0.15 s^-1 exactly; 2,400 uM / 1000 = 2.4 mM exactly; kcat/Km is not taken from the printed ratio cell but is the quotient of this row's own two printed cells, and it back-converts to the printed ratio cell: 0.15 s^-1 / 2.4 mM = 0.0625 s^-1 mM^-1 = 9.0 min^-1 / 2,400 uM = 0.00375 min^-1 uM^-1, which rounds to the printed 0.0038 cell at its two-significant-figure precision.

normalized_value_unit_evidence: metric: kcat; raw value: 9.0 ± 2.0 min^-1; raw unit: min^-1; normalized value: 0.15 s^-1; metric: Km; raw value: 2,400 ± 530 uM; raw unit: uM; normalized value: 2.4 mM; metric: kcat/Km; raw value: derived from this row's own two printed cells; normalized value: 0.0625 s^-1 mM^-1; assay condition: Recombinant hamster AKR1C35; coenzyme kinetic constants of Table I; 0.1 M potassium phosphate buffer, pH 7.4; 25 C; NADP+ varied as the coenzyme.

raw_value_unit_evidence: Table I row AKR1C35 / NADP+: Km 2,400 ± 530 uM; kcat 9.0 ± 2.0 min^-1; kcat/Km 0.0038 min^-1 uM^-1.

row_label: AKR1C35 | NADP+

table_label: Table I. Kinetic constants for coenzymes


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192T/V306G


proof_lines: pH and temperature not specified in the publication, mutant enzyme V306G


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192T


proof_lines: pH and temperature not specified in the publication, mutant enzyme V306I


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192T/V306I


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


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192V


km_display: Not reported

proof_lines: pH and temperature not specified in the publication, mutant enzyme 0.00184 I192T/V306G


substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G261A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor NAD+

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G261A; column pH 6.0 KM (mM); raw 4.1 x 10^2 +/- 35 mM; normalized Km=410 mM.

normalized_value_unit_evidence: Km=410 mM

substrate: D-glucose


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature A258F to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row A258F; column pH 6.0 KM (mM); raw 4.3 +/- 0.2 mM; normalized Km=4.3 mM.

normalized_value_unit_evidence: Km=4.3 mM


assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row A258F; column pH 8.0 KM (mM); raw 9.8 +/- 1.0 mM; normalized Km=9.8 mM.

normalized_value_unit_evidence: Km=9.8 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G259A to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G259A; column pH 6.0 KM (mM); raw 81 +/- 7.1 mM; normalized Km=81 mM.

normalized_value_unit_evidence: Km=81 mM


column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G259A; column pH 8.0 KM (mM); raw 380 +/- 16 mM; normalized Km=380 mM.

normalized_value_unit_evidence: Km=380 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature ΔG261 to reconstruct the assayed variant sequence.

mutation_type: deletion

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row DeltaG261; column pH 6.0 KM (mM); raw 1.1 x 10^3 +/- 170 mM; normalized Km=1100 mM.

row_label: DeltaG261 / pH 6.0 KM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G259V to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G259V; column pH 6.0 KM (mM); raw 1.4 x 10^3 +/- 96 mM; normalized Km=1400 mM.


assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G261V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6


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


substrate_name: D-xylose

substrate: D-xylose


substrate_name: beta-D-galactose

proof_lines:
wild type enzyme, NADP+ as cofactor
wild type enzyme, NAD+ as cofactor

substrate: beta-D-galactose


enzyme_display_name: L-gulonate 3-dehydrogenase

organism: Oryctolagus cuniculus

assay_conditions_summary: pH 7; cofactor NAD+

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column WTa Value; raw value 0.010 mM; normalized Km 0.01 mM; NAD+-linked activity; WT value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 0.01 mM

row_label: Km NAD+ (mM)

enzyme: L-gulonate 3-dehydrogenase


substrate_name: L-gulonate

column_label: Table 3; WT column; NAD-linked activity; Km L-gulonate row.

normalized_value_unit_evidence: Km paper=0.18 mM for NAD-linked WT; export=0.018 mM.

raw_value_unit_evidence: WT Km L-gulonate 0.18 mM; NADP-linked WT Km L-gulonate is 2.4 mM.

row_label: WT; NAD-linked activity; Km L-gulonate

table_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations

substrate: L-gulonate


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q41N to reconstruct the assayed variant sequence.

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column Q41N Value; raw value 0.028 +/- 0.001 mM; normalized Km 0.028 mM; NAD+-linked activity; Q41N mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E97Q to reconstruct the assayed variant sequence.

column_label: Table 3 NAD+-linked activity, Km NAD+, mutant E97Q: 0.054 ± 0.06 mM.

row_label: NAD+-linked activity; Km NAD+; mutant E97Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36R/Q41N to reconstruct the assayed variant sequence.

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column D36R/Q41N Value; raw value 0.12 +/- 0.01 mM; normalized Km 0.12 mM; NADP+-linked activity; D36R/Q41N double mutant

normalized_value_unit_evidence: Km 0.12 mM

row_label: Km NADP+ (mM)

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36R to reconstruct the assayed variant sequence.

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column D36Ra Value; raw value 0.20 mM; normalized Km 0.2 mM; NADP+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 0.2 mM

raw_value_unit_evidence: Km 0.20 mM


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

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column WTa Value; raw value 0.67 mM; normalized Km 0.67 mM; NADP+-linked activity; WT value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 0.67 mM

raw_value_unit_evidence: Km 0.67 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column Q41N Value; raw value 0.86 +/- 0.13 mM; normalized Km 0.86 mM; NADP+-linked activity; Q41N mutant

normalized_value_unit_evidence: Km 0.86 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column D36Ra Value; raw value 1.3 mM; normalized Km 1.3 mM; NAD+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 1.3 mM

raw_value_unit_evidence: Km 1.3 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column Q41N Value; raw value 1.3 +/- 0.1 mM; normalized Km 1.3 mM; NAD+-linked activity; Q41N mutant

row_label: Km L-gulonate (mM)


column_label: Table 3 NAD+-linked activity, Km L-gulonate, mutant E97Q: 1.6 ± 0.1 mM.

row_label: NAD+-linked activity; Km L-gulonate; mutant E97Q


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column D36R/Q41N Value; raw value 2.6 +/- 0.4 mM; normalized Km 2.6 mM; NAD+-linked activity; D36R/Q41N double mutant

normalized_value_unit_evidence: Km 2.6 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36R/Q41N Value; raw value 2.6 +/- 0.2 mM; normalized Km 2.6 mM; NADP+-linked activity; D36R/Q41N double mutant


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36R/Q41N Value; raw value 3.3 +/- 0.3 mM; normalized Km 3.3 mM; NAD+-linked activity; D36R/Q41N double mutant

normalized_value_unit_evidence: Km 3.3 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36Ra Value; raw value 14 mM; normalized Km 14.0 mM; NAD+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 14.0 mM

raw_value_unit_evidence: Km 14 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column Q41N Value; raw value 14 +/- 1.2 mM; normalized Km 14.0 mM; NADP+-linked activity; Q41N mutant


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36Ra Value; raw value 18 mM; normalized Km 18.0 mM; NADP+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 18.0 mM

raw_value_unit_evidence: Km 18 mM


substrate_name: NADH

assay_conditions_summary: pH 8.5; cofactor NADH

proof_lines:
at pH 8.5, rabbit liver GDH
at pH 8.5, recombinant rabbit GDH

substrate: NADH


assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines:
at pH 8.5, recombinant rabbit GDH
at pH 8.5, rabbit liver GDH


proof_lines: mutant enzyme E157Q, NAD+-linked activity


assay_conditions_summary: pH 8.5; cofactor NADP+


substrate_name: L-threonate

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

substrate: L-threonate


proof_lines: mutant enzyme S124A, NAD+-linked activity


substrate_name: acetoacetate

substrate: acetoacetate


proof_lines: mutant enzyme D36R, NAD+-linked activity


assay_conditions_summary: cofactor NADP+

proof_lines: mutant enzyme D36R, NADP+-linked activity


proof_lines: mutant enzyme E157Q, NADP+-linked activity


organism: Escherichia coli

assay_conditions_summary: pH 8.2; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADP+


proof_lines: mutant enzyme K18A/R50A, at pH 8.2 and 25°C


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines:
wild type enzyme, at pH 8.2 and 25°C
25°C, pH 8.0, wild-type strain K-10


organism: Sus scrofa


substrate_name: beta-keto-L-gulonate

assay_conditions_summary: pH 6.3; cofactor NADH

substrate: beta-keto-L-gulonate


substrate_name: L-Idonate

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

substrate: L-Idonate


organism: Corynebacterium sp.

assay_conditions_summary: pH 9.8; cofactor NAD+

proof_lines:
strain 93-1
pH 9.8
strain 150-1

substrate: NAD+


proof_lines:
strain 93-1
strain 150-1


substrate_name: gentiobiose

substrate: gentiobiose


substrate_name: cellobiose

substrate: cellobiose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl

proof_lines: apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


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

proof_lines: apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E170K to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl; cofactor NAD+

column_label: PMCID PMC1151818 HTML Table 1; row Q252L; column Apparent Km (NAD+) (mM); raw value 0.15 mM; normalized value 0.15 mM. Footnote a defines the pH 8.0, fixed 0.1 M glucose, and NAD+ concentration range.

normalized_value_unit_evidence: 0.15 mM is already normalized as 0.15 mM.

raw_value_unit_evidence: Table 1 row Q252L, column Apparent Km (NAD+) (mM): 0.15 mM.

row_label: Q252L glucose dehydrogenase

table_label: PMC HTML Table 1 (PMID 15933031; PMCID PMC1151818)


column_label: PMCID PMC1151818 HTML Table 1; row E170K; column Apparent Km (NAD+) (mM); raw value 0.22 mM; normalized value 0.22 mM. Footnote a defines the pH 8.0, fixed 0.1 M glucose, and NAD+ concentration range.

normalized_value_unit_evidence: 0.22 mM is already normalized as 0.22 mM.

raw_value_unit_evidence: Table 1 row E170K, column Apparent Km (NAD+) (mM): 0.22 mM.

row_label: E170K glucose dehydrogenase


column_label: PMCID PMC1151818 HTML Table 1; row Q252L/E170K; column Apparent Km (NAD+) (mM); raw value 0.33 mM; normalized value 0.33 mM. Footnote a defines the pH 8.0, fixed 0.1 M glucose, and NAD+ concentration range.

normalized_value_unit_evidence: 0.33 mM is already normalized as 0.33 mM.

raw_value_unit_evidence: Table 1 row Q252L/E170K, column Apparent Km (NAD+) (mM): 0.33 mM.

row_label: Q252L/E170K glucose dehydrogenase


substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R454C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with deamino-NADP+

substrate: D-glucose 6-phosphate


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

proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with NADP+

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R454H to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant R454H, with NADP+


proof_lines: pH 8.0, 25°C, recombinant mutant R454H, with D-glucose 6-phosphate


proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with D-glucose 6-phosphate


proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with deoxy-D-glucose 6-phosphate


substrate_name: deamino-NADP+

substrate: deamino-NADP+


organism: Trypanosoma cruzi

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

assay_conditions_summary: pH 7.5; 298.15 K; buffer B (50 mM Tris pH 7; cofactor NADPH

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'L80G'; column 'KM G6P (uM)' = 74; column 'kcat (s^-1)' = 2.0; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.027.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 2.0 s^(-1). Km: printed Table 1 cell 74 uM; 74 / 1000 = 0.074 mM. kcat/Km: printed Table 1 cell 0.027 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.027 x 1000 = 27.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row L80G, G6P columns: KM G6P = 74 uM; kcat = 2.0 s^-1; printed kcat/KM G6P = 0.027 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row L80G, G6P columns


substrate_name: NADP+

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

assay_conditions_summary: pH 7.5; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1WBU6 and applied mutation signature K83A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K83A'; column 'KM G6P (uM)' = 537; column 'kcat (s^-1)' = 2.8; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.005.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.8 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 2.8 s^(-1). Km: printed Table 1 cell 537 uM; 537 / 1000 = 0.537 mM. kcat/Km: printed Table 1 cell 0.005 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.005 x 1000 = 5.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K83A, G6P columns: KM G6P = 537 uM; kcat = 2.8 s^-1; printed kcat/KM G6P = 0.005 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K83A, G6P columns


assay_conditions_summary: pH 7.5; 298.15 K; buffer B (50 mM Tris pH 7; cofactor NADP+

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K83A'; column 'KM NADP+ (uM)' = 21; column 'kcat (s^-1)' = 3.0; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 0.14.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 3.0 s^(-1). Km: printed Table 1 cell 21 uM; 21 / 1000 = 0.021 mM. kcat/Km: printed Table 1 cell 0.14 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.14 x 1000 = 140.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K83A, NADP+ columns: KM NADP+ = 21 uM; kcat = 3.0 s^-1; printed kcat/KM NADP+ = 0.14 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K83A, NADP+ columns


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

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'R408A'; column 'KM G6P (uM)' = 168; column 'kcat (s^-1)' = 15.0; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.089.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 15.0 s^(-1). Km: printed Table 1 cell 168 uM; 168 / 1000 = 0.168 mM. kcat/Km: printed Table 1 cell 0.089 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.089 x 1000 = 89.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row R408A, G6P columns: KM G6P = 168 uM; kcat = 15.0 s^-1; printed kcat/KM G6P = 0.089 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row R408A, G6P columns


column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'R408A'; column 'KM NADP+ (uM)' = 17; column 'kcat (s^-1)' = 19; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 1.1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 19 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 19.0 s^(-1). Km: printed Table 1 cell 17 uM; 17 / 1000 = 0.017 mM. kcat/Km: printed Table 1 cell 1.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.1 x 1000 = 1100.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row R408A, NADP+ columns: KM NADP+ = 17 uM; kcat = 19 s^-1; printed kcat/KM NADP+ = 1.1 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row R408A, NADP+ columns


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

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K84A'; column 'KM G6P (uM)' = 618; column 'kcat (s^-1)' = 24.6; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.04.

normalized_value_unit_evidence: kcat: printed Table 1 cell 24.6 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 24.6 s^(-1). Km: printed Table 1 cell 618 uM; 618 / 1000 = 0.618 mM. kcat/Km: printed Table 1 cell 0.04 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.04 x 1000 = 40.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K84A, G6P columns: KM G6P = 618 uM; kcat = 24.6 s^-1; printed kcat/KM G6P = 0.04 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K84A, G6P columns


column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'WT'; column 'KM NADP+ (uM)' = 16; column 'kcat (s^-1)' = 52; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 3.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 52 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 52.0 s^(-1). Km: printed Table 1 cell 16 uM; 16 / 1000 = 0.016 mM. kcat/Km: printed Table 1 cell 3.2 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.2 x 1000 = 3200.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row WT, NADP+ columns: KM NADP+ = 16 uM; kcat = 52 s^-1; printed kcat/KM NADP+ = 3.2 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row WT, NADP+ columns


column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K84A'; column 'KM NADP+ (uM)' = 17; column 'kcat (s^-1)' = 58; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 3.4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 58 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 58.0 s^(-1). Km: printed Table 1 cell 17 uM; 17 / 1000 = 0.017 mM. kcat/Km: printed Table 1 cell 3.4 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.4 x 1000 = 3400.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K84A, NADP+ columns: KM NADP+ = 17 uM; kcat = 58 s^-1; printed kcat/KM NADP+ = 3.4 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K84A, NADP+ columns


column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'WT'; column 'KM G6P (uM)' = 77; column 'kcat (s^-1)' = 62; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 62 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 62.0 s^(-1). Km: printed Table 1 cell 77 uM; 77 / 1000 = 0.077 mM. kcat/Km: printed Table 1 cell 0.8 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.8 x 1000 = 800.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row WT, G6P columns: KM G6P = 77 uM; kcat = 62 s^-1; printed kcat/KM G6P = 0.8 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row WT, G6P columns


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q1WBU6 and applied mutation signature K83A to reconstruct the assayed variant sequence.


substrate_name: 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.

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 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.

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/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 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 to reconstruct the assayed variant sequence.

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.


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/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.


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

assay_conditions_summary: pH 7.4; cofactor NADH

proof_lines: pH 7.4, reaction with 4-dionetestosterone


assay_conditions_summary: pH 7.4; cofactor NAD+


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

assay_conditions_summary: pH 7.4; cofactor NADP+


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


proof_lines:
pH 7.4, reaction with testosterone
pH 7.4, reaction with estradiol


substrate_name: testosterone

proof_lines:
pH 7.4, with NAD+ as cofactor
NADP+ as variable substrate

substrate: testosterone


substrate_name: estradiol

substrate: estradiol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G163S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G163D 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.

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


proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme, with D-glucose 6-phosphate


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


organism: Canis lupus familiaris

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

proof_lines: pH 7.4, 37°C, with D-glucose 6-phosphate or 2-deoxy-D-glucose 6-phosphate


proof_lines: pH 7.4, 37°C, with NADP+ or deamino-NADP+


proof_lines: pH 7.4, 37°C, with D-glucose 6-phosphate


organism: Bacillus amyloliquefaciens

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines: with NADP+ as cosubstrate,at pH 8.0 and 37°C


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


substrate_name: NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G488V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G488S to reconstruct the assayed variant sequence.


assay_conditions_summary: cofactor NADP+


organism: Lysinibacillus sphaericus

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


proof_lines:
with NADP+, pH 8.0, 25°C
with NAD+, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R393H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R393G to reconstruct the assayed variant sequence.


substrate_name: beta-D-glucose

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

proof_lines:
pH 7.5, 37°C, coenzyme NAD+, 37°C
pH 10.0, 37°C, coenzyme NAD+
pH 7.5, 37°C, coenzyme NADP+

substrate: beta-D-glucose


proof_lines:
37°C, pH 7.5, coenzyme NADP+
pH 10.0, 37°C, coenzyme NADP+
pH 10.0


proof_lines: pH 7.5, 37°C, reaction with D-glucose-6-phosphate

proof_lines: pH 10.0, 37°C, reaction with beta-D-glucose


organism: Bacillus thuringiensis serovar kurstaki

assay_conditions_summary: pH 9; 328.15 K; cofactor NADP+


assay_conditions_summary: pH 9; 328.15 K; cofactor NAD+


proof_lines: pH 7.6, temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 7.6; cofactor NADP+


proof_lines: substrate D-glucose 6-phosphate, pH 7.6, temperature not specified in the publication

proof_lines: substrate NADP+, pH 7.6, temperature not specified in the publication


organism: Bacillus subtilis

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


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADP+

proof_lines: pH 6.5, Km -value decreases with decreasing pH


substrate_name: D-glucosamine

substrate: D-glucosamine


organism: Bos taurus

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: isoform G6PD1, at pH 8.0, temperature not specified in the publication


assay_conditions_summary: cofactor NAD+


organism: Bacillus sp. (in: firmicutes)


organism: Ovis aries


organism: Arabidopsis thaliana


assay_conditions_summary: cofactor NADPH


organism: Nicotiana tabacum

proof_lines: G6PDH activity extracted from source leaves of wild-type tobacco Xanthi cultivars

proof_lines: G6PDH activity extracted from source leaves of wild-type tobacco SNN cultivars


enzyme_display_name: isocitrate dehydrogenase (NADP+)

organism: Staphylococcus aureus

substrate_name: isocitrate

enzyme: isocitrate dehydrogenase (NADP+)

substrate: isocitrate


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADP+

proof_lines:
pH 7.6, 25°C, leaf enzyme
pH 7.6, 25°C, root enzyme


substrate_name: D-isocitrate

substrate: D-isocitrate


substrate_name: D,L-isocitrate

substrate: D,L-isocitrate


substrate_name: DL-isocitrate

substrate: DL-isocitrate


organism: Thermus aquaticus

proof_lines:
25°C assay temperature
70°C assay temperature


organism: Archaeoglobus fulgidus


substrate: NAD+


organism: Lathyrus oleraceus


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

organism: Enterococcus faecalis


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


proof_lines:
coenzyme NAD+
coenzyme NADP+


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NADP+

proof_lines:
coenzyme NADP+
coenzyme NAD+
pH 9.5, 30°C, coenzyme NAD+


organism: Klebsiella pneumoniae

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer (pH 8.0), 20 mM MgCl2, at 25°C


assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl; cofactor NADP+


organism: Priestia megaterium


organism: Phormidium sp.


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 7.5; 338.15 K; cofactor NADP+

proof_lines: cosubstrate D-glucose, 65°C, pH not specified in the publication

proof_lines: cosubstrate D-glucose, 70°C, pH not specified in the publication


assay_conditions_summary: pH 7.5; 338.15 K; cofactor NAD+


organism: Nostoc sp.

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: pH 7.5, enzyme reduced with Nostoc sp. thioredoxin


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_exact_accession:P00350 and applied mutation signature Y378C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl; cofactor NADP+

column_label: Table 2 reports Ec6PGDH NADP+ Km (uM) = 49 +/- 7.

raw_value_unit_evidence: Km raw_value=49 +/- 7 uM raw_unit=uM

row_label: Ec6PGDH row / NADP+ Km column

table_label: ScienceDirect PMID 19686854 Table 2


column_label: Table 2 reports Ec6PGDH 6PG Km (uM) = 93 +/- 1.

raw_value_unit_evidence: Km raw_value=93 +/- 1 uM raw_unit=uM

row_label: Ec6PGDH row / 6PG Km column


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


proof_lines: pH 9.5, 30°C, reaction with D-glucose 6-phosphate


organism: Bacillus subtilis

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: 25°C, pH 8.0, high-level glucose-6-phosphate dehydrogenase strain DF82

proof_lines: pH 8.0, temperature not specified in the publication


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


enzyme_display_name: D-galactose 1-dehydrogenase

organism: Pseudomonas fluorescens

substrate_name: D-galactose

enzyme: D-galactose 1-dehydrogenase

substrate: D-galactose


assay_conditions_summary: cofactor NADP+


organism: Mus musculus

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


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


organism: Hordeum vulgare

assay_conditions_summary: 298.15 K; cofactor NADP+

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

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication


organism: Cavia porcellus

proof_lines: enzyme activity in microsomal fraction after centrifugation


enzyme_display_name: 17beta-estradiol 17-dehydrogenase

organism: Curvularia lunata

substrate_name: NADPH

enzyme: 17beta-estradiol 17-dehydrogenase

substrate: NADPH


proof_lines: 25°C, pH 8.0, wild-type enzyme, cosubstrate: 4-estrene-3,17-dione


enzyme_display_name: mannitol 2-dehydrogenase

organism: Tetraselmis subcordiformis

substrate_name: D-mannitol

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

assay_conditions_summary: cofactor NADH

enzyme: mannitol 2-dehydrogenase

substrate: D-mannitol


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Homo sapiens

proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.37 min(-1) for 3alpha-hydroxy-5alpha-androstan-17-one reduction (PubMed:10998348). kcat is 0.046 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one oxydation (PubMed:10998348).

enzyme: Aldo-keto reductase family 1 member C3


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


organism: Leuconostoc pseudomesenteroides

assay_conditions_summary: pH 8.6; cofactor NADH

column_label: The extracted paper text states the apparent Km for D-mannitol at 5 mM NAD+ is 12 mM and Table 4 lists D-mannitol Km as 12 mM, matching the expected row.

raw_value_unit_evidence: Km raw_value=12 raw_unit=mM

row_label: D-mannitol

table_label: Table 4 / purification properties paragraph


assay_conditions_summary: pH 5.4; cofactor NADH

column_label: The extracted paper text states the apparent Km for D-fructose at 200 uM NADH is 44 mM and Table 4 lists D-fructose Km as 44 mM, matching the expected row.

raw_value_unit_evidence: Km raw_value=44 raw_unit=mM

row_label: D-fructose


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table 1; row 2-Cyclohexen-1-ol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 7000 uM, 3.5 min^-1, 0.0005 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 7000 uM; kcat 3.5 min^-1; kcat/Km 0.0005 min^-1 uM^-1.

row_label: 2-Cyclohexen-1-ol / Rat 17HSD5

table_label: PMID 16788056 Table 1, non-steroidal substrates


substrate_name: Dimethylglyoxal

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

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: PMID 16788056 Table 1, non-steroidal substrates; row 2,3-Butanedione; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 126 uM, kcat 16 min^-1, kcat/Km 0.13 min^-1 uM^-1.

raw_value_unit_evidence: Km 126 uM; kcat 16 min^-1; kcat/Km 0.13 min^-1 uM^-1

row_label: 2,3-Butanedione / Rat 17HSD5

substrate: Dimethylglyoxal


column_label: Table 2; row 17beta-Estradiol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 14 uM, 25 min^-1, 1.8 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 Rat 17HSD5 cells: Km 14 uM; kcat 25 min^-1; kcat/Km 1.8 min^-1 uM^-1.

row_label: 17beta-Estradiol / Rat 17HSD5


substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: p-Nitrobenzaldehyde

column_label: Table 1; row 4-Nitrobenzaldehyde; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 11 uM, 7.9 min^-1, 0.72 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 11 uM; kcat 7.9 min^-1; kcat/Km 0.72 min^-1 uM^-1.

row_label: 4-Nitrobenzaldehyde / Rat 17HSD5

substrate: p-Nitrobenzaldehyde


column_label: Table 1; row S-Indan-1-ol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 3080 uM, 6.8 min^-1, 0.002 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 3080 uM; kcat 6.8 min^-1; kcat/Km 0.002 min^-1 uM^-1.

row_label: S-Indan-1-ol / Rat 17HSD5


column_label: Table 1; row trans-Benzene dihydrodiol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 2300 uM, 4.1 min^-1, 0.002 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 2300 uM; kcat 4.1 min^-1; kcat/Km 0.002 min^-1 uM^-1.

row_label: trans-Benzene dihydrodiol / Rat 17HSD5


organism: Drosophila melanogaster

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 NAD+

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


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

column_label: Table 3; Drosophila species columns; row 5α-Pregnan-20β-ol-3-one; Km column

normalized_value_unit_evidence: Km=0.009 mM converted from 9 uM

raw_value_unit_evidence: Table 3 Drosophila 5α-Pregnan-20β-ol-3-one Km 9 +/- 2 ×10^-6 M


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)

column_label: Table 3; Drosophila species columns; row Isoursodeoxycholic acid; Km column

normalized_value_unit_evidence: Km=0.003 mM converted from 3 uM

raw_value_unit_evidence: Table 3 Drosophila Isoursodeoxycholic acid Km 3 +/- 0.3 ×10^-6 M

row_label: Isoursodeoxycholic acid


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


enzyme_display_name: 4-hydroxybutyrate dehydrogenase

organism: Clostridium kluyveri

substrate_name: succinic semialdehyde

sequence_source: multiple

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

assay_conditions_summary: pH 6.1; cofactor NADH

column_label: The official abstract states Km values for NADH and succinic semialdehyde were 150 +/- 20 uM and 560 +/- 80 uM, respectively.

raw_value_unit_evidence: Km raw_value=560 +/- 80 raw_unit=uM

row_label: succinic semialdehyde

table_label: Official ScienceDirect abstract kinetic summary for purified 4-hydroxybutanoate dehydrogenase

source_databases_merged: brenda uniprot

enzyme: 4-hydroxybutyrate dehydrogenase

substrate: succinic semialdehyde


substrate_name: NAD

assay_conditions_summary: pH 9.4; cofactor NAD+

column_label: The official abstract states that in the reverse direction the Km values were 670 +/- 80 uM and 55 +/- 16 mM for NAD and 4-hydroxybutanoate, respectively.

raw_value_unit_evidence: Km raw_value=670 +/- 80 raw_unit=uM

row_label: NAD

substrate: NAD


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 6, substrate `4-Androstene-3,17-dione`, Rat 17HSD5 column group: Km = 1.6 uM (normalized 0.0016 mM); kcat = 2.0 min-1 (normalized 0.03333333333333333 s^-1); kcat/Km = 1.3 min-1 uM-1 (normalized 21.666666666666668 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 2.0 min-1 / 60 = 0.03333333333333333 s^-1; the catalog holds 0.033 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 1.3 min-1 uM-1, which is 1.3 x 1000 / 60 = 21.666666666666668 s^-1 mM^-1; the catalog holds 16.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 6, substrate `4-Androstene-3,17-dione`, Rat 17HSD5 column group: Km = 1.6 uM; kcat = 2.0 min-1; kcat/Km = 1.3 min-1 uM-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


substrate_name: testosterone

column_label: PMID 16788056 Table 2, steroid substrates; row Testosterone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 21 uM, kcat 21 min^-1, kcat/Km 1.0 min^-1 uM^-1.

raw_value_unit_evidence: Km 21 uM; kcat 21 min^-1; kcat/Km 1.0 min^-1 uM^-1

row_label: Testosterone / Rat 17HSD5

substrate: testosterone


enzyme_display_name: isocitrate dehydrogenase (NAD+)

organism: Saccharomyces cerevisiae

substrate_name: D,L-isocitrate

enzyme: isocitrate dehydrogenase (NAD+)


organism: Aspergillus niger

substrate_name: NADP+

substrate: NADP+


substrate_name: D-glucose 6-phosphate


substrate_name: Unknown

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: pH 8.0, temperature not specified in the publication, varied substrate: NADP+

proof_lines: 25°C, pH 8.0, competitive inhibition constant

proof_lines: pH 8.0, temperature not specified in the publication, varied substrate: glucose 6-phosphate, slope inhibition constant

substrate: Unknown


organism: Plasmodium falciparum

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Figure 2B, NADP+ x-axis panel, in-panel label Km: 8.6 uM; Results paragraph P24 repeats the same NADP+ Km value.

normalized_value_unit_evidence: 8.6 uM = 0.0086 mM; matches package/export Km 0.0086 mM.

raw_value_unit_evidence: Figure 2B labels the Michaelis-Menten fit for NADP+ as Km: 8.6 uM; Results paragraph P24 states the NADP+ Km was 8.6 uM for the ChemBridge batch.

row_label: NADP+ co-substrate Km

table_label: PMC8765527 Figure 2B and Results paragraph P24


proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: estradiol 17beta-dehydrogenase

substrate_name: NADPH; H+; Estrone

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

proof_lines: pH 7.4, 37°C recombinant His-tagged enzyme

proof_lines: pH and temperature not specified in the publication

enzyme: estradiol 17beta-dehydrogenase

substrate: NADPH; H+; Estrone


organism: Bos taurus

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+


organism: Pseudomonas sp.


organism: Mycobacterium tuberculosis

substrate_name: isocitrate

sequence_source: UniProt P9WKL1 inferred from PMID 23409873 and linked PDB 4HCX (ICDH-1 from Mycobacterium tuberculosis H37Rv / Rv3339c)

proof_lines: pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme

substrate: isocitrate


substrate: D,L-isocitrate


organism: Bacillus sp. (in: firmicutes)


enzyme_display_name: pyridoxine 4-dehydrogenase

organism: Schizosaccharomyces pombe

substrate_name: pyridoxal

assay_conditions_summary: cofactor NADPH

enzyme: pyridoxine 4-dehydrogenase

substrate: pyridoxal


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O93874 and applied mutation signature H111A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM phosphate; cofactor NADP+

column_label: Table 2 (Kinetic constants and Tm values for the wild-type and mutant 17beta-HSDcl), enzyme row 'His111Ala', NADP+ coenzyme axis; column 'KMNADP+ (uM)' = 4.6; column 'kcatNADP+ (s-1)' = 0.9; column 'kcat/KM, NADP+ (s-1M-1)' = 1.9 x 10^5; column '*KdNADP+ (uM)' = 5.8; column 'Tm (C)' = 37.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.9 s-1 in the kcatNADP+ (s-1) column; already in s^-1, so no unit conversion applies; the value is 0.9 s^(-1). Km: printed Table 2 cell 4.6 in the KMNADP+ (uM) column, which is headed uM; 4.6 / 1000 = 0.0046 mM; the value is 0.0046 mM. kcat/Km: printed Table 2 cell 1.9 x 10^5 under the head kcat/KM, NADP+ (s-1M-1), that is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^5 x 0.001 = 190.0 s^-1 mM^-1. The quotient of the two printed component cells of the same row is 0.9 / 0.0046 = 195.6521739130435 s^-1 mM^-1. That quotient lies outside the rounding interval of the printed efficiency cell, whose half-width at the printed precision is 5 x 10^3 M^-1 s^-1, so the printed cell is an independently reported primary value and this record reports it as 190.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row His111Ala, NADP+ axis: KMNADP+ (uM) = 4.6 uM; kcatNADP+ (s-1) = 0.9 s-1; printed kcat/KM, NADP+ (s-1M-1) = 1.9 x 10^5 M^-1 s^-1.

row_label: Table 2, row His111Ala, NADP+ axis

table_label: Table 2: Kinetic constants and Tm values for the wild-type and mutant 17beta-HSDcl (BMC Biochemistry 2005, 6:28)


organism: Sus scrofa

assay_conditions_summary: cofactor NADP+

substrate: NAD+


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

substrate_name: 5-alpha-androstan-3-alpha-ol-17-one (at 37 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 1; row 17-Ketosteroids / 5alpha-Androstan-3alpha-ol-17-one; Km column

normalized_value_unit_evidence: Km=0.0013 mM converted from 1.3 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / 5alpha-Androstan-3alpha-ol-17-one Km 1.3 uM

table_label: Table 1


substrate_name: dehydroepiandrosterone (DHEA) (at 37 degrees Celsius)

column_label: Table 1; row 17-Ketosteroids / DHEA; Km column

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / DHEA Km 11 uM

row_label: 17-Ketosteroids / DHEA

enzyme: Dehydrogenase/reductase SDR family member 11


substrate_name: DHEA sulfate (at 37 degrees Celsius)

column_label: Table 1; row 17-Ketosteroids / DHEA sulfate; Km column

normalized_value_unit_evidence: Km=0.012 mM converted from 12 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / DHEA sulfate Km 12 uM

row_label: 17-Ketosteroids / DHEA sulfate

substrate: DHEA sulfate (at 37 degrees Celsius)


substrate_name: dehydrolithocholic acid (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / Dehydrolithocholic acid; Km column

normalized_value_unit_evidence: Km=0.0011 mM converted from 1.1 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Dehydrolithocholic acid Km 1.1 uM


substrate_name: 20-alpha-hydroxyprogesterone (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / 20alpha-Hydroxyprogesterone; Km column

normalized_value_unit_evidence: Km=0.0051 mM converted from 5.1 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / 20alpha-Hydroxyprogesterone Km 5.1 uM


substrate_name: taurodehydrocholic acid (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / Taurodehydrocholic acid; Km column

normalized_value_unit_evidence: Km=0.044 mM converted from 44 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Taurodehydrocholic acid Km 44 uM


substrate_name: dehydrocholic acid (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / Dehydrocholic acid; Km column

normalized_value_unit_evidence: Km=0.029 mM converted from 29 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Dehydrocholic acid Km 29 uM

row_label: 3-Ketosteroids / Dehydrocholic acid


substrate_name: 5-beta-dihydrotestosterone (DHT) (at 37 degrees Celsius)


substrate_name: Isatin

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, Rat 17HSD5 column group: Km = 2.1 uM (normalized 0.0021000000000000003 mM); kcat = 11 min-1 (normalized 0.18333333333333332 s^-1); kcat/Km = 5.2 min-1 uM-1 (normalized 86.66666666666667 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, Rat 17HSD5 column group: Km = 2.1 uM; kcat = 11 min-1; kcat/Km = 5.2 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


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor NADH

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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 CoA


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


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)


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)

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


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

assay_conditions_summary: pH 7; cofactor NADH


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


organism: Aspergillus fumigatus

substrate_name: D-mannitol

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

substrate: D-mannitol


substrate_name: D-Xylulose

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NAD+

column_label: Table label: Table 1: AfM2DH substrate rows. Row: AfM2DH | D-Xylulose. Enzyme column group: AfM2DH. Columns read: kcat (s^-1) cell 64, open-chain-corrected Km (mM) cell 1.7, corrected kcat/Km (s^-1 mM^-1) cell 39. metric: kcat; raw value: 64; raw unit: s^-1; normalized value: 64.0 s^(-1); metric: Km; raw value: 1.7; raw unit: mM; normalized value: 1.7 mM; metric: kcat/Km; raw value: 39 +/- 2; raw unit: s^-1 mM^-1; normalized value: 39 s^-1 mM^-1; explicit printed primary cell; assay condition: ketose reduction at pH 7.1, Km and kcat/Km corrected for the available open-chain form of the carbonyl substrate; companion Table 2 measurements at 25 C and pH 7.1. Export row conditions: pH 7.1; 298.15 K.

normalized_value_unit_evidence: kcat raw 64 s^-1 -> 64.0 s^(-1); Km raw 1.7 mM -> 1.7 mM; explicit printed kcat/Km raw 39 +/- 2 s^-1 mM^-1 -> 39 s^-1 mM^-1. Conversion: 39 s^-1 mM^-1 requires no unit conversion. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 1: AfM2DH substrate rows | row: D-Xylulose, ketose reduction at pH 7.1: kcat `64 +/- 1 s^-1`; open-chain-corrected Km `1.7 +/- 0.1 mM`; corrected kcat/Km `39 +/- 2 s^-1 mM^-1`. | AfM2DH cells read: kcat = 64 s^-1; open-chain-corrected Km = 1.7 mM; corrected kcat/Km = 39 s^-1 mM^-1

row_label: AfM2DH | D-Xylulose

table_label: Table 1: AfM2DH substrate rows

substrate: D-Xylulose


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Mus musculus

substrate_name: all-trans-retinol

proof_lines:
mouse 17betaHSD9
retinol dehydrogenase activity

substrate: all-trans-retinol


organism: Pseudomonas fluorescens

substrate_name: D-arabitol

substrate: D-arabitol


proof_lines: mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C


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


organism: Gallus gallus

proof_lines:
in absence of bovine serum albumin
in presence of bovine serum albumin


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: cosubstrate NADP+, secretory endometrium


substrate_name: testosterone


substrate_name: androsterone

substrate: androsterone


substrate_name: D-fructose

assay_conditions_summary: pH 10; buffer 50 mM glycine/NaOH

proof_lines:
in 50 mM glycine/NaOH buffer at pH 10.0
recombinant protein

substrate: D-fructose


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -9, so it is treated as a source-provided variant sequence.


substrate_name: estrone

substrate: estrone


organism: Aeropyrum pernix

substrate_name: NADP+

assay_conditions_summary: pH 8; cofactor NADP+


organism: Cavia porcellus


substrate: testosterone


enzyme_display_name: 2-hydroxy-3-oxopropionate reductase

organism: Mycosarcoma maydis

protein_accession_database: NCBI Protein

sequence_source: paper_backed_accession:EAK83762.1 (PMID:21305026; archived GenBank protein for UM02592/Tsr1)

assay_conditions_summary: pH 8.5; cofactor NADH

column_label: Prose immediately above Table 1 reports Km 0.19 +/- 0.03 mM for tartronic semialdehyde in the reduction reaction.

raw_value_unit_evidence: Km raw_value=0.19 raw_unit=mM

row_label: Tartronic semialdehyde

table_label: Table 1. Kinetic parameters of rTsr1.

enzyme: 2-hydroxy-3-oxopropionate reductase


assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: Primary PMC HTML/JATS Table 1, Oxidation section, beta-NADP+ row, Km column = 0.30 +/- 0.04 uM.

normalized_value_unit_evidence: Normalized paper Km: 0.30 uM = 0.00030 mM, matching export Km 0.0003 mM.

raw_value_unit_evidence: Table 1 reports beta-NADP+ Km 0.30 +/- 0.04 uM.

row_label: Oxidation; beta-NADP+ row; Km column

table_label: Table 1. Kinetic parameters of rTsr1

substrate: NADP+


substrate_name: NADH

column_label: Primary PMC HTML/JATS Table 1, Reduction section, beta-NADH row, Km column = 14.29 +/- 3.1 uM.

normalized_value_unit_evidence: Normalized paper Km: 14.29 uM = 0.01429 mM; export has 0.0143 mM, matching by rounded value and within reported uncertainty.

raw_value_unit_evidence: Table 1 reports beta-NADH Km 14.29 +/- 3.1 uM.

row_label: Reduction; beta-NADH row; Km column

substrate: NADH


substrate_name: D-glycerate

column_label: Table 1 row D-Glycerate lists Km 17.7 +/- 2.3 mM.

raw_value_unit_evidence: Km raw_value=17.7 raw_unit=mM

row_label: D-Glycerate

substrate: D-glycerate


substrate_name: L-Glycerate

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

column_label: Table 1 row L-Glycerate lists Km 123.2 +/- 21.8 mM.

raw_value_unit_evidence: Km raw_value=123.2 raw_unit=mM

row_label: L-Glycerate

substrate: L-Glycerate


organism: Pseudomonas putida


organism: Rhodococcus sp. P14


organism: Thermotoga maritima

sequence_source: UniProt Q9WYD4 mapped from Thermotoga maritima TM_0298 / TM0298 named in PMID 18719905

assay_conditions_summary: pH 6.1; cofactor NADH

row_label: 60 C / pH 6.1 / NADH


substrate_name: NAD+

assay_conditions_summary: pH 8.3; cofactor NAD+


substrate_name: NADPH

assay_conditions_summary: pH 6.1; cofactor NADPH

column_label: Table 1 row 80 C, pH 6.1, NADPH under Km (mM): 0.17 +/- 0.017.

row_label: 80 C / pH 6.1 / NADPH

substrate: NADPH


column_label: Table 1 row 80 C, pH 8.3, D-Mannitol under Km (mM): 5.51 +/- 0.74.

row_label: 80 C / pH 8.3 / D-Mannitol


assay_conditions_summary: pH 8.3; cofactor NADP+

column_label: Table 1 row 80 C, pH 8.3, NADP+ under Km (mM): 7.5 +/- 0.53.

normalized_value_unit_evidence: Km 7.5 mM.


organism: Levilactobacillus brevis

assay_conditions_summary: cofactor NADH


assay_conditions_summary: cofactor NAD+


organism: Absidia glauca


organism: Curvularia lunata

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: 25°C, pH 8.0, mutant enzyme Y49D, cosubstrate: 4-estrene-3,17-dione


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: 25°C, pH 8.0, mutant enzyme Y49D, cosubstrate: 4-estrene-17beta-ol-3-one


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


proof_lines: 25°C, pH 8.0, mutant enzyme H164W, cosubstrate: 4-estrene-3,17-dione


proof_lines: 25°C, pH 8.0, mutant enzyme H164G, cosubstrate: 4-estrene-3,17-dione


proof_lines: 25°C, pH 8.0, mutant enzyme H164W, cosubstrate: 4-estrene-17beta-ol-3-one


proof_lines: 25°C, pH 8.0, mutant enzyme H164G, cosubstrate: 4-estrene-17beta-ol-3-one


assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM phosphate; cofactor NADP+

column_label: Table 2 (Kinetic constants and Tm values for the wild-type and mutant 17beta-HSDcl), enzyme row 'Wild type', NADP+ coenzyme axis; column 'KMNADP+ (uM)' = 0.06; column 'kcatNADP+ (s-1)' = 0.65; column 'kcat/KM, NADP+ (s-1M-1)' = 1.1 x 10^7; column '*KdNADP+ (uM)' = 0.2; column 'Tm (C)' = 44.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.65 s-1 in the kcatNADP+ (s-1) column; already in s^-1, so no unit conversion applies; the value is 0.65 s^(-1). Km: printed Table 2 cell 0.06 in the KMNADP+ (uM) column, which is headed uM; 0.06 / 1000 = 0.00006 mM; the value is 0.00006 mM. kcat/Km: printed Table 2 cell 1.1 x 10^7 under the head kcat/KM, NADP+ (s-1M-1), that is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^7 x 0.001 = 11000.0 s^-1 mM^-1. The quotient of the two printed component cells of the same row is 0.65 / 0.00006 = 10833.333333333334 s^-1 mM^-1. That quotient lies inside the rounding interval of the printed efficiency cell, whose half-width at the printed precision is 5 x 10^5 M^-1 s^-1, so the printed cell is the paper's own two-significant-figure rendering of the same quotient and the catalog value is kept.

raw_value_unit_evidence: Table 2, row Wild type, NADP+ axis: KMNADP+ (uM) = 0.06 uM; kcatNADP+ (s-1) = 0.65 s-1; printed kcat/KM, NADP+ (s-1M-1) = 1.1 x 10^7 M^-1 s^-1.

row_label: Table 2, row Wild type, NADP+ axis


column_label: Table 2 (Kinetic constants and Tm values for the wild-type and mutant 17beta-HSDcl), enzyme row 'His111Ala', NADP+ coenzyme axis; column 'KMNADP+ (uM)' = 4.6; column 'kcatNADP+ (s-1)' = 0.9; column 'kcat/KM, NADP+ (s-1M-1)' = 1.9 x 10^5; column '*KdNADP+ (uM)' = 5.8; column 'Tm (C)' = 37.


assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM phosphate; cofactor NADPH

column_label: Table 2 (Kinetic constants and Tm values for the wild-type and mutant 17beta-HSDcl), enzyme row 'His111Ala', NADPH coenzyme axis; column 'KMNADPH (uM)' = 50.6; column 'kcatNADPH (s-1)' = 2.4; column 'kcat/KM, NADPH (s-1M-1)' = 4.7 x 10^4; column '*KdNADP+ (uM)' = 5.8; column 'Tm (C)' = 37.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.4 s-1 in the kcatNADPH (s-1) column; already in s^-1, so no unit conversion applies; the value is 2.4 s^(-1). Km: printed Table 2 cell 50.6 in the KMNADPH (uM) column, which is headed uM; 50.6 / 1000 = 0.0506 mM; the value is 0.0506 mM. kcat/Km: printed Table 2 cell 4.7 x 10^4 under the head kcat/KM, NADPH (s-1M-1), that is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.7 x 10^4 x 0.001 = 47.0 s^-1 mM^-1. The quotient of the two printed component cells of the same row is 2.4 / 0.0506 = 47.43083003952569 s^-1 mM^-1. That quotient lies inside the rounding interval of the printed efficiency cell, whose half-width at the printed precision is 5 x 10^2 M^-1 s^-1, so the printed cell is the paper's own two-significant-figure rendering of the same quotient and the catalog value is kept.

raw_value_unit_evidence: Table 2, row His111Ala, NADPH axis: KMNADPH (uM) = 50.6 uM; kcatNADPH (s-1) = 2.4 s-1; printed kcat/KM, NADPH (s-1M-1) = 4.7 x 10^4 M^-1 s^-1.

row_label: Table 2, row His111Ala, NADPH axis


column_label: Table 2 (Kinetic constants and Tm values for the wild-type and mutant 17beta-HSDcl), enzyme row 'Wild type', NADPH coenzyme axis; column 'KMNADPH (uM)' = 6.5; column 'kcatNADPH (s-1)' = 3.8; column 'kcat/KM, NADPH (s-1M-1)' = 5.8 x 10^5; column '*KdNADP+ (uM)' = 0.2; column 'Tm (C)' = 44.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.8 s-1 in the kcatNADPH (s-1) column; already in s^-1, so no unit conversion applies; the value is 3.8 s^(-1). Km: printed Table 2 cell 6.5 in the KMNADPH (uM) column, which is headed uM; 6.5 / 1000 = 0.0065 mM; the value is 0.0065 mM. kcat/Km: printed Table 2 cell 5.8 x 10^5 under the head kcat/KM, NADPH (s-1M-1), that is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.8 x 10^5 x 0.001 = 580.0 s^-1 mM^-1. The quotient of the two printed component cells of the same row is 3.8 / 0.0065 = 584.6153846153846 s^-1 mM^-1. That quotient lies inside the rounding interval of the printed efficiency cell, whose half-width at the printed precision is 5 x 10^3 M^-1 s^-1, so the printed cell is the paper's own two-significant-figure rendering of the same quotient and the catalog value is kept.

raw_value_unit_evidence: Table 2, row Wild type, NADPH axis: KMNADPH (uM) = 6.5 uM; kcatNADPH (s-1) = 3.8 s-1; printed kcat/KM, NADPH (s-1M-1) = 5.8 x 10^5 M^-1 s^-1.

row_label: Table 2, row Wild type, NADPH axis


organism: Leuconostoc mesenteroides


sequence_source: GenBank AY090766.1 CDS / protein AAM09029.1 linked from PMID 12226722 (Leuconostoc mesenteroides ATCC 9135 mdh)


organism: Bradyrhizobium japonicum


organism: Porphyromonas gingivalis

substrate_name: succinate semialdehyde

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: with NADH as cosubstrate, at pH 8.0 and 37°C

substrate: succinate semialdehyde


assay_conditions_summary: pH 9


organism: Tetraselmis subcordiformis


organism: Montipora capitata

assay_conditions_summary: cofactor NADP+


organism: Sus scrofa


substrate: NAD+


organism: Fructilactobacillus sanfranciscensis


proof_lines:
isoenzyme 2
isoenzyme 1


assay_conditions_summary: cofactor NADPH


substrate_name: androstenedione

substrate: androstenedione


substrate_name: benzene dihydrodiol

proof_lines:
isoenzyme 1
isoenzyme 2

substrate: benzene dihydrodiol


organism: Canis lupus familiaris

substrate_name: Unknown

substrate: Unknown


assay_conditions_summary: pH 7; buffer pH 7; cofactor NAD+

column_label: Accepted manuscript page 14 states the kinetic constants for purified H6-17beta-HSD: Km, Vmax, kcat, and kcat/Km values are 18.9 uM, 12.5 umol/min/mg, 9.38 s^-1, and 4.96 x 10^5 s^-1 M^-1, respectively.

normalized_value_unit_evidence: Km normalized_value=0.0189 normalized_unit=mM; kcat normalized_value=9.38 normalized_unit=s^-1; kcat/Km normalized_value=496.29629629629636 normalized_unit=s^-1 mM^-1 from 9.38 / 0.0189.

raw_value_unit_evidence: Km raw_value=18.9 raw_unit=uM; kcat raw_value=9.38 raw_unit=s^-1; kcat/Km printed_value=4.96 x 10^5 printed_unit=s^-1 M^-1.

row_label: Purified H6-17beta-HSD from Rhodococcus sp. P14 with estradiol

table_label: Accepted manuscript page 14 kinetic-constant prose


organism: Thermotoga neapolitana

proof_lines:
pH 6.5, 90°C
at pH 6.5 and 90°C


organism: Homo sapiens

substrate_name: NAD

proof_lines: The kinetic parameters were determined using microsomes from transfected cells.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6

substrate: NAD


substrate_name: NADP

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: allopregnanolone

substrate: allopregnanolone


substrate_name: androsterone

substrate: androsterone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


enzyme_display_name: Aldo-keto reductase family 1 member C4

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4; columns Km (uM), 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 catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4: Km 10.5 uM; kcat 2.1 min^-1; kcat/Km 200 min^-1 mM^-1.

enzyme: Aldo-keto reductase family 1 member C4


proof_lines: kcat is 1.99 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction. kcat is 1.79 min(-1) for 5alpha-androstan-3,17-dione reduction. kcat is 2.1 min(-1) for 5alpha-androstane-3alpha,17beta-diol oxydation. kcat is 1.39.1 min(-1) for 3al


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4; columns Km (uM), 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 catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4: Km 1.44 uM; kcat 1.79 min^-1; kcat/Km 1243 min^-1 mM^-1.


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


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: progesterone (reduction)

column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Progesterone reduction / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Progesterone reduction / AKR1C1: Km 2.65 uM; kcat 0.29 min^-1; kcat/Km 109 min^-1 mM^-1.

row_label: Progesterone reduction / AKR1C1

enzyme: Aldo-keto reductase family 1 member C1

substrate: progesterone (reduction)


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1: Km 16.2 uM; kcat 1.10 min^-1; kcat/Km 68 min^-1 mM^-1.


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1: Km 14.7 uM; kcat 1.20 min^-1; kcat/Km 82 min^-1 mM^-1.


column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R); columns Km (uM), 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 catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R): Km 80.6 uM; kcat 0.66 min^-1; kcat/Km 8 min^-1 mM^-1.

row_label: 5alpha-DHT reduction / AKR1C1 (R)


column_label: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R): Km 39.8 uM; kcat 0.044 min^-1; kcat/Km 1.1 min^-1 mM^-1.

row_label: Testosterone oxidation / AKR1C1 (R)


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1: Km 19.4 uM; kcat 3.23 min^-1; kcat/Km 167 min^-1 mM^-1.


enzyme_display_name: Aldo-keto reductase family 1 member C2

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2; columns Km (uM), 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 catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2: Km 22.0 uM; kcat 0.24 min^-1; kcat/Km 11 min^-1 mM^-1.

enzyme: Aldo-keto reductase family 1 member C2


substrate_name: (s)-tetralol

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

substrate: (s)-tetralol


substrate_name: (s)-tetralol (oxidation)

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

substrate: (s)-tetralol (oxidation)


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


enzyme_display_name: Aldo-keto reductase family 1 member B15

substrate_name: all-trans-retinal

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 min(-1) using isoform 1 for the reduction of androsterone. kcat is 1.1 min(-1) using isoform 1 for the reduction of delta-4-androstenedione. kcat is 1.0 min(-1) using isoform 1 for the reduction of estrone. kcat is 0.5 min(-1) u

enzyme: Aldo-keto reductase family 1 member B15

substrate: all-trans-retinal


substrate_name: D,L-glyceraldehyde

smiles: OCC(O)C=O

substrate: D,L-glyceraldehyde