sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y100H/S148A/E156V to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / Y100H/S148A/E156V; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / Y100H/S148A/E156V; kcat 4.86 s^-1, kcat_over_km 405 s^-1 mM^-1, km 0.012 mM.

normalized_value_unit_evidence: kcat normalized value: 4.86; normalized unit: s^-1; kcat_over_km normalized value: 405; normalized unit: s^-1 mM^-1; km normalized value: 0.012; normalized unit: mM

raw_value_unit_evidence: km raw value: 12.4 ± 1.4; raw unit: uM; kcat raw value: 4.86 ± 0.30; raw unit: s^-1; kcat_over_km raw value: 4.86 / 0.012; raw unit: s^-1 per mM after normalizing Km to row/export precision


enzyme_display_name: tropinone reductase II

organism: Datura stramonium

substrate_name: tropinone

source_db: oed

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50163 and applied mutation signature E156V with inferred residue-numbering offset -36 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 301.15 K; cofactor NADPH

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / E156V; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / E156V; kcat 1.11 s^-1, kcat_over_km 0.038675958188153316 s^-1 mM^-1, km 28.7 mM.

normalized_value_unit_evidence: kcat normalized value: 1.11; normalized unit: s^-1; kcat_over_km normalized value: 0.038675958188153316; normalized unit: s^-1 mM^-1; km normalized value: 28.7; normalized unit: mM

raw_value_unit_evidence: km raw value: 28.7 ± 4.44; raw unit: mM; kcat raw value: 1.11 ± 0.07; raw unit: s^-1; kcat_over_km raw value: 1.11 / 28.7; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-II / E156V

data_origin: experimental

enzyme: tropinone reductase II

substrate: tropinone

status: verified

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L210I/L213F to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / L210I/L213F; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / L210I/L213F; kcat 1.88 s^-1, kcat_over_km 41.77777777777778 s^-1 mM^-1, km 0.045 mM.

normalized_value_unit_evidence: kcat normalized value: 1.88; normalized unit: s^-1; kcat_over_km normalized value: 41.77777777777778; normalized unit: s^-1 mM^-1; km normalized value: 0.045; normalized unit: mM

raw_value_unit_evidence: km raw value: 0.0448 ± 0.0072; raw unit: mM; kcat raw value: 1.88 ± 0.11; raw unit: s^-1; kcat_over_km raw value: 1.88 / 0.045; raw unit: s^-1 per mM after normalizing Km to row/export precision


mutation_signature: Unknown

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

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / Wild type; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / Wild type; kcat 2.73 s^-1, kcat_over_km 56.875 s^-1 mM^-1, km 0.048 mM.

normalized_value_unit_evidence: kcat normalized value: 2.73; normalized unit: s^-1; kcat_over_km normalized value: 56.875; normalized unit: s^-1 mM^-1; km normalized value: 0.048; normalized unit: mM

raw_value_unit_evidence: km raw value: 0.0476 ± 0.0122; raw unit: mM; kcat raw value: 2.73 ± 0.16; raw unit: s^-1; kcat_over_km raw value: 2.73 / 0.048; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-II / Wild type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y100H to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / Y100H; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / Y100H; kcat 6.84 s^-1, kcat_over_km 1.5 s^-1 mM^-1, km 4.56 mM.

normalized_value_unit_evidence: kcat normalized value: 6.84; normalized unit: s^-1; kcat_over_km normalized value: 1.5; normalized unit: s^-1 mM^-1; km normalized value: 4.56; normalized unit: mM

raw_value_unit_evidence: km raw value: 4.56 ± 0.23; raw unit: mM; kcat raw value: 6.84 ± 0.16; raw unit: s^-1; kcat_over_km raw value: 6.84 / 4.56; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-II / Y100H


enzyme_display_name: Tropinone reductase

organism: Cochlearia officinalis

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: pH 6.4; cofactor NADPH

column_label: Table 1; C. officinalis CoTR; row Tropinone; K_M (SD) (uM) column; raw 3290 (633) uM.

raw_value_unit_evidence: Table 1 Tropinone K_M cell: 3290 (633) uM

row_label: Tropinone

table_label: PMID 18221363 Table 1, C. officinalis CoTR kinetic properties

enzyme: Tropinone reductase

source: uniprot


substrate_name: nortropinone

column_label: Table 1; C. officinalis CoTR; row Nortropinone; K_M (SD) (uM) column; raw 2002 (863) uM.

raw_value_unit_evidence: Table 1 Nortropinone K_M cell: 2002 (863) uM

row_label: Nortropinone

substrate: nortropinone


column_label: Table 1; C. officinalis CoTR; row TBON; K_M (SD) (uM) column; raw 42 (0 02) uM.

raw_value_unit_evidence: Table 1 TBON K_M cell: 42 (0 02) uM

row_label: TBON


substrate_name: quinuclidinone

column_label: Table 1; C. officinalis CoTR; row Quinuclidinone; K_M (SD) (uM) column; raw 2636 (338) uM.

raw_value_unit_evidence: Table 1 Quinuclidinone K_M cell: 2636 (338) uM

row_label: Quinuclidinone

substrate: quinuclidinone


column_label: Table 1; C. officinalis CoTR; row 3-methylcyclohexanone; K_M (SD) (uM) column; raw 13 (1.97) uM.

raw_value_unit_evidence: Table 1 3-methylcyclohexanone K_M cell: 13 (1.97) uM


column_label: Table 1; C. officinalis CoTR; row 4-methylcyclohexanone; K_M (SD) (uM) column; raw 15 (4.45) uM.

raw_value_unit_evidence: Table 1 4-methylcyclohexanone K_M cell: 15 (4.45) uM


enzyme_display_name: hydroxyphenylpyruvate reductase

organism: Wickerhamia fluorescens

substrate_name: glyoxylate

smiles: O=CC(=O)O

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH

column_label: ScienceDirect full-text Table 2 row Glyoxylate with fixed substrate NADPH gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 18.9 mM; kcat 19 s^-1; kcat/Km 1.0052910052910053 s^-1*mM^-1 from the same row quotient 19/18.9; printed kcat/Km is rounded.

row_label: Glyoxylate / NADPH

table_label: Table 2. Kinetic properties of PPR isolated from W. fluorescens TK1

enzyme: hydroxyphenylpyruvate reductase

substrate: glyoxylate


substrate_name: hydroxyphenylpyruvate

column_label: ScienceDirect full-text Table 2 row Hydroxyphenylpyruvate with fixed substrate NADPH gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 0.64 mM; kcat 73 s^-1; kcat/Km 114.0625 s^-1*mM^-1 from the same row quotient 73/0.64; printed kcat/Km is rounded.

row_label: Hydroxyphenylpyruvate / NADPH

substrate: hydroxyphenylpyruvate


substrate_name: Hydroxypyruvate

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

column_label: ScienceDirect full-text Table 2 row Hydroxypyruvate with fixed substrate NADPH gives all three metric columns.

row_label: Hydroxypyruvate / NADPH

substrate: Hydroxypyruvate


substrate_name: NADH

column_label: ScienceDirect full-text Table 2 row NADH with fixed substrate PPA gives all three metric columns.

row_label: NADH / PPA

substrate: NADH


substrate_name: NADPH

column_label: ScienceDirect full-text Table 2 row NADPH with fixed substrate PPA gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 0.01 mM; kcat 121 s^-1; kcat/Km 12100 s^-1*mM^-1 from the same row quotient 121/0.010; printed kcat/Km is rounded.

row_label: NADPH / PPA

substrate: NADPH


substrate_name: phenylpyruvate

column_label: ScienceDirect full-text Table 2 row Phenylpyruvate with fixed substrate NADPH gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 0.4 mM; kcat 150 s^-1; kcat/Km 375 s^-1*mM^-1 from the same row quotient 150/0.40; printed kcat/Km is rounded.

row_label: Phenylpyruvate / NADPH

substrate: phenylpyruvate


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Bos taurus

substrate_name: prostaglandin D2

verification_status: unverified

proof_lines:
prostaglandin D2
Bos taurus
prostaglandin F synthase

enzyme: Aldo-keto reductase family 1 member C3

substrate: prostaglandin D2

status: unverified


proof_lines:
9,10-phenanthroquinone
Bos taurus
prostaglandin F synthase


substrate_name: menadione

proof_lines:
menadione
Bos taurus
prostaglandin F synthase

substrate: menadione


assay_conditions_summary: cofactor NADPH

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

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

row_label: PGFS / 4-nitrobenzaldehyde


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 2

organism: Homo sapiens

substrate_name: estradiol

assay_conditions_summary: pH 7.4; cofactor NAD+

column_label: Table I, row Estradiol -> Estrone; NAD+, column K_m (uM).

normalized_value_unit_evidence: Km=0.00021 mM converted from 0.21 uM.

raw_value_unit_evidence: Table I reports Estradiol -> Estrone; NAD+ Km=0.21 +/- 0.04 uM.

row_label: Estradiol -> Estrone; NAD+

table_label: Table I: Characterization in vitro of human 17beta-HSD type 2 expressed in transfected 293 cells

substrate: estradiol


substrate_name: testosterone

column_label: Table I, row Testosterone -> Androstenedione; NAD+, column K_m (uM).

normalized_value_unit_evidence: Km=0.00039 mM converted from 0.39 uM.

raw_value_unit_evidence: Table I reports Testosterone -> Androstenedione; NAD+ Km=0.39 +/- 0.09 uM.

row_label: Testosterone -> Androstenedione; NAD+

enzyme: 17-beta-hydroxysteroid dehydrogenase type 2

substrate: testosterone


substrate_name: dihydrotestosterone

column_label: Table III row Dihydrotestosterone / cofactor NAD / Km app column = 0.25 +/- 0.11 uM.

row_label: Dihydrotestosterone row; cofactor NAD

table_label: Table III. Kinetic constants of substrates in the oxidation reaction with purified reconstituted His6-tagged 17beta-HSD2

substrate: dihydrotestosterone


column_label: Table III row 20alpha-Dihydroprogesterone P / cofactor NAD / Km app column = 0.53 +/- 0.22 uM.

row_label: 20alpha-Dihydroprogesterone P row; cofactor NAD


substrate_name: androstenedione

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Table I, row Androstenedione -> Testosterone; NADH, column K_m (uM).

normalized_value_unit_evidence: Km=0.00263 mM converted from 2.63 uM.

raw_value_unit_evidence: Table I reports Androstenedione -> Testosterone; NADH Km=2.63 +/- 0.20 uM.

row_label: Androstenedione -> Testosterone; NADH

substrate: androstenedione


substrate_name: estrone

column_label: Table I, row Estrone -> Estradiol; NADH, column K_m (uM).

normalized_value_unit_evidence: Km=0.00078 mM converted from 0.78 uM.

raw_value_unit_evidence: Table I reports Estrone -> Estradiol; NADH Km=0.78 +/- 0.08 uM.

row_label: Estrone -> Estradiol; NADH

substrate: estrone


enzyme_display_name: (3R)-3-hydroxyacyl-CoA dehydrogenase

organism: Mus musculus

assay_conditions_summary: buffer 50 mM Hepes

column_label: Results prose tied to Fig. 5; substrate row estradiol/E2; metric label Km; raw unit uM; Fig. 5A Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.110 uM / 1000 = 0.000110 mM; required UniProt Km row value is 0.00011 mM.

raw_value_unit_evidence: Results prose / Fig. 5A: estradiol Km = 0.110 +/- 0.02 uM.

row_label: estradiol (E2), Fig. 5A

table_label: Results prose and Fig. 5

enzyme: (3R)-3-hydroxyacyl-CoA dehydrogenase


column_label: Results prose tied to Fig. 5; substrate row testosterone/T; metric label Km; raw unit uM; Fig. 5B Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.422 uM / 1000 = 0.000422 mM; required UniProt Km row value is 0.000422 mM.

raw_value_unit_evidence: Results prose / Fig. 5B: testosterone Km = 0.422 +/- 0.063 uM.

row_label: testosterone (T), Fig. 5B


assay_conditions_summary: buffer potassium phosphate; cofactor NADPH

column_label: Results prose tied to Fig. 5; substrate row estrone/E1; metric label Km; raw unit uM; Fig. 5D Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.368 uM / 1000 = 0.000368 mM; required UniProt Km row value is 0.000368 mM.

raw_value_unit_evidence: Results prose / Fig. 5D: estrone Km = 0.368 +/- 0.063 uM.

row_label: estrone (E1), Fig. 5D


column_label: Results prose tied to Fig. 5; substrate row dihydrotestosterone/DHT; metric label Km; raw unit uM; Fig. 5C Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.360 uM / 1000 = 0.000360 mM; required UniProt Km row value is 0.00036 mM.

raw_value_unit_evidence: Results prose / Fig. 5C: dihydrotestosterone Km = 0.360 +/- 0.04 uM.

row_label: dihydrotestosterone (DHT), Fig. 5C


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

assay_conditions_summary: pH 9; buffer 0.25 ml CHES; cofactor NAD+

column_label: Official OUP Table 5; row 3alpha-Adiolb; column K0.5 (uM); raw value 1.4; normalized km 0.0014 mM

normalized_value_unit_evidence: K0.5=0.0014 mM for km field; raw 1.4 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row 3alpha-Adiolb; column K0.5 (uM); raw cell 1.4 uM.


substrate_name: androsterone

column_label: Official OUP Table 5; row Androsterone; column K0.5 (uM); raw value 1.3; normalized km 0.0013 mM

normalized_value_unit_evidence: K0.5=0.0013 mM for km field; raw 1.3 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row Androsterone; column K0.5 (uM); raw cell 1.3 uM.

row_label: Androsterone

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6

substrate: androsterone


substrate_name: all-trans-retinol

column_label: Official OUP Table 5; row All-trans-retinol; column K0.5 (uM); raw value 3.2; normalized km 0.0032 mM

normalized_value_unit_evidence: K0.5=0.0032 mM for km field; raw 3.2 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row All-trans-retinol; column K0.5 (uM); raw cell 3.2 uM.

row_label: All-trans-retinol

substrate: all-trans-retinol


column_label: Official OUP Table 5; row Estradiol; column K0.5 (uM); raw value 1.5; normalized km 0.0015 mM

normalized_value_unit_evidence: K0.5=0.0015 mM for km field; raw 1.5 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row Estradiol; column K0.5 (uM); raw cell 1.5 uM.

row_label: Estradiol


organism: Atropa belladonna

source_db: brenda

source: brenda


substrate_name: tropinone

substrate: tropinone


enzyme_display_name: Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase

organism: Malus domestica

substrate_name: eriodictyol

column_label: Table 2 reports Malus cv. 'Weirouge' substrate ERI (eriodictyol), Km (μM) = 3.9; normalized Km = 0.0039 mM.

normalized_value_unit_evidence: Km=0.0039 mM after μM to mM conversion from Table 2 3.9 μM.

raw_value_unit_evidence: 3.9 μM in Table 2 Km (μM) column

row_label: Malus cv. 'Weirouge' / ERI (eriodictyol) / Km (μM) column

table_label: Table 2 / Overview of kinetic data obtained with the heterologously expressed DFR enzymes from Malus domestica cv. 'Weirouge' and Pyrus communis cv. 'Pyrodwarf'

substrate: eriodictyol


substrate_name: dihydrokaempferol

column_label: Table 2 reports Malus cv. 'Weirouge' substrate DHK (dihydrokaempferol), Km (μM) = 34.0; normalized Km = 0.034 mM.

normalized_value_unit_evidence: Km=0.034 mM after μM to mM conversion from Table 2 34.0 μM.

raw_value_unit_evidence: 34.0 μM in Table 2 Km (μM) column

row_label: Malus cv. 'Weirouge' / DHK (dihydrokaempferol) / Km (μM) column

enzyme: Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase

substrate: dihydrokaempferol


substrate_name: dihydroquercetin

column_label: Table 2 reports Malus cv. 'Weirouge' substrate DHQ (dihydroquercetin), Km (μM) = 26.0; normalized Km = 0.026 mM.

normalized_value_unit_evidence: Km=0.026 mM after μM to mM conversion from Table 2 26.0 μM.

raw_value_unit_evidence: 26.0 μM in Table 2 Km (μM) column

row_label: Malus cv. 'Weirouge' / DHQ (dihydroquercetin) / Km (μM) column

substrate: dihydroquercetin


verification_status: corrected

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 3; row 5alpha-Dihydrotestosterone oxidation / AKR1C3; columns Km (microM), kcat (min^-1), kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 reports 5alpha-dihydrotestosterone oxidation / AKR1C3: Km=11.9 +/- 4.4 microM, kcat=0.046 min^-1, kcat/Km=3.8 min^-1 mM^-1.

table_label: Table 3

status: corrected


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 2; row 5alpha-Androstane-3,17-dione reduction / AKR1C3; columns kcat (min^-1), kcat/Km (min^-1 mM^-1), and Km (microM).

normalized_value_unit_evidence: Converted: kcat=0.28/60=0.004667 s^-1; Km=0.005 mM; kcat/Km=56/60=0.9333 s^-1 mM^-1. Export values 0.005 and 1.0 are supported by rounded table conversion.

raw_value_unit_evidence: Table 2 reports 5alpha-androstane-3,17-dione reduction / AKR1C3: Km=5.00 +/- 0.86 microM, kcat=0.28 min^-1, kcat/Km=56 min^-1 mM^-1.

table_label: Table 2


proof_lines:
3alpha-hydroxy-5alpha-androstan-17-one
androsterone
KM 8.96 uM


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)O)O

column_label: Abstract reports apparent values of Km of 8.3 microM and Vmax of 2.8 nmoles/mg.min in the oxidation of 15-HETE.

raw_value_unit_evidence: Km raw_value=8.3 microM raw_unit=microM

row_label: Mouse liver microsomal 15-HETE dehydrogenase / 15-HETE

table_label: PubMed XML abstract PMID 3052453


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

column_label: Results prose reports that at 200 microM 15-HETE the apparent Michaelis constant for NAD was 60 microM.

raw_value_unit_evidence: Km raw_value=60 microM raw_unit=microM

row_label: Mouse liver microsomal 15-HETE dehydrogenase / NAD cosubstrate

table_label: Results prose, journal page 527 (PDF page 4)

substrate: NAD+


organism: Pyrus communis

column_label: Table 2 reports Pyrus cv. 'Pyrodwarf' substrate ERI (eriodictyol), Km (μM) = 3.8; normalized Km = 0.0038 mM.

normalized_value_unit_evidence: Km=0.0038 mM after μM to mM conversion from Table 2 3.8 μM.

raw_value_unit_evidence: 3.8 μM in Table 2 Km (μM) column

row_label: Pyrus cv. 'Pyrodwarf' / ERI (eriodictyol) / Km (μM) column


column_label: Table 2 reports Pyrus cv. 'Pyrodwarf' substrate DHQ (dihydroquercetin), Km (μM) = 3.0; normalized Km = 0.003 mM.

normalized_value_unit_evidence: Km=0.003 mM after μM to mM conversion from Table 2 3.0 μM.

raw_value_unit_evidence: 3.0 μM in Table 2 Km (μM) column

row_label: Pyrus cv. 'Pyrodwarf' / DHQ (dihydroquercetin) / Km (μM) column


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

sequence_source: multiple

proof_lines:
tropinone reductase II
tropinone
Datura stramonium

source_databases_merged: brenda skid


proof_lines:
tropinone reductase II
kinetic characterisation
Datura stramonium


substrate_name: NAD

column_label: The abstract reports the Km of NAD being 110+/-10 microM and that of NADP 9600+/-100 microM using estradiol as substrate.

raw_value_unit_evidence: Km raw_value=110 microM raw_unit=microM

row_label: Prose segment: NAD Km

table_label: PubMed PMID 11940569 abstract

substrate: NAD


substrate_name: NADP

raw_value_unit_evidence: Km raw_value=9600 microM raw_unit=microM

row_label: Prose segment: NADP Km

substrate: NADP


enzyme_display_name: N-acylmannosamine 1-dehydrogenase

organism: Flavobacterium sp.

substrate_name: N-glycolyl-D-mannosamine

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

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Abstract reports apparent Km values for N-acetyl- and N-glycolyl-D-mannosamine and NAD+ were 1.0, 13.3, and 0.41 mM, respectively.

raw_value_unit_evidence: Km raw_value=13.3 mM raw_unit=mM

row_label: N-acyl-D-mannosamine dehydrogenase / N-glycolyl-D-mannosamine

table_label: PubMed XML abstract PMID 3240988

enzyme: N-acylmannosamine 1-dehydrogenase

substrate: N-glycolyl-D-mannosamine


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 288.15 K; cofactor NADPH

proof_lines: two crystal structures of enzyme-substrate complexes prior to reaction initiation

substrate: NADPH


organism: Przewalskia tangutica


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


substrate_name: Tropinone; H+; NADPH

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

assay_conditions_summary: cofactor NADP+

substrate: Tropinone; H+; NADPH


organism: Hyoscyamus niger


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: Unknown

km_display: Not reported

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

substrate: Unknown


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

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

assay_conditions_summary: pH 9.3; cofactor CoA

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.


enzyme_display_name: cyclohexanol dehydrogenase

organism: Pseudomonas sp.

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

enzyme: cyclohexanol dehydrogenase


substrate_name: Cyclohexanol

substrate: Cyclohexanol


organism: Nocardia sp.

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


enzyme_display_name: methanol dehydrogenase

organism: Lysinibacillus xylanilyticus

substrate_name: n-Propanol

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

smiles: CCCO

enzyme: methanol dehydrogenase

substrate: n-Propanol


enzyme_display_name: tetrahydroxynaphthalene reductase

organism: Pyricularia oryzae

enzyme: tetrahydroxynaphthalene reductase


substrate_name: Scytalone

substrate: Scytalone


organism: Bacillus methanolicus

substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: salutaridine reductase (NADPH)

organism: Papaver somniferum

substrate_name: salutaridine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M271A to reconstruct the assayed variant sequence.

enzyme: salutaridine reductase (NADPH)

substrate: salutaridine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L185A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N272A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature T182A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 303.15 K; cofactor NADPH

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'T182A'; column 'Km (uM)' = 4.1; column 'Kim (uM)' = 58 uM; column 'Vmax/opt (nkat mg^-1)' = 3.43; column 'kcat (s^-1)' = 0.126; column 'kcat/Km (s^-1 mM^-1)' = 32.4; column 'Km NADPH (uM)' = 21.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 4.1 uM; 1 uM is 0.001 mM, so 4.1 / 1000 = 0.0040999999999999995 mM; the exported value is 0.0041 mM. kcat: printed Table 1 cell 0.126 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.126 s^(-1); the exported value is 0.126 s^(-1). kcat/Km: printed Table 1 cell 32.4 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 32.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'T182A': Km = 4.1 uM; kcat = 0.126 s^-1; printed kcat/Km = 32.4 s^-1 mM^-1.

row_label: Table 1, version row 'T182A'

table_label: Table 1: Apparent kinetic parameters for SalR and its mutated versions (J. Biol. Chem. 2009, volume 284, number 39, pages 26758-26767)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature L266A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'L266A'; column 'Km (uM)' = 49.4; column 'Kim (uM)' = ND; column 'Vmax/opt (nkat mg^-1)' = 13.68; column 'kcat (s^-1)' = 0.501; column 'kcat/Km (s^-1 mM^-1)' = 10.2; column 'Km NADPH (uM)' = 15.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 49.4 uM; 1 uM is 0.001 mM, so 49.4 / 1000 = 0.0494 mM; the exported value is 0.0494 mM. kcat: printed Table 1 cell 0.501 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.501 s^(-1); the exported value is 0.501 s^(-1). kcat/Km: printed Table 1 cell 10.2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 10.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'L266A': Km = 49.4 uM; kcat = 0.501 s^-1; printed kcat/Km = 10.2 s^-1 mM^-1.

row_label: Table 1, version row 'L266A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature D107A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'D107A'; column 'Km (uM)' = 14.8; column 'Kim (uM)' = 436 uM; column 'Vmax/opt (nkat mg^-1)' = 16.61; column 'kcat (s^-1)' = 0.610; column 'kcat/Km (s^-1 mM^-1)' = 41.7; column 'Km NADPH (uM)' = 30.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 14.8 uM; 1 uM is 0.001 mM, so 14.8 / 1000 = 0.0148 mM; the exported value is 0.0148 mM. kcat: printed Table 1 cell 0.610 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.61 s^(-1); the exported value is 0.61 s^(-1). kcat/Km: printed Table 1 cell 41.7 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 41.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'D107A': Km = 14.8 uM; kcat = 0.610 s^-1; printed kcat/Km = 41.7 s^-1 mM^-1.

row_label: Table 1, version row 'D107A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature K186V to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'K186V'; column 'Km (uM)' = 7.8; column 'Kim (uM)' = 18 uM; column 'Vmax/opt (nkat mg^-1)' = 27.23; column 'kcat (s^-1)' = 0.998; column 'kcat/Km (s^-1 mM^-1)' = 149.3; column 'Km NADPH (uM)' = 3.4.

normalized_value_unit_evidence: Km: printed Table 1 cell 7.8 uM; 1 uM is 0.001 mM, so 7.8 / 1000 = 0.0078 mM; the exported value is 0.0078 mM. kcat: printed Table 1 cell 0.998 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.998 s^(-1); the exported value is 0.998 s^(-1). kcat/Km: printed Table 1 cell 149.3 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 149.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'K186V': Km = 7.8 uM; kcat = 0.998 s^-1; printed kcat/Km = 149.3 s^-1 mM^-1.

row_label: Table 1, version row 'K186V'


column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'SalR-WT'; column 'Km (uM)' = 2.1; column 'Kim (uM)' = 184 uM; column 'Vmax/opt (nkat mg^-1)' = 35.61; column 'kcat (s^-1)' = 1.306; column 'kcat/Km (s^-1 mM^-1)' = 661.7; column 'Km NADPH (uM)' = 3.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.1 uM; 1 uM is 0.001 mM, so 2.1 / 1000 = 0.0021000000000000003 mM; the exported value is 0.0021 mM. kcat: printed Table 1 cell 1.306 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 1.306 s^(-1); the exported value is 1.306 s^(-1). kcat/Km: printed Table 1 cell 661.7 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 661.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'SalR-WT': Km = 2.1 uM; kcat = 1.306 s^-1; printed kcat/Km = 661.7 s^-1 mM^-1.

row_label: Table 1, version row 'SalR-WT'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature S181A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'S181A'; column 'Km (uM)' = 5.0; column 'Kim (uM)' = 199 uM; column 'Vmax/opt (nkat mg^-1)' = 52.75; column 'kcat (s^-1)' = 1.933; column 'kcat/Km (s^-1 mM^-1)' = 430.3; column 'Km NADPH (uM)' = 4.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.0 uM; 1 uM is 0.001 mM, so 5.0 / 1000 = 0.005 mM; the exported value is 0.005 mM. kcat: printed Table 1 cell 1.933 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 1.933 s^(-1); the exported value is 1.933 s^(-1). kcat/Km: printed Table 1 cell 430.3 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 430.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'S181A': Km = 5.0 uM; kcat = 1.933 s^-1; printed kcat/Km = 430.3 s^-1 mM^-1.

row_label: Table 1, version row 'S181A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature F104A/I275A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'F104A/I275A'; column 'Km (uM)' = 408.6; column 'Kim (uM)' = ND; column 'Vmax/opt (nkat mg^-1)' = 66.85; column 'kcat (s^-1)' = 2.450; column 'kcat/Km (s^-1 mM^-1)' = 5.9; column 'Km NADPH (uM)' = 43.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 408.6 uM; 1 uM is 0.001 mM, so 408.6 / 1000 = 0.4086 mM; the exported value is 0.4086 mM. kcat: printed Table 1 cell 2.450 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 2.45 s^(-1); the exported value is 2.45 s^(-1). kcat/Km: printed Table 1 cell 5.9 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 5.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'F104A/I275A': Km = 408.6 uM; kcat = 2.450 s^-1; printed kcat/Km = 5.9 s^-1 mM^-1.

row_label: Table 1, version row 'F104A/I275A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature V106A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'V106A'; column 'Km (uM)' = 8.9; column 'Kim (uM)' = 283 uM; column 'Vmax/opt (nkat mg^-1)' = 67.13; column 'kcat (s^-1)' = 2.458; column 'kcat/Km (s^-1 mM^-1)' = 295.4; column 'Km NADPH (uM)' = 7.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 8.9 uM; 1 uM is 0.001 mM, so 8.9 / 1000 = 0.0089 mM; the exported value is 0.0089 mM. kcat: printed Table 1 cell 2.458 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 2.458 s^(-1); the exported value is 2.458 s^(-1). kcat/Km: printed Table 1 cell 295.4 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 295.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'V106A': Km = 8.9 uM; kcat = 2.458 s^-1; printed kcat/Km = 295.4 s^-1 mM^-1.

row_label: Table 1, version row 'V106A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature F104A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'F104A'; column 'Km (uM)' = 31.8; column 'Kim (uM)' = 466 uM; column 'Vmax/opt (nkat mg^-1)' = 74.38; column 'kcat (s^-1)' = 2.727; column 'kcat/Km (s^-1 mM^-1)' = 86.2; column 'Km NADPH (uM)' = 9.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 31.8 uM; 1 uM is 0.001 mM, so 31.8 / 1000 = 0.0318 mM; the exported value is 0.0318 mM. kcat: printed Table 1 cell 2.727 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 2.727 s^(-1); the exported value is 2.727 s^(-1). kcat/Km: printed Table 1 cell 86.2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 86.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'F104A': Km = 31.8 uM; kcat = 2.727 s^-1; printed kcat/Km = 86.2 s^-1 mM^-1.

row_label: Table 1, version row 'F104A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature I275A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'I275A'; column 'Km (uM)' = 33.1; column 'Kim (uM)' = 1249 uM; column 'Vmax/opt (nkat mg^-1)' = 87.03; column 'kcat (s^-1)' = 3.188; column 'kcat/Km (s^-1 mM^-1)' = 98.0; column 'Km NADPH (uM)' = 21.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 33.1 uM; 1 uM is 0.001 mM, so 33.1 / 1000 = 0.033100000000000004 mM; the exported value is 0.0331 mM. kcat: printed Table 1 cell 3.188 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 3.188 s^(-1); the exported value is 3.188 s^(-1). kcat/Km: printed Table 1 cell 98.0 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 98.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'I275A': Km = 33.1 uM; kcat = 3.188 s^-1; printed kcat/Km = 98.0 s^-1 mM^-1.

row_label: Table 1, version row 'I275A'


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K186V 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.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S181A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V106A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F104A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L266A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M271A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I275A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T182A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L185A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D107A to reconstruct the assayed variant sequence.


substrate_name: methanol

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

smiles: CO

substrate: methanol


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

assay_conditions_summary: pH 9.5; 328.15 K; cofactor NAD+


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: butanol

smiles: CCCCO

substrate: butanol


organism: Pyricularia grisea


substrate_name: Phenanthrenequinone

substrate: Phenanthrenequinone


substrate_name: NADP+

proof_lines: with 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one as cosubstrate

substrate: NADP+


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: D-arabinitol 2-dehydrogenase

organism: Thermotoga maritima

substrate_name: D-arabitol

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

proof_lines:
85°C, pH 8.5, Strep-tagged enzyme
85°C, pH 8.5, tag-less enzyme

enzyme: D-arabinitol 2-dehydrogenase

substrate: D-arabitol


substrate_name: D-ribulose

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

proof_lines:
85°C, pH 7.5, Strep-tagged enzyme
85°C, pH 7.5, tag-less enzyme

substrate: D-ribulose


substrate_name: NADH

assay_conditions_summary: pH 7.5; 358.15 K; cofactor NADH

proof_lines: 85°C, pH 7.5, Strep-tagged enzyme, cosubstrate D-ribulose

proof_lines: 85°C, pH 7.5, tag-less enzyme, cosubstrate D-ribulose

substrate: NADH


assay_conditions_summary: pH 8.5; 358.15 K; cofactor NAD+

proof_lines: 85°C, pH 8.5, tag-less enzyme, cosubstrate D-arabitol

proof_lines: 85°C, pH 8.5, Strep-tagged enzyme, cosubstrate D-arabitol


enzyme_display_name: (S)-carnitine 3-dehydrogenase

organism: Agrobacterium sp.

assay_conditions_summary: cofactor NADH

enzyme: (S)-carnitine 3-dehydrogenase


substrate_name: (S)-carnitine

substrate: (S)-carnitine


organism: Xanthobacter sp.


organism: Agrobacterium sp. 525a


substrate_name: D-carnitine

substrate: D-carnitine


substrate_name: NAD+; Ethanol

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

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

substrate: NAD+; Ethanol


enzyme_display_name: codeinone reductase (NADPH)

substrate_name: codeine

enzyme: codeinone reductase (NADPH)

substrate: codeine


substrate_name: codeinone

substrate: codeinone


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+


substrate_name: NADPH

assay_conditions_summary: pH 6.8; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: NADPH-dependent codeinone reductase 1-3

substrate_name: codeine (at pH 9.0 and 30 degrees Celsius)

assay_conditions_summary: pH 9; cofactor NADPH

proof_lines: kcat is 0.040 sec(-1) with codeinone as substrate (PubMed:29779229). kcat is 0.015 sec(-1) with codeine as substrate (PubMed:29779229). kcat is 0.060 sec(-1) with NADPH as substrate (PubMed:29779229). kcat is 0.044 sec(-1) with NADP(+) as s

enzyme: NADPH-dependent codeinone reductase 1-3


substrate_name: codeinone (at pH 9.0 and 30 degrees Celsius)


substrate_name: NADPH (at pH 9.0 and 30 degrees Celsius)


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

substrate: NADP (at pH 9.0 and 30 degrees Celsius)


substrate_name: morphine (at pH 9.0 and 30 degrees Celsius)


substrate_name: dihydrocodeine (at pH 9.0 and 30 degrees Celsius)


substrate_name: morphinone (at pH 9.0 and 30 degrees Celsius)


substrate_name: hydrocodone (at pH 9.0 and 30 degrees Celsius)


substrate_name: hydromorphone (at pH 9.0 and 30 degrees Celsius)


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: Cyclohexanol

source_databases_merged: brenda uniprot

substrate: Cyclohexanol


smiles: CCCCC(CO)O


substrate_name: Cyclopentanol

substrate: Cyclopentanol


organism: Papaver bracteatum

column_label: Table I: Kinetic parameters of SalR of P. bracteatum for the forward and reverse reaction and the cofactors (Plant Physiology, April 2007, Vol. 143, pp. 1493-1503); printed column heads Substrates: K_m (uM) | K_i (uM) | V_max (nkat mg^-1) | V_opt (nkat mg^-1) | K_cat (s^-1) | K_cat K_m^-1 (s^-1 M^-1 10^3); Cofactors: K_m (uM) | V_max (nkat mg^-1) | K_cat (s^-1) | K_cat K_m^-1 (s^-1 M^-1 10^3). Cofactors block, cofactor row NADPH read across the Salutaridine line; column K_m (uM) = 3.5; column V_max (nkat mg^-1) = 57.5; column K_cat (s^-1) = 2.1; column K_cat K_m^-1 (s^-1 M^-1 10^3) = 600. captured primary segment: Cofactor row NADPH for the salutaridine reduction | Km 3.5 uM | Vmax 57.5 nkat mg^-1 | kcat 2.1 s^-1 | kcat/Km 600 x 10^3 s^-1 M^-1

normalized_value_unit_evidence: Km: printed Table I Cofactors cell 3.5 uM; 1 uM is 1/1000 mM, so 3.5 / 1000 = 0.0035 mM, which is the exported value. kcat: printed Table I Cofactors cell 2.1 s^-1; the printed unit is already s^-1, so no unit conversion applies, giving 2.1 s^(-1), which is the exported value. kcat/Km: the printed cell is 600 in a column headed s^-1 M^-1 10^3, that is 600 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 600 x 10^3 / 1000 = 600.0 s^(-1)*mM^(-1), which is the exported value. Quotient disclosure for this row: 2.1 / 0.0035 = 600.0 s^-1 mM^-1, the same number as the printed efficiency cell.

raw_value_unit_evidence: Table I, Cofactors block, cofactor row NADPH read across the Salutaridine line: K_m = 3.5 uM; V_max = 57.5 nkat mg^-1; K_cat = 2.1 s^-1; printed K_cat K_m^-1 = 600 in a column headed s^-1 M^-1 10^3. Table II prints the same wild-type NADPH cofactor tuple: K_m 3.5 uM, K_cat 2.1 s^-1 and K_cat K_m^-1 600.

row_label: Table I, Cofactors block, cofactor row NADPH for the salutaridine reduction


substrate_name: salutaridine

column_label: Table I: Kinetic parameters of SalR of P. bracteatum for the forward and reverse reaction and the cofactors (Plant Physiology, April 2007, Vol. 143, pp. 1493-1503); printed column heads Substrates: K_m (uM) | K_i (uM) | V_max (nkat mg^-1) | V_opt (nkat mg^-1) | K_cat (s^-1) | K_cat K_m^-1 (s^-1 M^-1 10^3); Cofactors: K_m (uM) | V_max (nkat mg^-1) | K_cat (s^-1) | K_cat K_m^-1 (s^-1 M^-1 10^3). Substrates block, substrate row Salutaridine; column K_m (uM) = 7.9; column K_i (uM) = 140; column V_max (nkat mg^-1) = 93.8; column V_opt (nkat mg^-1) = 63.2; column K_cat (s^-1) = 2.3; column K_cat K_m^-1 (s^-1 M^-1 10^3) = 291. captured primary segment: Substrate row Salutaridine, reduction direction with NADPH as cofactor | Km 7.9 uM | Ki 140 uM | Vmax 93.8 nkat mg^-1 | Vopt 63.2 nkat mg^-1 | kcat 2.3 s^-1 | kcat/Km 291 x 10^3 s^-1 M^-1

normalized_value_unit_evidence: Km: printed Table I Substrates cell 7.9 uM; 1 uM is 1/1000 mM, so 7.9 / 1000 = 0.0079 mM. kcat: printed Table I Substrates cell 2.3 s^-1; the printed unit is already s^-1, so no unit conversion applies, giving 2.3 s^(-1), which is the exported value. kcat/Km: the printed cell is 291 in a column headed s^-1 M^-1 10^3, that is 291 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 291 x 10^3 / 1000 = 291.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.3 / 0.0079 = 291.13924050632916 s^-1 mM^-1, which the paper writes as its printed efficiency cell 291.

raw_value_unit_evidence: Table I, Substrates block, substrate row Salutaridine: K_m = 7.9 uM; K_i = 140 uM; V_max = 93.8 nkat mg^-1; V_opt = 63.2 nkat mg^-1; K_cat = 2.3 s^-1; printed K_cat K_m^-1 = 291 in a column headed s^-1 M^-1 10^3. Table III prints the same wild-type salutaridine tuple: K_m 7.9 uM, K_i 140 uM, V_opt 63.2 nkat mg^-1, K_cat 2.3 s^-1 and K_cat K_m^-1 291. The Results text states the same two constants in prose, printed there with the same micro-sign glyph substitution as the tables: Extraction of the kinetic parameters yielded Km and Ki values for salutaridine of 7.9 and 140, respectively.

row_label: Table I, Substrates block, substrate row Salutaridine (reduction direction, NADPH as cofactor)

substrate: salutaridine


substrate_name: NADH

column_label: Table II: Kinetic parameters with respect to the cofactors of mutated variants of SalR designed for the investigations on cofactor preference (Plant Physiology, April 2007, Vol. 143, pp. 1493-1503); printed column heads Variant | Cofactor | K_m (uM) | V_max (nkat mg^-1) | K_cat (s^-1) | K_cat K_m^-1 (s^-1 M^-1 10^3). Wild type block, cofactor row NADH; column K_m (uM) = 1,190; column V_max (nkat mg^-1) = 102; column K_cat (s^-1) = 3.7; column K_cat K_m^-1 (s^-1 M^-1 10^3) = 3.1. captured primary segment: Wild type | Cofactor row NADH | Km 1,190 uM | Vmax 102 nkat mg^-1 | kcat 3.7 s^-1 | kcat/Km 3.1 x 10^3 s^-1 M^-1

normalized_value_unit_evidence: Km: printed Table II cell 1,190 uM; 1 uM is 1/1000 mM, so 1,190 / 1000 = 1.19 mM, which is the exported value. kcat: printed Table II cell 3.7 s^-1; the printed unit is already s^-1, so no unit conversion applies, giving 3.7 s^(-1), which is the exported value. kcat/Km: the printed cell is 3.1 in a column headed s^-1 M^-1 10^3, that is 3.1 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.1 x 10^3 / 1000 = 3.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.7 / 1.19 = 3.109243697478992 s^-1 mM^-1, which is the exported efficiency, and the table prints that same quotient to the two significant figures its efficiency column uses.

raw_value_unit_evidence: Table II, Wild type block, cofactor row NADH: K_m = 1,190 uM; V_max = 102 nkat mg^-1; K_cat = 3.7 s^-1; printed K_cat K_m^-1 = 3.1 in a column headed s^-1 M^-1 10^3.


assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: The enzyme does not obey Michaelis-Menten kinetics because the theorectical Vmax cannot be achieved due to strong substrate inhibition, instead the optimal velocity, Vopt, is taken as the measure of enzyme performance.


substrate_name: NADP+

assay_conditions_summary: pH 6; cofactor NADP+

proof_lines: pH 6.0, 40°C, recombinant enzyme, with salutaridinol


enzyme_display_name: Salutaridine reductase

substrate_name: NADP(+)

assay_conditions_summary: cofactor NADPH

enzyme: Salutaridine reductase

substrate: NADP(+)


organism: Cupriavidus necator

substrate_name: methanol

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

source_databases_merged: brenda oed

substrate: methanol


proof_lines: pH 9.5, 30°C, recombinant mutant A26V/A31V/A169V


proof_lines: pH 9.5, 30°C, recombinant mutant A26V/A169V


substrate_name: n-butanol

substrate: n-butanol


enzyme_display_name: NADPH-dependent codeinone reductase 1-5

substrate_name: codeinone

proof_lines: kcat is 0.023 sec(-1) with codeinone as substrate (PubMed:29779229). kcat is 0.027 sec(-1) with codeine as substrate (PubMed:29779229). kcat is 0.045 sec(-1) with NADPH as substrate (PubMed:29779229). kcat is 0.067 sec(-1) with NADP(+) as s

enzyme: NADPH-dependent codeinone reductase 1-5


substrate_name: codeine


substrate_name: NADPH


substrate_name: formaldehyde

substrate: formaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F104A/I275A to reconstruct the assayed variant sequence.


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S97T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.5; cofactor NAD+

proof_lines: S97T mutant enzyme without added Mg2+, pH 9.5, 50°C

substrate: NAD+


sequence_variant_note: Mutation signature S97G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: S97G mutant enzyme without added Mg2+, pH 9.5, 50°C


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

assay_conditions_summary: pH 6

proof_lines: pH 6.0, 30°C, recombinant enzyme, reduction reaction


assay_conditions_summary: pH 9.5; cofactor NADP+

proof_lines: pH 9.5, 30°C, recombinant enzyme, oxidation reaction

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A164P/A363L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A363L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A164P to reconstruct the assayed variant sequence.


enzyme_display_name: NADPH-dependent codeinone reductase 1-1

substrate_name: NADPH (at pH 9.0 and 30 degrees Celsius)

column_label: Table 3 row 'Km NADPH (uM)', COR1.1 column = 180 uM.

raw_value_unit_evidence: Km raw_value=180 raw_unit=uM

row_label: COR1.1; Km NADPH

enzyme: NADPH-dependent codeinone reductase 1-1


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

assay_conditions_summary: pH 9

column_label: Table 3 row 'Km NADP (uM)', COR1.1 column = 53 uM.

raw_value_unit_evidence: Km raw_value=53 raw_unit=uM

row_label: COR1.1; Km NADP


enzyme_display_name: NADPH-dependent codeinone reductase 1-2

substrate_name: codeine (at pH 9.0 and 30 degrees Celsius)

proof_lines: NADPH-dependent reduction of codeinone to codeine

enzyme: NADPH-dependent codeinone reductase 1-2


substrate_name: codeinone (at pH 9.0 and 30 degrees Celsius)


substrate: NADPH (at pH 9.0 and 30 degrees Celsius)


enzyme_display_name: NADPH-dependent codeinone reductase 1-4

enzyme: NADPH-dependent codeinone reductase 1-4

substrate: codeine (at pH 9.0 and 30 degrees Celsius)


substrate: codeinone (at pH 9.0 and 30 degrees Celsius)


organism: Candida tropicalis

assay_conditions_summary: cofactor NAD+

column_label: Abstract states the apparent Km for NAD+ at DA concentration 384 mM is 0.12 mM.

raw_value_unit_evidence: Km raw_value=0.12 raw_unit=mM

row_label: Candida tropicalis D-arabinitol dehydrogenase with NAD+

table_label: PubMed abstract PMID 8250887


substrate_name: D-arabinitol

substrate: D-arabinitol


enzyme_display_name: NAD-dependent methanol dehydrogenase

proof_lines:
Bacillus methanolicus
methanol dehydrogenase
NAD-dependent methanol dehydrogenase

enzyme: NAD-dependent methanol dehydrogenase

substrate: NADH


substrate_name: D-xylitol

substrate: D-xylitol


substrate_name: D-Ribulose

substrate: D-Ribulose


substrate_name: D-Arabitol

substrate: D-Arabitol


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


substrate_name: NAD

column_label: Table IV lists bMDH row with Km NAD+ = 0.02 mM.

raw_value_unit_evidence: Km raw_value=0.02 mM raw_unit=mM

row_label: bMDH row

table_label: JBC full text Table IV: Kinetic characteristics and metal composition of bMDH and cMDH

substrate: NAD


enzyme_display_name: NADH-dependent L-xylulose reductase

organism: Ambrosiozyma monospora

substrate_name: L-xylulose

enzyme: NADH-dependent L-xylulose reductase

substrate: L-xylulose


proof_lines:
D-ribulose
D-arabinitol
L-xylulose reductase


substrate_name: formaldehyde (without activator protein at pH 9.5 and 50 degrees Celsius)


substrate_name: ethanol (with the activator protein at pH 9.5 and 50 degrees Celsius)


substrate_name: methanol (with the activator protein at pH 9.5 and 50 degrees Celsius)


substrate_name: salutaridinol

column_label: Table 2 reports salutaridinol substrate Km as 23.0 +/- 6.9 microM, not the CatLog value 0.018 mM.

raw_value_unit_evidence: Km raw_value=23.0 +/- 6.9 microM raw_unit=microM

row_label: Salutaridine reductase / salutaridinol reverse-reaction substrate row

table_label: Wiley/The Plant Journal full text Table 2

substrate: salutaridinol


organism: Curvularia lunata

assay_conditions_summary: pH 7


organism: Escherichia coli (strain K12)

substrate_name: 4-(phosphooxy)-L-threonine (at 0.1 M Tris-HCl and pH 7.5)


enzyme_display_name: UniProt P9WNS1

organism: Mycobacterium tuberculosis

substrate_name: 1-deoxy-D-xylulose 5-phosphate

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt P9WNS1

substrate: 1-deoxy-D-xylulose 5-phosphate

source: skid


enzyme_display_name: UniProt P45568

organism: Escherichia coli

enzyme: UniProt P45568


substrate_name: NADPH

substrate: NADPH


substrate_name: Methanol; NAD+

substrate: Methanol; NAD+


substrate_name: Unknown

substrate: Unknown


substrate_name: DNA with apurinic site

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NADPH

substrate: DNA with apurinic site


substrate_name: salutaridine (Termination and extraction with NaHCO(3) and ethylacetate, respectively)


ki_unit: mM

proof_lines: at 0.04 mM 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one, at pH 7.0 and 25°C


enzyme_display_name: L-idonate 5-dehydrogenase

organism: Gluconobacter oxydans

enzyme: L-idonate 5-dehydrogenase


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: D-gluconate

substrate: D-gluconate


organism: Fusarium sp.


organism: synthetic construct


organism: Aspergillus niger

substrate_name: L-Idonate

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

assay_conditions_summary: pH 8

proof_lines: pH 8, temperature not specified in the publication

proof_lines: pH 7, temperature not specified in the publication

substrate: L-Idonate


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

organism: Ensifer adhaerens

proof_lines: mutant G206I in the presence of 1,5-anhydro-D-fructose

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


proof_lines: mutant K94G in the presence of 1,5-anhydro-D-fructose


proof_lines: mutant S10G in the presence of 1,5-anhydro-D-fructose


proof_lines: mutant A13G/S10G in the presence of 1,5-anhydro-D-fructose


proof_lines: mutant A13G/S33D in the presence of 1,5-anhydro-D-fructose


substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: mutant A13G in the presence of 1,5-anhydro-D-fructose


substrate_name: D-glucosone

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

substrate: D-glucosone


enzyme_display_name: 3-methylbutanal reductase

organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y128A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

smiles: CC(C)CC=O

enzyme: 3-methylbutanal reductase


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature F85A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y198A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y198F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y128F with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature V162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature F132A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


enzyme_display_name: sn-glycerol-1-phosphate dehydrogenase

organism: Pyrobaculum calidifontis

assay_conditions_summary: pH 7; cofactor NADPH

enzyme: sn-glycerol-1-phosphate dehydrogenase


substrate_name: dihydroxyacetone phosphate

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

proof_lines: wild-type, cosubstrate NADPH, pH 7.0, 50°C

proof_lines: wild-type, cosubstrate NADH, pH 7.0, 50°C

substrate: dihydroxyacetone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S40A/T42A to reconstruct the assayed variant sequence.

proof_lines: mutant S40A/T42A, cosubstrate NADPH, pH 7.0, 50°C

proof_lines: mutant S40A/T42A, cosubstrate NADH, pH 7.0, 50°C


assay_conditions_summary: pH 7; cofactor NADH

substrate: NADH


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


proof_lines: mutant A13G/S10G in the presence of NADH

proof_lines: mutant A13G/S10Gin the presence of NADPH


proof_lines: mutant A13G/S33D in the presence of NADPH

proof_lines: mutant A13G/S33D in the presence of NADH


proof_lines:
mutant A13G in the presence of NADH
mutant A13G in the presence of NADPH


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

proof_lines: recombinant wild type enzyme in the presence of NADPH

proof_lines: native wild type enzyme in the presence of NADPH


proof_lines: recombinant wild type enzyme in the presence of 1,5-anhydro-D-fructose

proof_lines: native wild type enzyme in the presence of 1,5-anhydro-D-fructose


organism: Synechocystis sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W204A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature W204L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature W204V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, so it is treated as a source-provided variant sequence.


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

proof_lines: pH 7.8, 37°C, recombinant wild-type enzyme


enzyme_display_name: dTDP-4-dehydro-6-deoxyglucose reductase

organism: Aggregatibacter actinomycetemcomitans

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

enzyme: dTDP-4-dehydro-6-deoxyglucose reductase


organism: Vitis vinifera


enzyme_display_name: NADPH-dependent methylglyoxal reductase GRE2

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 31.3 min(-1) with 3-chloro-1-phenyl-1-propanol as substrate and 29.1 min(-1) for NADPH.


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

enzyme: NADPH-dependent methylglyoxal reductase GRE2


smiles: CC(CCC(C)O)O


proof_lines: kcat is 406 min(-1) for the reduction reaction with NADPH, and 1594 min(-1) for that with NADH.


organism: Methanocaldococcus jannaschii

proof_lines: with NADH as cosubstrate, at pH 7.8 and 65°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines:
pH 7.5, 37°C, presence of 1 mM Co2+
pH 7.5, 37°C, presence of 1 mM Mn2+
pH 7.5, 37°C, presence of 1 mM Mg2+


proof_lines:
pH 7.5, 37°C, presence of 1 mM Co2+
pH 7.5, 37°C, presence of 1 mM Mg2+
pH 7.5, 37°C, presence of 1 mM Mn2+


organism: Plectranthus barbatus

assay_conditions_summary: pH 8; cofactor NADPH


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: phenylglyoxal

substrate: phenylglyoxal


organism: Mus musculus


substrate_name: Hexanol

smiles: CCCCCCO

proof_lines:
in the presence of NADP+
presence of NADP+

substrate: Hexanol


substrate_name: acetaldehyde

smiles: CC=O

proof_lines:
in the presence of NADPH
pH 7.0, 30°C
presence of NADPH

substrate: acetaldehyde


smiles: CCCC=CCO


substrate_name: Butanal

smiles: CCCC=O

proof_lines:
presence of NADH
presence of NADPH

substrate: Butanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: propanal

smiles: CCC=O

proof_lines:
presence of NADPH
presence of NADH

substrate: propanal


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


substrate_name: Heptanal

smiles: CCCCCCC=O

substrate: Heptanal


smiles: CCC(C)C=O


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

substrate_name: DHAP (in the presence of NADH as coenzyme)


substrate_name: NADPH

substrate: NADPH


substrate_name: G1P (in the presence of NAD as coenzyme)


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


organism: Aeropyrum pernix

substrate_name: glycerone phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature D144A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 8; 338.15 K; buffer 50 mM Tris-HCl; cofactor NADH

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'D144A': the line 'k cat (min -1)' cell reads 1126.5 ± 158.6 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 1.12 ± 0.34. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1126.5 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 1126.5 / 60 = 18.775 and the paper value is 18.775 s^(-1). Km: printed Table 1 cell 1.12 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 1.12 mM. kcat/Km: Table 1 carries no kcat/Km line, so 16.763392857142854 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 18.775 / 1.12 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'D144A': the 'k cat (min -1)' cell reads 1126.5 ± 158.6 and the 'Kb (mM)' cell, the Km for DHAP, reads 1.12 ± 0.34. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'D144A'

substrate: glycerone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature D144N with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'D144N': the line 'k cat (min -1)' cell reads 3628.2 ± 380.5 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 1.12 ± 0.20. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3628.2 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 3628.2 / 60 = 60.47 and the paper value is 60.47 s^(-1). Km: printed Table 1 cell 1.12 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 1.12 mM. kcat/Km: Table 1 carries no kcat/Km line, so 53.99107142857142 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 60.47 / 1.12 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'D144N': the 'k cat (min -1)' cell reads 3628.2 ± 380.5 and the 'Kb (mM)' cell, the Km for DHAP, reads 1.12 ± 0.20. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'D144N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature D191N with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'D191N': the line 'k cat (min -1)' cell reads 196.2 ± 38.4 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 0.633 ± 0.32. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 196.2 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 196.2 / 60 = 3.27 and the paper value is 3.27 s^(-1). Km: printed Table 1 cell 0.633 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 0.633 mM. kcat/Km: Table 1 carries no kcat/Km line, so 5.165876777251185 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 3.27 / 0.633 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'D191N': the 'k cat (min -1)' cell reads 196.2 ± 38.4 and the 'Kb (mM)' cell, the Km for DHAP, reads 0.633 ± 0.32. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'D191N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature H271A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'H271A': the line 'k cat (min -1)' cell reads 29.58 ± 16.6 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 1.09 ± 0.13. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 29.58 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 29.58 / 60 = 0.493 and the paper value is 0.493 s^(-1). Km: printed Table 1 cell 1.09 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 1.09 mM. kcat/Km: Table 1 carries no kcat/Km line, so 0.4522935779816513 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.493 / 1.09 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'H271A': the 'k cat (min -1)' cell reads 29.58 ± 16.6 and the 'Kb (mM)' cell, the Km for DHAP, reads 1.09 ± 0.13. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'H271A'


substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature H287A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'H287A': the line 'k cat (min -1)' cell reads 176.7 ± 4.99 and the line 'Ka (mM)' cell, which the table caption defines as the Km for the coenzyme NADH, reads 0.036 ± 0.004. The same column also prints a 'Kb (mM)' cell, the Km for DHAP, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 176.7 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 176.7 / 60 = 2.945 and the paper value is 2.945 s^(-1). Km: printed Table 1 cell 0.036 in the 'Ka (mM)' line, the Km for the coenzyme NADH; the unit is already mM, so no unit conversion applies and the paper value is 0.036 mM. kcat/Km: Table 1 carries no kcat/Km line, so 81.80555555555556 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.945 / 0.036 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'H287A': the 'k cat (min -1)' cell reads 176.7 ± 4.99 and the 'Ka (mM)' cell, the Km for the coenzyme NADH, reads 0.036 ± 0.004. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'H287A'


assay_conditions_summary: pH 8; 338.15 K; buffer 50 mM Tris-HCl; cofactor NADPH

column_label: Table 2: Kinetic parameters for the wild-type and mutant sn-glycerol-1-phosphate dehydrogenases (Gro1PDH) in dihydroxyacetone phosphate (DHAP) reduction with NADPH as the coenzyme (Archaea 2005), column 'D144N': the line 'k cat (min -1)' cell reads 284.1 ± 50.8 and the line 'Ka (mM)' cell, which the table caption defines as the Km for the coenzyme NADPH, reads 0.165 ± 0.06. The same column also prints a 'Kb (mM)' cell, the Km for DHAP, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 2 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 284.1 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 284.1 / 60 = 4.735 and the paper value is 4.735 s^(-1). Km: printed Table 2 cell 0.165 in the 'Ka (mM)' line, the Km for the coenzyme NADPH; the unit is already mM, so no unit conversion applies and the paper value is 0.165 mM. kcat/Km: Table 2 carries no kcat/Km line, so 28.6969696969697 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.735 / 0.165 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, column 'D144N': the 'k cat (min -1)' cell reads 284.1 ± 50.8 and the 'Ka (mM)' cell, the Km for the coenzyme NADPH, reads 0.165 ± 0.06. Table 2 carries no kcat/Km line.

row_label: Table 2, column 'D144N'


enzyme_display_name: UniProt Q2VEQ7

organism: Haloferax mediterranei

enzyme: UniProt Q2VEQ7


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


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


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


substrate_name: pyruvate

substrate: pyruvate


substrate_name: dihydroxyacetone phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S40A/T42A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 323.15 K; cofactor NADPH


column_label: Table 2; NADPH row; columns Km, kcat, kcat/Km.

row_label: NADPH row

table_label: Carbone et al. 2015, J Biol Chem, Structure and Evolution of the Archaeal Lipid Synthesis Enzyme sn-Glycerol-1-phosphate Dehydrogenase; kinetic table evidence


column_label: Table 2; NADH row; columns Km, kcat, kcat/Km.

row_label: NADH row


column_label: Table 2; DHAP (NADPH) row; columns Km, kcat, kcat/Km.

row_label: DHAP (NADPH) row


assay_conditions_summary: pH 7; 323.15 K; cofactor NADH


substrate_name: glycolaldehyde

smiles: C(C=O)O

proof_lines: three aliphatic aldehydes (acetaldehyde, glycolaldehyde, and 3-methylbutanal)

substrate: glycolaldehyde


substrate_name: furfural

proof_lines: two furan aldehydes (furfural and 5-hydroxymethylfurfural)

substrate: furfural


substrate_name: acetaldehyde

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: when acetaldehyde was used as the substrate


smiles: O=CCO


substrate_name: NAD+

assay_conditions_summary: pH 7; 338.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7; 338.15 K; cofactor NADPH

column_label: PMID 11846799 Table 2, Dihydroxyacetone phosphate reduction section, row NADH (4 mM dihydroxyacetone phosphate): Km 0.032 +/- 0.005 mM and kcat 143.96 +/- 6.81 min^-1. The same-row central-value ratio after minute-to-second conversion is 74.979166666666666666666666666666666666666666666666 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row NADH (4 mM dihydroxyacetone phosphate): Km 0.032 +/- 0.005 mM; kcat 143.96 +/- 6.81 min^-1.

row_label: NADH (4 mM dihydroxyacetone phosphate)

table_label: Table 2. Substrate specificity of Gro1P dehydrogenase from A. pernix

substrate: NADH


substrate_name: sn-Glycerol 1-phosphate

substrate: sn-Glycerol 1-phosphate


enzyme_display_name: vellosimine dehydrogenase

organism: Rauvolfia serpentina

substrate_name: vellosimine

enzyme: vellosimine dehydrogenase

substrate: vellosimine


assay_conditions_summary: cofactor NADPH


substrate_name: geissoschizal

substrate: geissoschizal


enzyme_display_name: 3beta-hydroxysteroid 3-dehydrogenase

organism: Eggerthella sp. CAG:298

substrate_name: 3-oxodeoxycholic acid

assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: coenzyme: NADPH, pH 6.5, temperature not specified in the publication

enzyme: 3beta-hydroxysteroid 3-dehydrogenase

substrate: 3-oxodeoxycholic acid


substrate_name: isodeoxycholic acid

assay_conditions_summary: pH 9.5; cofactor NADP+

proof_lines: coenzyme: NADP+, pH 9.5, temperature not specified in the publication

substrate: isodeoxycholic acid


enzyme_display_name: D-2-hydroxyacid dehydrogenase (NADP+)

substrate_name: NADPH

assay_conditions_summary: pH 8.5; 313.15 K; cofactor NADPH

proof_lines: pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisocaproate

proof_lines: pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisoleucine

proof_lines: pH 8.5, 40°C, recombinant enzyme, substrate 2-oxobutyrate

enzyme: D-2-hydroxyacid dehydrogenase (NADP+)


assay_conditions_summary: pH 8.5; 313.15 K; cofactor NADH


proof_lines: pH 8.5, 40°C, recombinant enzyme, cofactor NADPH

proof_lines: pH 8.5, 40°C, recombinant enzyme, cofactor NADH


assay_conditions_summary: pH 5; 313.15 K; cofactor NADPH

proof_lines: pH 5.0, 40°C, recombinant enzyme, cofactor NADPH


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: DHAP (in the presence of NADH as coenzyme)

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

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


column_label: Table 2; section Dihydroxyacetone phosphate reduction; row NADH (4 mM dihydroxyacetone phosphate); column Km (mM); cell 0.032 +/- 0.005.

normalized_value_unit_evidence: Km=0.032 mM for NADH.

raw_value_unit_evidence: Table 2 row NADH (4 mM dihydroxyacetone phosphate); Km (mM) cell = 0.032 +/- 0.005.

table_label: Table 2: Substrate specificity of Gro1P dehydrogenase from A. pernix


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 2; section Dihydroxyacetone phosphate reduction; row NADPH (4 mM dihydroxyacetone phosphate); column Km (mM); cell 0.044 +/- 0.022.

normalized_value_unit_evidence: Km=0.044 mM for NADPH.

raw_value_unit_evidence: Table 2 row NADPH (4 mM dihydroxyacetone phosphate); Km (mM) cell = 0.044 +/- 0.022.

row_label: NADPH (4 mM dihydroxyacetone phosphate)


assay_conditions_summary: pH 7

column_label: Table 2; section Gro1P oxidation; row Gro1P (5 mM NAD); column Km (mM); cell 8.92 +/- 0.64.

normalized_value_unit_evidence: Km=8.92 mM for G1P/Gro1P.

raw_value_unit_evidence: Table 2 row Gro1P (5 mM NAD); Km (mM) cell = 8.92 +/- 0.64.

row_label: Gro1P (5 mM NAD)


substrate_name: NAD(+)

assay_conditions_summary: pH 7; cofactor NAD+

column_label: Table 2; section Gro1P oxidation; row NAD (50 mM Gro1P); column Km (mM); cell 1.57 +/- 0.44.

normalized_value_unit_evidence: Km=1.57 mM for NAD(+).

raw_value_unit_evidence: Table 2 row NAD (50 mM Gro1P); Km (mM) cell = 1.57 +/- 0.44.

row_label: NAD (50 mM Gro1P)


enzyme_display_name: (R)-2-hydroxyacid dehydrogenase

organism: Enterococcus faecalis

substrate_name: H+; NADH; 2-Oxobutyrate

assay_conditions_summary: cofactor NADH

enzyme: (R)-2-hydroxyacid dehydrogenase

substrate: H+; NADH; 2-Oxobutyrate


organism: Zea mays

mutation_signature: Δ7

mutation_type: deletion


substrate_name: cycloartenone

substrate: cycloartenone


substrate_name: cyclolaudenone

substrate: cyclolaudenone


substrate_name: cycloeucalenone

substrate: cycloeucalenone


substrate_name: cholestanone

substrate: cholestanone


organism: Escherichia coli

substrate_name: 1-Deoxy-D-xylulose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E231K with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

substrate: 1-Deoxy-D-xylulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H153Q with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H209Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H257Q with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


enzyme_display_name: 4-methyl-2-oxopentanoate reductase A

organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40)

substrate_name: 4-methyl-2-oxopentanoate (MOA)

proof_lines: kcat is 15.0 sec(-1) with 4-methyl-2-oxopentanoate (MOA) as substrate. kcat is 140.0 sec(-1) with pyruvate as substrate. kcat is 10.0 sec(-1) with hydroxypyruvate as substrate. kcat is 11.0 sec(-1) with glyoxylate as substrate. kcat is 0.74

enzyme: 4-methyl-2-oxopentanoate reductase A

substrate: 4-methyl-2-oxopentanoate (MOA)


substrate_name: pyruvate

substrate: pyruvate


substrate_name: hydroxypyruvate

substrate: hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate: NADPH


substrate_name: NADH

substrate: NADH


enzyme_display_name: 2-hydroxyacid dehydrogenase A

proof_lines: kcat is 14.0 sec(-1) with pyruvate as substrate. kcat is 170.0 sec(-1) with hydroxypyruvate as substrate. kcat is 591.0 sec(-1) with glyoxylate as substrate.

enzyme: 2-hydroxyacid dehydrogenase A


organism: Corynebacterium sp.

sequence_variant_note: Mutation signature F22Y/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature F22Y/S233T/R235S/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/S233T/R235S/R238H/A272G isoenzyme A mutant


assay_conditions_summary: pH 7; cofactor NADH

column_label: Table 6: Full Kinetic Parameters with NADH as a Cofactor, row wild type, substrate/cofactor context NADH: kcat 170 min^-1; Ka 1.4 mM for NADH; normalized kcat 2.83333 s^-1; Km 1.4 mM; kcat/Km 2.02381 s^-1*mM^-1.

raw_value_unit_evidence: kcat 170 min^-1; Ka 1.4 mM for NADH

row_label: wild type


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232G/R238H to reconstruct the assayed variant sequence.

column_label: Table 8: Full Kinetic Parameters with NADPH as a Cofactor, row K232G/R238H, substrate/cofactor context NADPH: kcat 200 min^-1; Ka 0.13 mM for NADPH; normalized kcat 3.33333 s^-1; Km 0.13 mM; kcat/Km 25.641 s^-1*mM^-1.

raw_value_unit_evidence: kcat 200 min^-1; Ka 0.13 mM for NADPH


sequence_variant_note: Mutation signature F22Y/K232G/R235T/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235T/R238H/A272G isoenzyme A mutant


sequence_variant_note: Mutation signature F22Y/K232G/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R238H/A272G isoenzyme A mutant


sequence_variant_note: Mutation signature F22Y/K232G/R235G/R238E/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235G/R238E/A272G isoenzyme A mutant


sequence_variant_note: Mutation signature F22Y/K232G/R235G/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235G/R238H/A272G isoenzyme A mutant


column_label: Table 6: Full Kinetic Parameters with NADH as a Cofactor, row K232G/R238H, substrate/cofactor context NADH: kcat 1200 min^-1; Ka 0.66 mM for NADH; normalized kcat 20 s^-1; Km 0.66 mM; kcat/Km 30.303 s^-1*mM^-1.

raw_value_unit_evidence: kcat 1200 min^-1; Ka 0.66 mM for NADH


sequence_variant_note: Mutation signature F22Y/K232G/R235T/R238E/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235T/R238E/A272G isoenzyme A mutant


column_label: Table 8: Full Kinetic Parameters with NADPH as a Cofactor, row K232G/R238H, substrate/cofactor context 2,5-didehydro-D-gluconate: Kb 13 mM for 2,5-DKG substrate; normalized Km 13 mM.

normalized_value_unit_evidence: Km 13 mM

raw_value_unit_evidence: Kb 13 mM for 2,5-DKG substrate


sequence_variant_note: Mutation signature F22Y/S232T/R235S/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/S232T/R235S/R238H/A272G isoenzyme A mutant


enzyme_display_name: 2-(R)-hydroxypropyl-CoM dehydrogenase

organism: Xanthobacter autotrophicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R203A to reconstruct the assayed variant sequence.

smiles: CCC(=O)C

enzyme: 2-(R)-hydroxypropyl-CoM dehydrogenase


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; 303.15 K; buffer GPT; cofactor NAD+

column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-butanone span, enzyme row WT; column Vmax (units per mg) = 0.058; column Km (mM) = 52; column kcat (s^-1) = 0.027; column kcat/Km (M^-1 s^-1) = 0.52. captured primary segment: Table 2 row WT | ketone substrate 2-butanone | Vmax 0.058 units per mg | Km 52 mM | kcat 0.027 s^-1 | kcat/Km 0.52 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 52 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 52.0 mM. kcat: printed Table 2 cell 0.027 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 0.027 s^(-1). kcat/Km: printed Table 2 cell 0.52 M^-1 s^-1, that is 0.52 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.52 / 1000 = 0.0005200000000000001 s^-1 mM^-1. Quotient disclosure for this row: 0.027 / 52.0 = 0.0005192307692307692 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 0.5192307692307693 M^-1 s^-1, and the printed cell 0.52 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 2, 2-butanone span, enzyme row WT: Km = 52 mM; kcat = 0.027 s^-1; printed kcat/Km = 0.52 M^-1 s^-1.

row_label: Table 2, 2-butanone span, enzyme row WT


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R152A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R209A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56840 and applied mutation signature R196A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-butanone span, enzyme row R196A; column Vmax (units per mg) = 0.069; column Km (mM) = 23; column kcat (s^-1) = 0.033; column kcat/Km (M^-1 s^-1) = 1.4. captured primary segment: Table 2 row R196A | ketone substrate 2-butanone | Vmax 0.069 units per mg | Km 23 mM | kcat 0.033 s^-1 | kcat/Km 1.4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 23 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 23.0 mM. kcat: printed Table 2 cell 0.033 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 0.033 s^(-1). kcat/Km: printed Table 2 cell 1.4 M^-1 s^-1, that is 1.4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.4 / 1000 = 0.0014 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 0.033 / 23.0 = 0.0014347826086956522 s^-1 mM^-1, that is 1.434782608695652 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 1.4 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 2, 2-butanone span, enzyme row R196A: Km = 23 mM; kcat = 0.033 s^-1; printed kcat/Km = 1.4 M^-1 s^-1.


smiles: CCC(C)O

assay_conditions_summary: pH 7.5; 303.15 K; buffer mix (50 mM glycine; cofactor NAD+

column_label: Table 5 'Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol' (Biochemistry 2010, 49(16): 3487-3498); Table 5, enzyme block 'rR-HPCDH1', substrate row '(R)-2-butanol': column 'kcat (s^-1)' = 1.9; column 'Km (mM)' = 220; column 'kcat/Km (M^-1 s^-1)' = 8.69.

normalized_value_unit_evidence: kcat: printed Table 5 cell 1.9 s^-1; already in s^-1, no conversion; the value is 1.9 s^(-1) and the exported value is 9.3 s^(-1). Km: printed cell 220 mM; already in mM, no conversion; the value is 220.0 mM and the exported value is 220.0 mM. kcat/Km: printed cell 8.69 M^-1 s^-1; the column header prints M^-1 s^-1 and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.69 x 0.001 = 0.00869 s^-1 mM^-1; the exported value is 0.042272727272727274 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5, decoded plain-numeral transcription, Table 5, enzyme block 'rR-HPCDH1', substrate row '(R)-2-butanol': Km = 220 mM; kcat = 1.9 s^-1; printed kcat/Km = 8.69 M^-1 s^-1.

source_databases_merged: brenda skid uniprot


smiles: CCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-pentanol; column Vmax (units per mg) = 2.36; column Km (mM) = 20; column kcat (s^-1) = 1.1; column kcat/Km (M^-1 s^-1) = 5.6 x 10^1. captured primary segment: Table 1 row (R)-2-pentanol | Vmax 2.36 units per mg | Km 20 mM | kcat 1.1 s^-1 | kcat/Km 5.6 x 10^1 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 20 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 20.0 mM. kcat: printed Table 1 cell 1.1 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 1.1 s^(-1). kcat/Km: printed Table 1 cell 5.6 x 10^1 M^-1 s^-1, that is 56.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 56.0 / 1000 = 0.056 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 1.1 / 20.0 = 0.05500000000000001 s^-1 mM^-1, that is 55.00000000000001 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 5.6 x 10^1 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-pentanol: Km = 20 mM; kcat = 1.1 s^-1; printed kcat/Km = 5.6 x 10^1 M^-1 s^-1.


smiles: CCCCCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-octanol; column Vmax (units per mg) = 3.54; column Km (mM) = 1.08; column kcat (s^-1) = 1.7; column kcat/Km (M^-1 s^-1) = 1.5 x 10^3. captured primary segment: Table 1 row (R)-2-octanol | Vmax 3.54 units per mg | Km 1.08 mM | kcat 1.7 s^-1 | kcat/Km 1.5 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 1.08 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 1.08 mM. kcat: printed Table 1 cell 1.7 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 1.7 s^(-1). kcat/Km: printed Table 1 cell 1.5 x 10^3 M^-1 s^-1, that is 1500.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1500.0 / 1000 = 1.5 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 1.7 / 1.08 = 1.574074074074074 s^-1 mM^-1, that is 1574.074074074074 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 1.5 x 10^3 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-octanol: Km = 1.08 mM; kcat = 1.7 s^-1; printed kcat/Km = 1.5 x 10^3 M^-1 s^-1.


smiles: CCCCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-heptanol; column Vmax (units per mg) = 3.80; column Km (mM) = 2.64; column kcat (s^-1) = 1.8; column kcat/Km (M^-1 s^-1) = 6.8 x 10^2. captured primary segment: Table 1 row (R)-2-heptanol | Vmax 3.80 units per mg | Km 2.64 mM | kcat 1.8 s^-1 | kcat/Km 6.8 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 2.64 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 2.64 mM. kcat: printed Table 1 cell 1.8 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 1.8 s^(-1). kcat/Km: printed Table 1 cell 6.8 x 10^2 M^-1 s^-1, that is 680.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 680.0 / 1000 = 0.68 s^-1 mM^-1. Quotient disclosure for this row: 1.8 / 2.64 = 0.6818181818181818 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 681.8181818181818 M^-1 s^-1, and the printed cell 6.8 x 10^2 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-heptanol: Km = 2.64 mM; kcat = 1.8 s^-1; printed kcat/Km = 6.8 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R196A to reconstruct the assayed variant sequence.


smiles: CCCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-hexanol; column Vmax (units per mg) = 5.66; column Km (mM) = 4.6; column kcat (s^-1) = 2.7; column kcat/Km (M^-1 s^-1) = 5.8 x 10^2. captured primary segment: Table 1 row (R)-2-hexanol | Vmax 5.66 units per mg | Km 4.6 mM | kcat 2.7 s^-1 | kcat/Km 5.8 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 4.6 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 4.6 mM. kcat: printed Table 1 cell 2.7 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 2.7 s^(-1). kcat/Km: printed Table 1 cell 5.8 x 10^2 M^-1 s^-1, that is 580.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 580.0 / 1000 = 0.58 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 2.7 / 4.6 = 0.5869565217391305 s^-1 mM^-1, that is 586.9565217391305 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 5.8 x 10^2 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-hexanol: Km = 4.6 mM; kcat = 2.7 s^-1; printed kcat/Km = 5.8 x 10^2 M^-1 s^-1.


smiles: CC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row 2-propanol; column Vmax (units per mg) = 6.2; column Km (mM) = 1726; column kcat (s^-1) = 2.9; column kcat/Km (M^-1 s^-1) = 1.7 x 10^0. captured primary segment: Table 1 row 2-propanol | Vmax 6.2 units per mg | Km 1726 mM | kcat 2.9 s^-1 | kcat/Km 1.7 x 10^0 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 1726 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 1726.0 mM. kcat: printed Table 1 cell 2.9 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 2.9 s^(-1). kcat/Km: printed Table 1 cell 1.7 x 10^0 M^-1 s^-1, that is 1.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 / 1000 = 0.0017 s^-1 mM^-1. Quotient disclosure for this row: 2.9 / 1726.0 = 0.0016801853997682502 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 1.6801853997682503 M^-1 s^-1, and the printed cell 1.7 x 10^0 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 1, secondary-alcohol row 2-propanol: Km = 1726 mM; kcat = 2.9 s^-1; printed kcat/Km = 1.7 x 10^0 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56840 and applied mutation signature R209A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-KPC span, enzyme row R209A; column Vmax (units per mg) = 32; column Km (mM) = 0.15; column kcat (s^-1) = 15; column kcat/Km (M^-1 s^-1) = 1.0 x 10^5. captured primary segment: Table 2 row R209A | ketone substrate 2-KPC | Vmax 32 units per mg | Km 0.15 mM | kcat 15 s^-1 | kcat/Km 1.0 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.15 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 0.15 mM. kcat: printed Table 2 cell 15 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 15.0 s^(-1). kcat/Km: printed Table 2 cell 1.0 x 10^5 M^-1 s^-1, that is 100000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 100000.0 / 1000 = 100.0 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 15.0 / 0.15 = 100.0 s^-1 mM^-1, that is 100000.0 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 1.0 x 10^5 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 2, 2-KPC span, enzyme row R209A: Km = 0.15 mM; kcat = 15 s^-1; printed kcat/Km = 1.0 x 10^5 M^-1 s^-1.

row_label: Table 2, 2-KPC span, enzyme row R209A