column_label: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699Q; columns kcat (min^-1), KACAC (uM) and kcat/KACAC (uM^-1 min^-1); kcat cell = 26 min^-1; KACAC cell = 1.2 uM; kcat/KACAC cell = 22; author manuscript page 15 (PDF page 15). captured primary segment: acetoacetyl-CoA | K1699Q HFAS, the site-directed K1699Q mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE beta-ketoacyl reductase block, enzyme row K1699Q: Km ACAC 1.2 uM | kcat 26 min^-1 | kcat/Km ACAC printed cell 22 under the column head kcat/KACAC (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699Q: KACAC = 1.2 uM; kcat = 26 min^-1; printed kcat/KACAC = 22 uM^-1 min^-1.


organism: Homo sapiens

substrate_name: acetoacetyl-CoA

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: PMC2442872 section T3; table subsection beta-ketoacyl reductase; row label WT | beta-ketoacyl reductase | acetoacetyl-CoA; column label kcat plus substrate-specific K and kcat/K columns

normalized_value_unit_evidence: Unit conversion gives kcat 4.0 s^-1, Km 0.01 mM, and kcat/Km 400.0 s^-1 mM^-1; these equal the exported central values.

raw_value_unit_evidence: PMC2442872 section T3, row WT | beta-ketoacyl reductase | acetoacetyl-CoA; columns kcat, K_ACAC, and kcat/K_ACAC columns: 240 ± 12 min^-1; K_ACAC 10 ± 2 µM; kcat/K_ACAC 24 ± 6 µM^-1 min^-1.

table_label: Table 3 beta-ketoacyl reductase WT subsection

data_origin: experimental

substrate: acetoacetyl-CoA

status: verified

source: oed


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH7

substrate_name: 10-OH-decanoic acid (with 0.1 M sodium phosphate at pH 7.5)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

smiles: C(CCCCC(=O)O)CCCCO

column_label: Table 1, row 10-OH-Decanoic acid, column Km (mM).

raw_value_unit_evidence: Table 1 reports 10-OH-Decanoic acid Km=0.1 mM.

row_label: 10-OH-Decanoic acid

table_label: Table 1: Kinetic constants of human class IV ADH with gamma-hydroxyfatty acids and products of lipid peroxidation

source: uniprot


substrate_name: hexanol (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCCCCO

column_label: Table 1, row Hexanol, column Km (mM).

raw_value_unit_evidence: Table 1 reports Hexanol Km=0.14 mM.

row_label: Hexanol

enzyme: All-trans-retinol dehydrogenase [NAD(+)] ADH7


substrate_name: hexanal (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCCCC=O

column_label: Table 1, row Hexanal, column Km (mM).

raw_value_unit_evidence: Table 1 reports Hexanal Km=0.02 mM.

row_label: Hexanal


substrate_name: 2-hexenol (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCC=CCO

column_label: Table 1, row 2-Hexenol, column Km (mM).

raw_value_unit_evidence: Table 1 reports 2-Hexenol Km=0.017 mM.


substrate_name: 2-hexenal (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCC=CC=O

column_label: Table 1, row 2-Hexenal, column Km (mM).

raw_value_unit_evidence: Table 1 reports 2-Hexenal Km=0.025 mM.


substrate_name: 4-hydroxynonenal (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCCCC(C=CC=O)O

column_label: Table 1, row 4-Hydroxynonenal, column Km (mM).

raw_value_unit_evidence: Table 1 reports 4-Hydroxynonenal Km=0.038 mM.


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH1B

substrate_name: all-trans-4-hydroxyretinol (in allele ADH1B*1)

verification_status: unverified

status: unverified


substrate_name: all-trans-4-oxoretinal (in allele ADH1B*1)

enzyme: All-trans-retinol dehydrogenase [NAD(+)] ADH1B


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: all-trans-retinal

substrate: all-trans-retinal


enzyme_display_name: Retinol dehydrogenase 16

assay_conditions_summary: cofactor NAD+

column_label: Table I row Androstane-diol has Km 0.22 +/- 0.06 uM and Vmax 6.9 +/- 0.5 nmol/min/mg.

raw_value_unit_evidence: Table I reports Androstane-diol Km = 0.22 +/- 0.06 uM.

row_label: Androstane-diol

table_label: JBC 273(31) Table I, substrate kinetics of recombinant human RoDH-4

enzyme: Retinol dehydrogenase 16


assay_conditions_summary: pH 7.3; cofactor NADH

column_label: Table I; K_m (uM) block; Dihydrotestosterone row; raw Km value 0.80 uM.

raw_value_unit_evidence: Table I reports RoDH-4 steroid-substrate K_m for dihydrotestosterone = 0.80 uM.

row_label: RoDH-4 steroid substrate K_m block; Dihydrotestosterone row

table_label: PMID 9677409, Table I: Kinetic constants of RoDH-4 for steroid substrates


substrate_name: NAD

assay_conditions_summary: pH 7.3; cofactor NADP+

column_label: Table II; K_m (uM) block; NAD+ row; raw Km value 0.13 uM.

raw_value_unit_evidence: Table II reports RoDH-4 cofactor K_m for NAD+ = 0.13 uM.

row_label: RoDH-4 cofactor K_m block; NAD+ row

table_label: PMID 9677409, Table II: Apparent K_m values of RoDH-4 for cofactors

substrate: NAD


substrate_name: NADP

column_label: Table II; K_m (uM) block; NADP+ row; raw Km value 190 uM.

raw_value_unit_evidence: Table II reports RoDH-4 cofactor K_m for NADP+ = 190 uM.

row_label: RoDH-4 cofactor K_m block; NADP+ row

substrate: NADP


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: allopregnanolone

substrate: allopregnanolone


enzyme: Dehydrogenase/reductase SDR family member 9


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


substrate_name: androsterone

substrate: androsterone


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


enzyme_display_name: L-threonine 3-dehydrogenase

organism: Thermoplasma volcanium

substrate_name: L-serine

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G114A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: L-threonine 3-dehydrogenase

substrate: L-serine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I113A to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97BK3 and applied mutation signature T178A to reconstruct the assayed variant sequence.

column_label: ACS Omega DOI 10.1021/acsomega.7b00519 Supporting Information Table S3. Kinetic characterization of tvTDH and mutants on L-serine; row T178A; columns kcat/KM (M^-1 s^-1), kcat (s^-1), and KM (M).

raw_value_unit_evidence: Table S3. Kinetic characterization of tvTDH and mutants on L-serine row T178A: kcat/KM 9.5E-03 M^-1 s^-1; kcat 1.4E-02 s^-1; KM 1.6E+00 M.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G114A to reconstruct the assayed variant sequence.

column_label: ACS Omega DOI 10.1021/acsomega.7b00519 Supporting Information Table S3. Kinetic characterization of tvTDH and mutants on L-serine; row WT; columns kcat/KM (M^-1 s^-1), kcat (s^-1), and KM (M).

raw_value_unit_evidence: Table S3. Kinetic characterization of tvTDH and mutants on L-serine row WT: kcat/KM 1.7E-01 M^-1 s^-1; kcat 1.0E-02 s^-1; KM 6.1E-02 M.

row_label: WT


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97BK3 and applied mutation signature G114A to reconstruct the assayed variant sequence.

column_label: ACS Omega DOI 10.1021/acsomega.7b00519 Supporting Information Table S4. Kinetic characterization of tvTDH and mutants on (R)-(-)-1-amino-2-propanol; row G114A; columns kcat/KM (M^-1 s^-1), kcat (s^-1), and KM (M).

raw_value_unit_evidence: Table S4. Kinetic characterization of tvTDH and mutants on (R)-(-)-1-amino-2-propanol row G114A: kcat/KM 2.3E-02 M^-1 s^-1; kcat 8.5E-03 s^-1; KM 3.6E-01 M.


substrate_name: L-Threonine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97BK3 and applied mutation signature D180A to reconstruct the assayed variant sequence.

column_label: ACS Omega DOI 10.1021/acsomega.7b00519 Supporting Information Table S2. Kinetic characterization of tvTDH and mutants on L-threonine; row D180A*; columns kcat/KM (M^-1 s^-1), kcat (s^-1), and KM (M).

raw_value_unit_evidence: Table S2. Kinetic characterization of tvTDH and mutants on L-threonine row D180A*: kcat/KM 1.1E+01 M^-1 s^-1; kcat 3.7E-01 s^-1; KM 4.3E-02 M.

substrate: L-Threonine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97BK3 and applied mutation signature I113A to reconstruct the assayed variant sequence.

column_label: ACS Omega DOI 10.1021/acsomega.7b00519 Supporting Information Table S2. Kinetic characterization of tvTDH and mutants on L-threonine; row I113A; columns kcat/KM (M^-1 s^-1), kcat (s^-1), and KM (M).

raw_value_unit_evidence: Table S2. Kinetic characterization of tvTDH and mutants on L-threonine row I113A: kcat/KM 1.1E+02 M^-1 s^-1; kcat 7.3E-01 s^-1; KM 8.8E-03 M.


column_label: ACS Omega DOI 10.1021/acsomega.7b00519 Supporting Information Table S2. Kinetic characterization of tvTDH and mutants on L-threonine; row WT; columns kcat/KM (M^-1 s^-1), kcat (s^-1), and KM (M).

raw_value_unit_evidence: Table S2. Kinetic characterization of tvTDH and mutants on L-threonine row WT: kcat/KM 6.6E+02 M^-1 s^-1; kcat 1.7E+00 s^-1; KM 2.6E-03 M.


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Mus musculus


enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


substrate_name: estradiol

substrate: estradiol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M333E to reconstruct the assayed variant sequence.


substrate_name: L-threonine

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

substrate: L-threonine


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: pyridoxal 4-dehydrogenase

organism: Microbacterium luteolum

substrate_name: D-Arabinose

assay_conditions_summary: pH 8; 303.15 K; buffer 50 mM sodium phosphate; cofactor NAD+

column_label: Table II; row D-Arabinose; columns Km, Kcat, Kcat/Km

raw_value_unit_evidence: Table II cells: compound=D-Arabinose; Km=0.91 +/- 0.08 mM; Kcat=175 +/- 1.9 s^-1; Kcat/Km=192.3 s^-1 mM^-1

row_label: D-Arabinose

table_label: Table II

enzyme: pyridoxal 4-dehydrogenase

substrate: D-Arabinose


substrate_name: L-Fucose

column_label: Table II; row L-Fucose; columns Km, Kcat, Kcat/Km

raw_value_unit_evidence: Table II cells: compound=L-Fucose; Km=0.41 +/- 0.05 mM; Kcat=125 +/- 2.0 s^-1; Kcat/Km=304.9 s^-1 mM^-1

row_label: L-Fucose

substrate: L-Fucose


substrate_name: L-Xylose

substrate: L-Xylose


substrate_name: Pyridoxal

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

column_label: Table II; row Pyridoxal; columns Km, Kcat, Kcat/Km

normalized_value_unit_evidence: normalized: Km=13.0 mM; Kcat=59.2 s^-1; table Kcat/Km=4.6 s^-1 mM^-1; row-derived central quotient=59.2/13=4.553846153846154 s^-1 mM^-1

raw_value_unit_evidence: Table II cells: compound=Pyridoxal; Km=13 +/- 2.5 mM; Kcat=59.2 +/- 7.3 s^-1; Kcat/Km=4.6 s^-1 mM^-1

row_label: Pyridoxal

substrate: Pyridoxal


substrate_name: NADPH (with homotetramer)

assay_conditions_summary: cofactor NADPH

column_label: Properties of recombinant CBR4 prose states the Km value for NADPH was 11 uM.

raw_value_unit_evidence: Km raw_value=11 raw_unit=uM

row_label: NADPH

table_label: Results and discussion / Properties of recombinant CBR4

substrate: NADPH (with homotetramer)


assay_conditions_summary: pH 7.4; buffer potassium phosphate; cofactor NADPH

column_label: Table 1 row 9,10-PQ lists Km 1.6 uM.

raw_value_unit_evidence: Km raw_value=1.6 raw_unit=uM

table_label: Table 1. Apparent kinetic constants for quinones.


substrate_name: 1,4-benzoquinone (with homotetramer)

column_label: Table 1 row 1,4-BQ lists Km 1.9 uM.

raw_value_unit_evidence: Km raw_value=1.9 raw_unit=uM

substrate: 1,4-benzoquinone (with homotetramer)


organism: Cupriavidus necator

substrate_name: acetoacetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q47L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: acetoacetyl-CoA


substrate_name: NADPH

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: Fatty acid synthase

substrate_name: acetyl-CoA

column_label: Overall reaction block; WT row; K ACET column; Km raw value 7 +/- 3 uM.

raw_value_unit_evidence: WT overall reaction row reports K ACET = 7 +/- 3 uM.

row_label: WT, Overall reaction; metric columns kcat, K NADPH, K MAL, K ACET, kcat/K columns

table_label: PMID 16215233, Table 3: Kinetic evaluation of wild-type, K1699A, and K1699Q HFAS

enzyme: Fatty acid synthase

substrate: acetyl-CoA


substrate_name: malonyl-CoA

column_label: Overall reaction block; WT row; K MAL column; Km raw value 6 +/- 2 uM.

raw_value_unit_evidence: WT overall reaction row reports K MAL = 6 +/- 2 uM.

substrate: malonyl-CoA


column_label: Overall reaction block; WT row; K NADPH column; Km raw value 5 +/- 1 uM.

raw_value_unit_evidence: WT overall reaction row reports K NADPH = 5 +/- 1 uM.


substrate_name: butanoyl-CoA

proof_lines:
human fatty acid synthase
substrate recognition
Table 3

substrate: butanoyl-CoA


organism: Persea americana

source_db: brenda

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

proof_lines: NADPH-linked 3-oxoacyl-(acyl-carrier protein) reductase

source: brenda


assay_conditions_summary: cofactor CoA


substrate_name: acetoacetyl-N-acetylcysteamine

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

proof_lines:
synthetic analogues
natural ACP substrate
Persea americana fruit mesocarp

substrate: acetoacetyl-N-acetylcysteamine


enzyme_display_name: NADPH-dependent 1-acyldihydroxyacetone phosphate reductase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: p-nitrophenylacetate

column_label: Table 6: In vitro esterase activities row Ayr1p / pNPA: Km raw_value=3.50 +/- 0.52 raw_unit=mM; Vmax context raw_value=18.50 +/- 2.76 raw_unit=umol/min/mg. Km normalized_value=3.5 normalized_unit=mM; CatLog value=3.5 mM.

row_label: Ayr1p / pNPA

table_label: Table 6: In vitro esterase activities

substrate: p-nitrophenylacetate


substrate_name: p-nitrophenylbutyrate

column_label: Table 6: In vitro esterase activities row Ayr1p / pNPB: Km raw_value=1.52 +/- 0.24 raw_unit=mM; Vmax context raw_value=14.06 +/- 2.23 raw_unit=umol/min/mg. Km normalized_value=1.52 normalized_unit=mM; CatLog value=1.52 mM.

row_label: Ayr1p / pNPB

enzyme: NADPH-dependent 1-acyldihydroxyacetone phosphate reductase

substrate: p-nitrophenylbutyrate


assay_conditions_summary: pH 7.5; buffer pH 7

column_label: Results prose / Figure 7: In vitro triacylglycerol lipase assays row Ayr1p hydrolyzing [9,10-3H]triolein: Km raw_value=61.21 raw_unit=uM; Vmax context raw_value=10.93 raw_unit=pmol/h/mg. Km normalized_value=0.06121 normalized_unit=mM after uM-to-mM conversion; CatLog value=0.06121 mM.

row_label: Ayr1p hydrolyzing [9,10-3H]triolein


substrate_name: Retinol

column_label: Table 1: Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids (Biochem. J. 2006, 399:101-109); substrate block 'All-trans-Retinol'; enzyme column head 'RoDH-4'; parameter rows 'K m (uM)' = 1.1, 'k cat (min^-1)' = 1.20 and 'k cat /K m (mM^-1 min^-1)' = 1100. The six enzyme column heads read, left to right, AKR1B1, AKR1B10, ADH4, ADH1B2, RDH11* and RoDH-4.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.1 uM; 1.1 / 1000 = 0.0011 mM. kcat: printed Table 1 cell 1.20 min^-1; 1.20 / 60 = 0.02 s^-1. kcat/Km: printed Table 1 cell 1100 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 of 1 s^-1 mM^-1, so 1100 / 60 = 18.333333333333332 s^-1 mM^-1. The prior exported tuple for this row carried these same three quantities rounded to one significant digit; this pass writes the printed paper cells at their converted precision instead.

raw_value_unit_evidence: Table 1, substrate block 'All-trans-Retinol', enzyme column 'RoDH-4': K m (uM) = 1.1; k cat (min^-1) = 1.20; printed k cat /K m (mM^-1 min^-1) = 1100.

substrate: Retinol


substrate_name: all-trans-retinaldehyde (in allele ADH1B*2)


substrate_name: all-trans-retinol (in allele ADH1B*2)

substrate: all-trans-retinol (in allele ADH1B*2)


organism: Escherichia coli (strain K12)

substrate_name: L-threonine (at 37 degrees Celsius and pH 8.4)


substrate_name: NAD(+) (at 37 degrees Celsius and pH 8.4)


enzyme_display_name: 4-oxoproline reductase

organism: Oryctolagus cuniculus

enzyme: 4-oxoproline reductase


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Pyrococcus horikoshii

substrate_name: NAD+

assay_conditions_summary: pH 7.5; 338.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 338.15 K; cofactor NADP+

proof_lines: Pyrococcus horikoshii L-threonine dehydrogenase

substrate: NADP+


substrate_name: all-trans-Retinal

proof_lines: Purified RalR1-His(6) exhibited the apparent K(m) values for all-trans-retinal and all-trans-retinol of 0.12 and 0.6 microM, respectively.

substrate: all-trans-Retinal


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: NADP(+) (at 65 degrees Celsius)

assay_conditions_summary: cofactor NADP+

proof_lines:
NADP+
L-threonine dehydrogenase
Pyrococcus horikoshii

substrate: NADP(+) (at 65 degrees Celsius)


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: butan-2,3-diol (at 70 degrees Celsius)

smiles: CC(C(C)O)O

assay_conditions_summary: 343.15 K; cofactor NAD+

proof_lines:
Pyrococcus furiosus
threonine dehydrogenase
L-threonine

substrate: butan-2,3-diol (at 70 degrees Celsius)


organism: Escherichia coli

assay_conditions_summary: pH 8.4; 310.15 K; buffer 50 mM Tris.HCl; cofactor NAD+


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH4

substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: all-trans-retinal

enzyme: All-trans-retinol dehydrogenase [NAD(+)] ADH4

substrate: all-trans-retinal


organism: Kangiella koreensis


assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: Table I row Androsterone, column Km (microM), reports 0.14 +/- 0.02.

raw_value_unit_evidence: Androsterone Km 0.14 +/- 0.02 microM

row_label: Androsterone

table_label: Table I. Kinetic constants of RoDH-4 for steroid substrates, PMID 9677409


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

assay_conditions_summary: pH 7.3; buffer pH 7; cofactor NAD+

column_label: JBC TABLE ONE, kinetic constants for purified alcohol dehydrogenases acting on 20-HETE, lists Human ADH4 with Km 9.5 +/- 0.8 uM.

raw_value_unit_evidence: Km raw_value=9.5 +/- 0.8 raw_unit=uM

row_label: Human ADH4

table_label: JBC TABLE ONE PMID 16081420 purified alcohol dehydrogenases acting on 20-HETE


assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Table II row Human wt, p-Benzoquinone column group, Km column = 0.088 mM.

raw_value_unit_evidence: Km raw_value=0.088 raw_unit=mM

row_label: Human wt; p-benzoquinone


column_label: Table II row Mouse wt, p-Benzoquinone column group, Km column = 0.24 mM.

raw_value_unit_evidence: Km raw_value=0.24 raw_unit=mM

row_label: Mouse wt; p-benzoquinone


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase 13

column_label: Supplementary Appendix Figure S12 panel A plots enzymatic activity versus [17beta-Estradiol] uM and annotates Km=6.08 uM for purified recombinant HSD17B13 protein.

raw_value_unit_evidence: Km raw_value=6.08 raw_unit=uM

row_label: Purified recombinant human HSD17B13 protein / 17beta-estradiol

table_label: NEJM Supplementary Appendix Figure S12 panel A

enzyme: 17-beta-hydroxysteroid dehydrogenase 13


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

organism: Oryza sativa

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

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

enzyme: ketol-acid reductoisomerase (NADP+)


km_display: Not reported

assay_conditions_summary: pH 8


substrate_name: NADPH

substrate: NADPH


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


organism: Mycobacterium tuberculosis


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Burkholderia cenocepacia

proof_lines: pH and temperature not specified in the publication

enzyme: hydroxymethylglutaryl-CoA reductase


organism: Pseudomonas sp. 'mevalonii'

assay_conditions_summary: cofactor NAD+

proof_lines: wild-type enzyme, oxidative acylation of mevalonate


enzyme_display_name: phosphoglycerate dehydrogenase

assay_conditions_summary: pH 7; buffer 50 mM MOPS

proof_lines: in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication

proof_lines: in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication

enzyme: phosphoglycerate dehydrogenase


organism: Bacillus subtilis


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Mycolicibacterium smegmatis


assay_conditions_summary: 298.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.1; cofactor NADH


enzyme_display_name: carnitine 3-dehydrogenase

organism: Xanthomonas translucens

substrate_name: carnitine

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

proof_lines: mutant enzyme S120A, at pH 9.5, temperature not specified in the publication

enzyme: carnitine 3-dehydrogenase

substrate: carnitine


proof_lines: mutant enzyme R200A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme F234A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme Y147A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme W228A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme F189A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme M231A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme Y237A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme R297A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme S117A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme M246A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme T262A, at pH 9.5, temperature not specified in the publication


substrate_name: L-carnitine

substrate: L-carnitine


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+

proof_lines: mutant enzyme G223S/A224F, at pH 9.5 and 30°C


enzyme_display_name: apiose 1-reductase

organism: Micrococcus sp.

enzyme: apiose 1-reductase


substrate_name: D-apiitol

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

substrate: D-apiitol


substrate_name: D-apiose

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

substrate: D-apiose


organism: Klebsiella aerogenes


enzyme_display_name: aromatic 2-oxoacid reductase

organism: Candida maltosa

enzyme: aromatic 2-oxoacid reductase


assay_conditions_summary: cofactor NADPH


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: p-hydroxyphenyllactate

substrate: p-hydroxyphenyllactate


substrate_name: D-phenyllactate

substrate: D-phenyllactate


substrate_name: NAD+

substrate: NAD+


substrate_name: indolelactate

substrate: indolelactate


proof_lines: mutant enzyme I190V/A191G, at pH 9.5 and 30°C


proof_lines: mutant enzyme G233S/A224F, at pH 9.5 and 30°C


proof_lines: mutant enzyme N144A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme Q252A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme E185A, at pH 9.5, temperature not specified in the publication


proof_lines: wild type enzyme, at pH 9.5, temperature not specified in the publication


assay_conditions_summary: pH 9.5; cofactor NAD+


proof_lines: mutant enzyme F234A, at pH 9.5, temperature not specified in the publication


enzyme_display_name: ribose 1-dehydrogenase (NADP+)

organism: Sus scrofa

substrate_name: D-xylose

enzyme: ribose 1-dehydrogenase (NADP+)

substrate: D-xylose


substrate_name: D-arabinose

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

substrate: D-arabinose


organism: Rhizobium meliloti (strain 1021)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 6.2 sec(-1) with L-carnitine as substrate. kcat is 5.1 sec(-1) with NAD(+) as substrate. kcat is 0.9 sec(-1) with L-carnitinyl-CoA as substrate. kcat is 142.3 sec(-1) with betainyl-CoA as substrate.


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: L-carnitinyl-CoA

substrate: L-carnitinyl-CoA


substrate_name: betainyl-CoA

substrate: betainyl-CoA


enzyme_display_name: Aldo-keto reductase family 1 member C2

organism: Homo sapiens

substrate_name: (s)-tetralol (oxidation)

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

enzyme: Aldo-keto reductase family 1 member C2

substrate: (s)-tetralol (oxidation)


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: (s)-tetralol

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

enzyme: Aldo-keto reductase family 1 member C1

substrate: (s)-tetralol


substrate_name: NADPH

substrate: NADPH


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


proof_lines: mutant enzyme F189A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme R200A, at pH 9.5, temperature not specified in the publication


proof_lines: mutant enzyme S120A, at pH 9.5, temperature not specified in the publication


substrate_name: carnitine

proof_lines: Km above 2000 mM, mutant enzyme F249A, at pH 9.5, temperature not specified in the publication

substrate: carnitine


proof_lines: Km above 2000 mM, mutant enzyme F253A, at pH 9.5, temperature not specified in the publication


proof_lines: Km above 2000 mM, mutant enzyme W261A, at pH 9.5, temperature not specified in the publication


proof_lines: Km above 2000 mM, mutant enzyme D298A, at pH 9.5, temperature not specified in the publication


enzyme_display_name: L-carnitine dehydrogenase

organism: Pseudomonas sp

proof_lines: Part of the values are for the recombinant protein expressed in E.coli (PubMed:20530902). Other values are for the wild-type protein (Ref.2).

enzyme: L-carnitine dehydrogenase


organism: Streptomyces viridifaciens

column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 2H2M3KB; enzyme column Svi2 Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=2 s^-1; km paper=1.8 mM; kcat_over_km paper=1.111 s^-1 mM^-1; kcat export=2 s^(-1); kcat_over_km export=1.1111111111111112 s^(-1)*mM^(-1); km export=1.8 mM.

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 2H2M3KB, enzyme Svi2; kcat (s^-1): 2 ± 0.07; K_M (mM): 1.8 ± 0.9; kcat/K_M (M^-1 s^-1): 1111 ± 115.

row_label: 2H2M3KB | Svi2


column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label MAA; enzyme column Svi2 Required metric(s) kcat, kcat_over_km, km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=2 s^-1; km paper=50 mM; kcat_over_km paper=0.04 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row MAA, enzyme Svi2; kcat (s^-1): 2 ± 0.2; K_M (mM): 50 ± 5; kcat/K_M (M^-1 s^-1): 40 ± 5.

row_label: MAA | Svi2


substrate_name: Hydroxypyruvate

column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label HP; enzyme column Svi2 Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=2 s^-1; km paper=50 mM; kcat_over_km paper=0.05 s^-1 mM^-1; kcat export=2 s^(-1); kcat_over_km export=0.04 s^(-1)*mM^(-1); km export=50 mM.

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row HP, enzyme Svi2; kcat (s^-1): 2 ± 0.2; K_M (mM): 50 ± 5; kcat/K_M (M^-1 s^-1): 50 ± 4.

row_label: HP | Svi2

substrate: Hydroxypyruvate


column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 3H3M2KB; enzyme column Svi2 Required metric(s) kcat, kcat_over_km, km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=2.5 s^-1; km paper=5 mM; kcat_over_km paper=0.5 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 3H3M2KB, enzyme Svi2; kcat (s^-1): 2.5 ± 0.3; K_M (mM): 5 ± 4.8; kcat/K_M (M^-1 s^-1): 500 ± 48.

row_label: 3H3M2KB | Svi2


substrate_name: pyruvate

column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label Pyr; enzyme column Svi2 Required metric(s) kcat, kcat_over_km, km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=5.7 s^-1; km paper=1140 mM; kcat_over_km paper=0.005 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row Pyr, enzyme Svi2; kcat (s^-1): 5.7 ± 0.5; K_M (mM): 1140 ± 112; kcat/K_M (M^-1 s^-1): 5 ± 0.4.

row_label: Pyr | Svi2

substrate: pyruvate


substrate_name: (s)-indan-1-ol (oxidation)

substrate: (s)-indan-1-ol (oxidation)


substrate_name: 5alpha-androstan-3,17-dione (reduction)

substrate: 5alpha-androstan-3,17-dione (reduction)


substrate_name: progesterone (reduction)

substrate: progesterone (reduction)


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7; cofactor NADP+

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

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


assay_conditions_summary: pH 7; cofactor NADPH

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

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

row_label: Progesterone reduction / AKR1C1


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

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


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

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


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

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

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


substrate_name: testosterone (oxidation)

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

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

row_label: Testosterone oxidation / AKR1C1 (R)

substrate: testosterone (oxidation)


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

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


organism: Alcaligenes sp.

substrate_name: NAD+

substrate: NAD+


substrate_name: L-carnitine

substrate: L-carnitine


enzyme_display_name: indanol dehydrogenase

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Primary Table 4; row DD4, substrate 1-indanol; columns KM, kcat, and kcat/KM. Primary Table 2 maps DD4 to AKR1C4.

raw_value_unit_evidence: Table 4 DD4 / 1-indanol: KM=170 uM; kcat=9.5 min^-1; kcat/KM=56 min^-1 mM^-1.

row_label: DD4 (AKR1C4) / 1-indanol

table_label: Table 4

enzyme: indanol dehydrogenase


column_label: Primary Table 4; row DDX, substrate 1-indanol; columns KM, kcat, and kcat/KM. Primary Table 2 maps DDX to AKR1C3.

raw_value_unit_evidence: Table 4 DDX / 1-indanol: KM=1400 uM; kcat=5.2 min^-1; kcat/KM=3.7 min^-1 mM^-1.

row_label: DDX (AKR1C3) / 1-indanol


column_label: Primary Table 4; row DD2, substrate 1-indanol; columns KM, kcat, and kcat/KM. Primary Table 2 maps DD2 to AKR1C2.

raw_value_unit_evidence: Table 4 DD2 / 1-indanol: KM=940 uM; kcat=9.8 min^-1; kcat/KM=11 min^-1 mM^-1.

row_label: DD2 (AKR1C2) / 1-indanol


column_label: Primary Table 4; row DD1, substrate 1-indanol; columns KM, kcat, and kcat/KM. Primary Table 2 maps DD1 to AKR1C1.

raw_value_unit_evidence: Table 4 DD1 / 1-indanol: KM=48 uM; kcat=12.5 min^-1; kcat/KM=260 min^-1 mM^-1.

row_label: DD1 (AKR1C1) / 1-indanol


enzyme_display_name: Aromatic 2-oxoacid reductase

organism: Clostridium sporogenes (strain ATCC 7955 / DSM 767 / NBRC 16411 / NCIMB 8053 / NCTC 8594 / PA 3679)

substrate_name: phenylpyruvate

enzyme: Aromatic 2-oxoacid reductase

substrate: phenylpyruvate


organism: Rhizobium sp

substrate_name: NAD(+)

substrate: NAD(+)


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: L-carnitine (at pH 9.5)

substrate: L-carnitine (at pH 9.5)


assay_conditions_summary: pH 9; cofactor NAD+

column_label: Tabelle 2 lists NAD+ (pH 9,0; 0,05 M Tris/HCl; 100 pMol L-Carnitin/ml) = 1,6 x 10-4 Mol/l.

raw_value_unit_evidence: Km raw_value=1,6 x 10-4 raw_unit=Mol/l

row_label: NAD+ row

table_label: Tabelle 2. Michaelis-Konstanten der Carnitindehydrogenase


substrate_name: 3-dehydrocarnitine (at pH 7.2)

assay_conditions_summary: pH 7.2; cofactor NAD+

column_label: Tabelle 2 lists 3-Dehydrocarnitin (pH 7,2; 0,05 M Tris/HCl; 0,125 pMol NADH/ml) = 1,3 x 10-3 Mol/l.

raw_value_unit_evidence: Km raw_value=1,3 x 10-3 raw_unit=Mol/l

row_label: 3-Dehydrocarnitin row

substrate: 3-dehydrocarnitine (at pH 7.2)


substrate_name: NADH (at pH 7.2)

column_label: Tabelle 2 lists NADH (pH 7.2; 0,05 M Tris/HCl; 12,5 pMol 3-Dehydrocarnitin/ml) = 2,2 x 10-5 Mol/l.

raw_value_unit_evidence: Km raw_value=2,2 x 10-5 raw_unit=Mol/l

row_label: NADH row

substrate: NADH (at pH 7.2)


organism: Clostridium sporogenes (strain ATCC 15579)

substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


substrate_name: NADH (in the presence of indolepyruvate)


substrate_name: indolelactate

substrate: indolelactate


substrate_name: p-hydroxyphenyllactate

substrate: p-hydroxyphenyllactate


substrate_name: NAD(+) (in the presence of indolelactate)


enzyme_display_name: D-arabinose 1-dehydrogenase (NAD+)

organism: Pseudomonas sp.

substrate_name: NADP+

enzyme: D-arabinose 1-dehydrogenase (NAD+)

substrate: NADP+


substrate_name: L-fucose

substrate: L-fucose


substrate_name: D-arabinose

substrate: D-arabinose


enzyme_display_name: UniProt Q96ZY1

organism: Sulfurisphaera tokodaii

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q96ZY1

source: skid


substrate_name: D-glucose

substrate: D-glucose


enzyme_display_name: UniProt Q977U7

organism: Haloferax mediterranei

substrate_name: NAD(P)+

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=40°C, pH=8.8

enzyme: UniProt Q977U7

substrate: NAD(P)+


proof_lines:
Raw SKiD Env: Temp=40°C, pH=8.8
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: beta-D-glucose

substrate: beta-D-glucose


enzyme_display_name: glucose 1-dehydrogenase (NADP(+))

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G206D with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

enzyme: glucose 1-dehydrogenase (NADP(+))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G206D/R207I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G206D/R207I/R208N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R207I 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.


enzyme_display_name: UniProt Q5SLC4

organism: Thermus thermophilus HB8

substrate_name: (R)-indanol

enzyme: UniProt Q5SLC4

substrate: (R)-indanol


substrate_name: alpha-tetralone

substrate: alpha-tetralone


substrate_name: D-fucose

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

substrate: D-fucose


substrate_name: D-xylose

substrate: D-xylose


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


substrate_name: D-talose

substrate: D-talose


substrate_name: D-galactosamine

substrate: D-galactosamine


substrate_name: cellobiose

substrate: cellobiose


substrate_name: cis-benzene dihydrodiol

substrate: cis-benzene dihydrodiol


substrate_name: isatin

substrate: isatin


enzyme_display_name: UniProt Q9HK51

organism: Thermoplasma acidophilum

substrate_name: D-mannose

enzyme: UniProt Q9HK51

substrate: D-mannose


enzyme_display_name: D-threo-aldose 1-dehydrogenase

organism: Agrobacterium tumefaciens

substrate_name: D-galactose

enzyme: D-threo-aldose 1-dehydrogenase

substrate: D-galactose


substrate_name: L-fucose (at 37 degrees Celsius)

substrate: L-fucose (at 37 degrees Celsius)


substrate_name: L-galactose (at 37 degrees Celsius)

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

substrate: L-galactose (at 37 degrees Celsius)


substrate_name: D-arabinose (at 37 degrees Celsius)

substrate: D-arabinose (at 37 degrees Celsius)


substrate_name: NADP(+) (at 37 degrees Celsius)

substrate: NADP(+) (at 37 degrees Celsius)


substrate_name: NAD(+) (at 37 degrees Celsius)

substrate: NAD(+) (at 37 degrees Celsius)


enzyme_display_name: aldose 1-dehydrogenase (NAD+)

substrate_name: (R)-tetralol

enzyme: aldose 1-dehydrogenase (NAD+)

substrate: (R)-tetralol


substrate_name: L-fucose

substrate: L-fucose


substrate_name: (R)-indanol

substrate: (R)-indanol


substrate_name: alpha-tetralone

substrate: alpha-tetralone


substrate_name: D-fucose

substrate: D-fucose


enzyme_display_name: glucose 1-dehydrogenase (NADP+)

substrate_name: D-glucose

enzyme: glucose 1-dehydrogenase (NADP+)

substrate: D-glucose


assay_conditions_summary: pH 8.8; 313.15 K; cofactor NADP+

proof_lines: cosubstrate NAD+, wild-type, pH 8.8, 40°C


substrate_name: NADP+

proof_lines:
wild-type
wild-type, pH 8.8, 40°C
wild type enzyme

substrate: NADP+


assay_conditions_summary: cofactor NADP+


proof_lines:
pH 9.0, 25°C, mutant enzyme I189V
pH 9.0, 80°C, mutant enzyme I189V


assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+


proof_lines:
pH 9.0, 25°C, wild-type enzyme
pH 9.0, 80°C, wild-type enzyme


proof_lines:
pH 9.0, 25°C, mutant enzyme V254I
pH 9.0, 80°C, mutant enzyme V254I


assay_conditions_summary: pH 8.8; 313.15 K; cofactor NAD+

proof_lines: cosubstrate NAD+, mutant G206D/R207I/R208N, pH 8.8, 40°C

proof_lines: mutant enzyme G206D/R207I/R208N, using NAD+ as cosubstrate


proof_lines: cosubstrate NAD+, mutant R207I, pH 8.8, 40°C

proof_lines: mutant enzyme R207I, using NADP+ as cosubstrate


proof_lines: cosubstrate NAD+, mutant G206D, pH 8.8, 40°C

proof_lines: mutant enzyme G206D, using NAD+ as cosubstrate


proof_lines: cosubstrate NAD+, mutant G206D/R207I, pH 8.8, 40°C

proof_lines: mutant enzyme G206D/R207I, using NAD+ as cosubstrate


substrate_name: NAD+

proof_lines:
wild-type, pH 8.8, 40°C
wild type enzyme

substrate: NAD+


proof_lines:
mutant G206D, pH 8.8, 40°C
mutant enzyme G206D


proof_lines:
mutant R207I, pH 8.8, 40°C
mutant enzyme R207I


proof_lines:
mutant G206D/R207I/R208N, pH 8.8, 40°C
mutant enzyme G206D/R207I/R208N


proof_lines:
mutant G206D/R207I, pH 8.8, 40°C
mutant enzyme G206D/R207I


enzyme_display_name: galactose 1-dehydrogenase (NADP+)

organism: Pseudomonas putida

enzyme: galactose 1-dehydrogenase (NADP+)


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


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

organism: Candida albicans

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


substrate_name: D-arabinose

substrate: D-arabinose


substrate_name: L-galactose

substrate: L-galactose


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: glucose 1-dehydrogenase (NAD+)

organism: Saccharolobus solfataricus

assay_conditions_summary: 343.15 K; buffer 100 mM triethanolamine/HCl; cofactor NADP+

proof_lines: in the presence of D-glucose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C

proof_lines: in the presence of D-galactose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C

proof_lines: in the presence of D-xylose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C

enzyme: glucose 1-dehydrogenase (NAD+)


proof_lines: in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C

proof_lines: in the presence of NAD+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C


assay_conditions_summary: 343.15 K; buffer 100 mM triethanolamine/HCl; cofactor NAD+


substrate_name: D-xylose

substrate: D-xylose


organism: Gluconobacter cerinus


substrate_name: NADPH

substrate: NADPH


substrate_name: D-mannose

assay_conditions_summary: pH 8; buffer pH 8

proof_lines:
in 0.1 M Tris-buffer pH 8.0
in 0.1 M potassium phosphate pH 6.2

substrate: D-mannose


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


organism: Sus scrofa

assay_conditions_summary: cofactor NAD+


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


substrate_name: digitoxose

substrate: digitoxose


substrate_name: D-ribose

substrate: D-ribose


enzyme_display_name: glucose 1-dehydrogenase (NAD(+))

organism: synthetic construct

enzyme: glucose 1-dehydrogenase (NAD(+))


assay_conditions_summary: pH 7.5; 313.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 313.15 K; cofactor NADP+


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

sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature I189V to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature V254I to reconstruct the assayed variant sequence.


substrate_name: D-altrose

substrate: D-altrose


organism: Aureobasidium pullulans


substrate_name: NAD(P)+

proof_lines:
with NADP+ as coenzyme
with NAD+ as coenzyme
pH 8.8, 40°C

substrate: NAD(P)+


proof_lines:
with NADP+ as coenzyme
pH 8.8, 40°C
with NAD+ as coenzyme


organism: Halococcus saccharolyticus


organism: Ovis aries aries

assay_conditions_summary: pH 10.4; cofactor NAD+

proof_lines:
at pH 10.4
at pH 8.6


proof_lines:
at pH 8.6
at pH 10.4


organism: Acinetobacter sp.

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


substrate_name: L-fucose

substrate: L-fucose


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


enzyme_display_name: sorbose 5-dehydrogenase (NADP+)

organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

enzyme: sorbose 5-dehydrogenase (NADP+)


substrate_name: 5-Keto-D-fructose 1-phosphate

substrate: 5-Keto-D-fructose 1-phosphate


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


organism: Neurospora crassa


organism: Trinickia caryophylli


substrate_name: L-Glucose

substrate: L-Glucose


organism: Pseudomonas sp.


organism: Filobasidium uniguttulatum


organism: Rattus norvegicus


organism: Clostridium pasteurianum

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: cofactor NADPH


substrate_name: D-galactose

substrate: D-galactose


enzyme_display_name: aldose 1-dehydrogenase

organism: Pseudomonas reinekei

substrate_name: D-Glucose; NAD+

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

enzyme: aldose 1-dehydrogenase

substrate: D-Glucose; NAD+


organism: Corynebacterium sp.


substrate_name: NADP+

substrate: NADP+


organism: Oryctolagus cuniculus

substrate_name: NAD+

sequence_source: multiple

proof_lines: kcat is 7.00 sec(-1) with L-fucose as substrate. kcat is 7.00 sec(-1) with NAD(+) as substrate (PubMed:38944119). kcat/KM=4878 min(-1) mM(-1) for L-fuctose (PubMed:38944119).

source_databases_merged: brenda uniprot

substrate: NAD+


enzyme_display_name: L-fucose dehydrogenase

organism: Homo sapiens

substrate_name: NAD(+)

proof_lines: kcat is 14.00 sec(-1) with L-fucose as substrate. kcat is 16.89 sec(-1) with NAD(+) as substrate (PubMed:38944119). kcat is 0.0003 sec(-1) with beta-estradiol as substrate. kcat is 0.00028sec(-1) with androst-5-en-3beta,17beta-diol as subst

enzyme: L-fucose dehydrogenase

substrate: NAD(+)


enzyme_display_name: Glucose 1-dehydrogenase

organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: glucose

proof_lines: The KM value for NAD(+) is superior to 30 mM, it could not be defined precisely as it was impossible to reach saturation of the enzyme.

enzyme: Glucose 1-dehydrogenase

substrate: glucose


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: D-arabinose 1-dehydrogenase (NAD+)

substrate_name: D-arabinose

proof_lines: pH 8.2, 25°C, recombinant His-tagged Ara2p

enzyme: D-arabinose 1-dehydrogenase (NAD+)

substrate: D-arabinose


assay_conditions_summary: pH 8.2; 298.15 K; cofactor NAD+


organism: Gluconobacter oxydans

proof_lines: kcat is 84.8 sec(-1) with glucose as substrate. kcat is 106 sec(-1) with mannose as substrate.


substrate_name: D-glucose

substrate: D-glucose


substrate_name: oestradiol

substrate: oestradiol


organism: Rhizobium leguminosarum bv. trifolii

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

assay_conditions_summary: pH 9; cofactor NADP+

proof_lines: with NAD+ as cosubstrate, at pH 9.0 and 23°C

proof_lines: with NADP+ as cosubstrate, at pH 9.0 and 23°C


proof_lines: kcat is 0.13 sec(-1) with L-fucose as substrate. kcat is 0.15 sec(-1) with NAD(+) as substrate.


organism: Bemisia argentifolii

substrate_name: fructose

substrate: fructose


organism: Agrobacterium tumefaciens


organism: Saccharolobus solfataricus

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

assay_conditions_summary: 343.15 K; cofactor NAD+

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

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

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

row_label: Glucose-NAD+ / coenzyme Km column

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


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

assay_conditions_summary: 343.15 K; cofactor NADP+

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

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

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

row_label: Glucose-NADP+ / coenzyme Km column


enzyme_display_name: aldose 1-dehydrogenase (NAD(+))

organism: Thermus thermophilus

substrate_name: L-Arabinose

assay_conditions_summary: pH 7.4; 323.15 K; cofactor NAD+

column_label: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates.; row l-Arabinose; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 262, kcat 273.

normalized_value_unit_evidence: Km: 262 mM is already the canonical Km unit; normalized Km = 262.0 mM. kcat: 273 min−1 / 60 = 4.55 s^-1; stated at the export row's stored precision as 4.55 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 4.55 s^-1 / Km 262.0 mM = 0.017366412213740457 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates. row l-Arabinose: Km 262 mM; kcat 273 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: l-Arabinose

enzyme: aldose 1-dehydrogenase (NAD(+))

substrate: L-Arabinose


substrate_name: D-Talose

column_label: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates.; row d-Talose; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 131, kcat 181.

normalized_value_unit_evidence: Km: 131 mM is already the canonical Km unit; normalized Km = 131.0 mM. kcat: 181 min−1 / 60 = 3.0166666666666666 s^-1; stated at the export row's stored precision as 3.0 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 3.0 s^-1 / Km 131.0 mM = 0.022900763358778626 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates. row d-Talose: Km 131 mM; kcat 181 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: d-Talose

substrate: D-Talose


column_label: Table 2: Substrate specificity for non-sugar compounds, row 1-Acenaphthenol: Km=0.14 mM; kcat=26000 min^-1; kcat/Km=1.8 x 10^5 min^-1 mM^-1


column_label: Table 2: Substrate specificity for non-sugar compounds, row 2-Cyclohexen-1-ol: Km=3.7 mM; kcat=210 min^-1; kcat/Km=57 min^-1 mM^-1


column_label: Table 1: Substrate specificity in the oxidation of carbohydrates, row 2-deoxy-D-galactose: Km=33 mM; kcat=768 min^-1; kcat/Km=23 min^-1 mM^-1


column_label: Table 1: Substrate specificity in the oxidation of carbohydrates, row 2-deoxy-D-glucose: Km=300 mM; kcat=416 min^-1; kcat/Km=1.4 min^-1 mM^-1


column_label: Table 1: Substrate specificity in the oxidation of carbohydrates, row 6-deoxy-D-glucose: Km=178 mM; kcat=381 min^-1; kcat/Km=2.1 min^-1 mM^-1


substrate_name: cellobiose

column_label: Table 1: Substrate specificity in the oxidation of carbohydrates, row cellobiose: Km=250 mM; kcat=346 min^-1; kcat/Km=1.4 min^-1 mM^-1

row_label: cellobiose

substrate: cellobiose


substrate_name: cis-benzene dihydrodiol

column_label: Table 2: Substrate specificity for non-sugar compounds, row cis-benzene dihydrodiol: Km=27 mM; kcat=443 min^-1; kcat/Km=16 min^-1 mM^-1

row_label: cis-benzene dihydrodiol

substrate: cis-benzene dihydrodiol


substrate_name: D-galactose

column_label: Table 1: Substrate specificity in the oxidation of carbohydrates, row D-galactose: Km=78 mM; kcat=495 min^-1; kcat/Km=6.4 min^-1 mM^-1

row_label: D-galactose


column_label: Table 1: Substrate specificity in the oxidation of carbohydrates, row D-glucose: Km=580 mM; kcat=231 min^-1; kcat/Km=0.40 min^-1 mM^-1

row_label: D-glucose


assay_conditions_summary: pH 10; cofactor NAD+

column_label: Abstract states Km values were 0.15 mM, 1.4 mM, and 0.7 mM for L-fucose, D-arabinose, and NAD+, respectively.

raw_value_unit_evidence: Km raw_value=1.4 raw_unit=mM

row_label: rabbit liver L-fucose dehydrogenase with D-arabinose

table_label: PubMed abstract PMID 521443


organism: Dickeya chrysanthemi

substrate_name: NADH

substrate: NADH


substrate_name: lactose

column_label: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates.; row Lactose; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 781, kcat 554.

normalized_value_unit_evidence: Km: 781 mM is already the canonical Km unit; normalized Km = 781.0 mM. kcat: 554 min−1 / 60 = 9.233333333333333 s^-1; stated at the export row's stored precision as 9.23 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 9.23 s^-1 / Km 781.0 mM = 0.011818181818181818 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates. row Lactose: Km 781 mM; kcat 554 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: Lactose

substrate: lactose


substrate_name: (R)-indanol

column_label: Table 2 Substrate speciﬁcity for non-sugar compounds.; row R-Indanol; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 1.3, kcat 10.

normalized_value_unit_evidence: Km: 1.3 mM is already the canonical Km unit; normalized Km = 1.3 mM. kcat: 10 min−1 / 60 = 0.16666666666666666 s^-1; stated at the export row's stored precision as 0.17 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 0.17 s^-1 / Km 1.3 mM = 0.13076923076923078 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Substrate speciﬁcity for non-sugar compounds. row R-Indanol: Km 1.3 mM; kcat 10 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: R-Indanol

substrate: (R)-indanol


substrate_name: (R)-tetralol

column_label: Table 2 Substrate speciﬁcity for non-sugar compounds.; row R-Tetralol; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 2.5, kcat 4.5.

normalized_value_unit_evidence: Km: 2.5 mM is already the canonical Km unit; normalized Km = 2.5 mM. kcat: 4.5 min−1 / 60 = 0.075 s^-1; stated at the export row's stored precision as 0.075 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 0.075 s^-1 / Km 2.5 mM = 0.03 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Substrate speciﬁcity for non-sugar compounds. row R-Tetralol: Km 2.5 mM; kcat 4.5 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: R-Tetralol

substrate: (R)-tetralol


substrate_name: (S)-indanol

column_label: Table 2 Substrate speciﬁcity for non-sugar compounds.; row S-Indanol; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 0.65, kcat 8,320.

normalized_value_unit_evidence: Km: 0.65 mM is already the canonical Km unit; normalized Km = 0.65 mM. kcat: 8,320 min−1 / 60 = 138.66666666666666 s^-1; stated at the export row's stored precision as 138.7 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 138.7 s^-1 / Km 0.65 mM = 213.38461538461536 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Substrate speciﬁcity for non-sugar compounds. row S-Indanol: Km 0.65 mM; kcat 8,320 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: S-Indanol

substrate: (S)-indanol


substrate_name: (S)-tetralol

column_label: Table 2 Substrate speciﬁcity for non-sugar compounds.; row S-Tetralol; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 0.17, kcat 9,700.

normalized_value_unit_evidence: Km: 0.17 mM is already the canonical Km unit; normalized Km = 0.17 mM. kcat: 9,700 min−1 / 60 = 161.66666666666666 s^-1; stated at the export row's stored precision as 161.7 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 161.7 s^-1 / Km 0.17 mM = 951.1764705882351 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Substrate speciﬁcity for non-sugar compounds. row S-Tetralol: Km 0.17 mM; kcat 9,700 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: S-Tetralol

substrate: (S)-tetralol


substrate_name: L-Fucose

column_label: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates.; row l-Fucose; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 162, kcat 6.4.

normalized_value_unit_evidence: Km: 162 mM is already the canonical Km unit; normalized Km = 162.0 mM. kcat: 6.4 min−1 / 60 = 0.10666666666666667 s^-1; stated at the export row's stored precision as 0.11 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 0.11 s^-1 / Km 162.0 mM = 0.0006790123456790123 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates. row l-Fucose: Km 162 mM; kcat 6.4 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: l-Fucose

substrate: L-Fucose


substrate_name: D-Glucosamine

column_label: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates.; row d-Glucosamine; column Km (mM); column kcat (min−1 ); column kcat /Km (min−1 /mM); raw cells Km 139, kcat 37.3.

normalized_value_unit_evidence: Km: 139 mM is already the canonical Km unit; normalized Km = 139.0 mM. kcat: 37.3 min−1 / 60 = 0.6216666666666666 s^-1; stated at the export row's stored precision as 0.62 s^-1 (the conversion quotient rounds to the exported value at the precision the export stores, so this is a precision restatement and not a corrected value). kcat/Km: the paper's kcat/Km column prints a coarsely rounded efficiency in min−1/mM, so the ratio is recorded instead as the quotient of this same table row's own two cells: kcat 0.62 s^-1 / Km 139.0 mM = 0.004460431654676259 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 Substrate speciﬁcity in the oxidation of carbohydrates. row d-Glucosamine: Km 139 mM; kcat 37.3 min−1; printed kcat/Km column is a rounded catalytic-efficiency figure and is not used as the kcat/Km source value here.

row_label: d-Glucosamine

substrate: D-Glucosamine


substrate_name: D-Galactosamine

substrate: D-Galactosamine


substrate_name: D-Xylose

substrate: D-Xylose


substrate_name: D-Fucose

substrate: D-Fucose


enzyme_display_name: fructose 5-dehydrogenase (NADP+)

substrate_name: NADPH

enzyme: fructose 5-dehydrogenase (NADP+)

substrate: NADPH


organism: Gluconobacter cerinus


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: 5-Keto-D-fructose 1-phosphate

substrate: 5-Keto-D-fructose 1-phosphate


substrate_name: D-fructose

substrate: D-fructose


organism: Pseudomonas sp.


enzyme_display_name: 3-dehydro-L-gulonate 2-dehydrogenase

organism: Klebsiella aerogenes

assay_conditions_summary: cofactor NADH

enzyme: 3-dehydro-L-gulonate 2-dehydrogenase


organism: Escherichia coli (strain K12)

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

proof_lines: kcat is 3.1 min(-1) for 11-DOC reduction. kcat is 16.6 min(-1) for 11-deoxycortisol (RSS) reduction. kcat is 58.3 min(-1) for D-gluconate oxidation. kcat is 30.7 min(-1) for 5-keto-D-gluconate reduction. kcat is 18.3 min(-1) for 1,2-propane


enzyme_display_name: (R)-aminopropanol dehydrogenase

organism: Escherichia coli

smiles: CC(CN)O

proof_lines:
washed cell suspension
cell free extracts

enzyme: (R)-aminopropanol dehydrogenase


enzyme_display_name: fructuronate reductase

substrate_name: D-tagaturonate

enzyme: fructuronate reductase

substrate: D-tagaturonate


enzyme_display_name: mannitol 2-dehydrogenase (NADP+)

organism: Agaricus bisporus

assay_conditions_summary: pH 7

enzyme: mannitol 2-dehydrogenase (NADP+)


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

organism: Azospirillum brasilense

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

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


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


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

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

enzyme: ketol-acid reductoisomerase (NADP+)


organism: Agaricus campestris


substrate_name: D-mannitol

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

substrate: D-mannitol


organism: Starmerella magnoliae

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: ribose

substrate: ribose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: Unknown

substrate: Unknown


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

proof_lines:
cosubstrate fructose, pH 7.5, 37°C
cosubstrate NADPH, pH 7.5, 37°C


organism: Uromyces viciae-fabae

assay_conditions_summary: pH 10; cofactor NADP+


assay_conditions_summary: pH 5.2; cofactor NADPH


assay_conditions_summary: pH 10


organism: Limosilactobacillus reuteri

assay_conditions_summary: pH 5.4; 310.15 K; cofactor NADPH


assay_conditions_summary: pH 5.4; 310.15 K; cofactor NADH


assay_conditions_summary: pH 6.2; 310.15 K; cofactor NADP+


substrate_name: NAD+

assay_conditions_summary: pH 6.2; 310.15 K; cofactor NAD+

substrate: NAD+


organism: Fusarium graminearum

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines:
cosubstrate mannitol, pH 9.0, 30°C
cosubstrate mannitol, pH 7.0, 30°C


proof_lines:
cosubstrate NADP+, pH 9.0, 30°C
cosubstrate NADP+, pH 7.0, 30°C


organism: Aspergillus parasiticus


substrate_name: D-arabinitol

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

substrate: D-arabinitol


organism: Erwinia sp.

sequence: AEQQNFLSDLTGSFSSPCNENPTVAMMXISYXXQXIWAS

column_label: Table 4 row NADP+ under Km (mM): 0.053 +/- 0.005.

row_label: NADP+


assay_conditions_summary: cofactor NADPH

column_label: Table 4 row NADPH under Km (mM): 0.071 +/- 0.004.

row_label: NADPH


column_label: Table 4 row NADH under Km (mM): 0.32 +/- 0.07.

normalized_value_unit_evidence: Km 0.32 mM

row_label: NADH


assay_conditions_summary: cofactor NAD+

column_label: Table 4 row NAD+ under Km (mM): 1.97 +/- 0.08.

normalized_value_unit_evidence: Km 1.97 mM

row_label: NAD+


assay_conditions_summary: pH 9.5; cofactor NADP+

column_label: Table 4 row D-Fructose under Km (mM): 9.1 +/- 0.7; Vmax 26.5 +/- 0.5 with NADP+ and 23.8 +/- 0.1 with NAD+.

normalized_value_unit_evidence: Km 9.1 mM

row_label: D-Fructose


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 4 row 5-Ketofructose under Km (mM): 12.7 +/- 0.9; Vmax 2900 +/- 300 with NADPH and 2700 +/- 500 with NADH.

normalized_value_unit_evidence: Km 12.7 mM


substrate_name: D-arabinose

assay_conditions_summary: pH 9.5; cofactor NAD+

column_label: Table 4 row D-Arabinose under Km (mM): 140 +/- 10; Vmax 0.36 +/- 0.01 with NAD+.

row_label: D-Arabinose

substrate: D-arabinose


enzyme_display_name: UDP-N-acetylglucosamine 6-dehydrogenase

substrate_name: UDP-N-acetyl-D-glucosamine

enzyme: UDP-N-acetylglucosamine 6-dehydrogenase

substrate: UDP-N-acetyl-D-glucosamine


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


organism: Pseudomonas aeruginosa

substrate_name: UDP-N-acetyl-D-glucosamine; NAD+; H2O

substrate: UDP-N-acetyl-D-glucosamine; NAD+; H2O


organism: Micrococcus luteus


organism: Salmonella enterica subsp. enterica serovar Typhi


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


enzyme_display_name: ribitol-5-phosphate 2-dehydrogenase

organism: Lacticaseibacillus casei

enzyme: ribitol-5-phosphate 2-dehydrogenase


substrate_name: D-ribitol 5-phosphate

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

substrate: D-ribitol 5-phosphate


enzyme_display_name: GDP-mannose 6-dehydrogenase

organism: Saccharina japonica

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

proof_lines:
isoform GMD1, at pH 8.0 and 30°C
isoform GMD2, at pH 8.3 and 20°C

enzyme: GDP-mannose 6-dehydrogenase


substrate_name: GDP-D-mannose

proof_lines:
isoform GMD2, at pH 8.3 and 20°C
isoform GMD1, at pH 8.0 and 30°C

substrate: GDP-D-mannose


organism: Alcaligenes sp.


organism: Penicillium chrysogenum

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+


organism: Gluconobacter oxydans

substrate_name: NADPH

substrate: NADPH


substrate_name: D-fructose


organism: Lactobacillus casei

substrate_name: D-Ribulose 5-phosphate; NADH; H+

substrate: D-Ribulose 5-phosphate; NADH; H+


assay_conditions_summary: pH 10; cofactor NADP+

proof_lines: at pH 10.0, temperature not specified in the publication

substrate: NADP+


assay_conditions_summary: pH 10

proof_lines: at pH 7.0, temperature not specified in the publication


organism: Diplodia viticola Desm.


organism: Lactobacillus intermedius

substrate: D-fructose


organism: Tuber borchii

assay_conditions_summary: pH 9; cofactor NADP+

column_label: Table 2, oxidation section, NADP+ row, Km (mM) column = 0.066 +/- 0.004.

table_label: Table 2


assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 2, reduction section, NADPH row, Km (mM) column = 0.1 +/- 0.006.


column_label: Table 2, reduction section, D-fructose row, Km (mM) column = 47 +/- 5.

normalized_value_unit_evidence: 47 mM

raw_value_unit_evidence: D-fructose Km 47 +/- 5 mM.

row_label: D-fructose


column_label: Table 2, oxidation section, D-mannitol row, Km (mM) column = 600 +/- 35.

raw_value_unit_evidence: D-mannitol Km 600 +/- 35 mM.

row_label: D-mannitol


organism: Escherichia coli (strain K12)


substrate_name: D-gluconate

substrate: D-gluconate


assay_conditions_summary: cofactor NADH


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: UDP-GlcNAc

proof_lines: kcat is 110 min(-1) with UDP-GlcNAc as substrate. kcat is 0.69 min(-1) with UDP-GalNAc as substrate. kcat is 110 min(-1) with NAD(+) as substrate. kcat is 0.71 min(-1) with NADP(+) as substrate (PubMed:18065759). kcat is 5.5 min(-1) with UD

substrate: UDP-GlcNAc


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: Probable NADP-dependent mannitol dehydrogenase

organism: Yarrowia lipolytica (strain CLIB 122 / E 150)

smiles: CCCCCC(C)O

proof_lines: kcat is 3.17 sec(-1) with rac-2-heptanol as substrate and 6.15 sec(-1) for NADP(+). kcat is 5.42 sec(-1) for ribulose.


substrate_name: ribulose

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

enzyme: Probable NADP-dependent mannitol dehydrogenase

substrate: ribulose


organism: Agaricus bisporus

substrate_name: D-mannitol

assay_conditions_summary: pH 9

proof_lines: kcat is 2.20 sec(-1) for mannitol. kcat is 7.31 sec(-1) for fructose.

substrate: D-mannitol


substrate_name: NADP(+) (refolded enzyme)

substrate: NADP(+) (refolded enzyme)


organism: Cladosporium herbarum

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+

proof_lines: plusminus 0.007 mM, pH 7.5, room temperature


assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADPH

proof_lines: plusminus 0.01 mM, pH 7.5, room temperature


proof_lines: plusminus 5 mM, pH 7.5, room temperature


proof_lines: plusminus 20 mM, pH 7.5, room temperature


organism: Salmonella typhi


enzyme_display_name: dTDP-4-dehydrorhamnose reductase

organism: Acanthamoeba polyphaga Mimivirus

enzyme: dTDP-4-dehydrorhamnose reductase


organism: Lactiplantibacillus plantarum

proof_lines:
ribitol-5-phosphate 2-dehydrogenase
Lactiplantibacillus plantarum
NADP+


substrate_name: D-ribulose 5-phosphate

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

proof_lines:
ribitol-5-phosphate 2-dehydrogenase
Lactiplantibacillus plantarum
D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Salmonella typhimurium


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

assay_conditions_summary: cofactor NAD+


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8.5; cofactor NADPH

column_label: The abstract reports apparent Km values of 90 microm for NADPH and 16.9 microm for dTDP-4-keto-6-deoxy-Glc.

raw_value_unit_evidence: Km raw_value=90 microm raw_unit=microM

row_label: Prose segment: NADPH Km

table_label: PubMed PMID 15020741 abstract


raw_value_unit_evidence: Km raw_value=16.9 microm raw_unit=microM

row_label: Prose segment: dTDP-4-keto-6-deoxy-Glc Km


organism: Aneurinibacillus thermoaerophilus

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlD'; substrate row 'NADH'; column 'Km (mM)' = 0.012 +/- 0.0017; column 'kcat (s-1)' = 1.5 +/- 6.6; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.012 mM; the column is already mM, so normalized Km = 0.012 mM. kcat: paper cell 1.5 s-1; the column is already s^(-1), so normalized kcat = 1.5 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 1.5 / 0.012 = 125.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlD', substrate row 'NADH': Km = 0.012 +/- 0.0017 mM; kcat = 1.5 +/- 6.6 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlD', substrate row 'NADH'


enzyme_display_name: NADP-dependent mannitol dehydrogenase

organism: Alternaria alternata

assay_conditions_summary: cofactor NADPH

enzyme: NADP-dependent mannitol dehydrogenase


organism: Davidiella tassiana

substrate_name: NADP(+) (at pH 7.5)

assay_conditions_summary: pH 7.5; buffer pH 7; cofactor NADP+

column_label: Results/Figure 4 text reports Michaelis-Menten constants for d-fructose, d-mannitol, NADPH, and NADP+ as 1.17 M, 0.23 M, 53 microM, and 67 microM, respectively.

raw_value_unit_evidence: Km raw_value=67 +/- 7 microM raw_unit=microM

row_label: Natural C. herbarum MtDH / NADP+ reverse reaction

table_label: JBC full text PMID 16608840 Results / Figure 4 Michaelis-Menten kinetics

substrate: NADP(+) (at pH 7.5)


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: dTDP-6-deoxy-L-mannose (at pH 6.5)

substrate: dTDP-6-deoxy-L-mannose (at pH 6.5)


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Pseudomonas sp. 'mevalonii'

substrate_name: mevalonate

smiles: CC(CCO)(CC(=O)[O-])O

enzyme: hydroxymethylglutaryl-CoA reductase

substrate: mevalonate


organism: Oryza sativa Japonica Group

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Oryza sativa

proof_lines: pH 8.0, 30°C, recombinant enzyme, versus hydroxypyruvate

proof_lines: pH 8.0, 30°C, recombinant enzyme, competitive mode


enzyme_display_name: phosphoglycerate dehydrogenase

organism: Escherichia coli

proof_lines:
apparent
Km at pH 7.5 is lower than at pH 8.8

enzyme: phosphoglycerate dehydrogenase


substrate_name: DL-mevalonate

smiles: CC(CCO)(CC(=O)O)O

substrate: DL-mevalonate


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Streptomyces sp.

substrate_name: coniferyl alcohol

proof_lines:
recombinant enzyme, pH 8.5, 30°C
pH 8.0, 30°C
native enzyme, pH 8.5, 30°C

enzyme: aryl-alcohol dehydrogenase

substrate: coniferyl alcohol


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7; buffer pH 7.0

proof_lines: in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication

proof_lines: in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication


organism: Homo sapiens

proof_lines: pH 7.1, 25°C, wild-type enzyme from fibroblasts

proof_lines: pH 7.1, 25°C, recombinant FLAG-tagged wild-type enzyme from HEK-293 cells


enzyme_display_name: glyoxylate reductase (NADP+)

organism: Zea mays

substrate_name: NADH; Glyoxylate; H+

enzyme: glyoxylate reductase (NADP+)

substrate: NADH; Glyoxylate; H+


enzyme_display_name: malate dehydrogenase (NADP+)

organism: Sorghum bicolor

substrate_name: Oxaloacetate; H+; NADPH

enzyme: malate dehydrogenase (NADP+)

substrate: Oxaloacetate; H+; NADPH


enzyme_display_name: L-threonine 3-dehydrogenase

organism: Capra hircus

substrate_name: NAD+; L-Threonine

enzyme: L-threonine 3-dehydrogenase

substrate: NAD+; L-Threonine


organism: Dictyostelium discoideum

substrate_name: Sepiapterin; NADPH; H+

substrate: Sepiapterin; NADPH; H+


organism: Streptomyces exfoliatus


enzyme_display_name: Aldo-keto reductase family 1 member C4

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

enzyme: Aldo-keto reductase family 1 member C4


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: NADH tested with dihydrotestosterone

substrate: NADH tested with dihydrotestosterone


enzyme_display_name: Aldo-keto reductase family 1 member C3

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

enzyme: Aldo-keto reductase family 1 member C3


enzyme_display_name: Aldo-keto reductase family 1 member C1

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

enzyme: Aldo-keto reductase family 1 member C1


enzyme_display_name: Retinol dehydrogenase 16

substrate_name: CRBP-all-trans-retinol

enzyme: Retinol dehydrogenase 16

substrate: CRBP-all-trans-retinol


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


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

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


organism: Drosophila melanogaster

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


organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


enzyme_display_name: Retinol dehydrogenase 5

organism: Bos taurus

enzyme: Retinol dehydrogenase 5


organism: Mus musculus


organism: Macaca fuscata fuscata

proof_lines: kcat is 4.9 min(-1) for 5-beta-pregnan-20-alpha-ol-3-one as substrate. kcat is 4.9 min(-1) for 3alpha-hydroxy-5alpha-androstan-17-one as substrate. kcat is 23 min(-1) for 5alpha-pregnane-3alpha,21-diol-20-one.


enzyme_display_name: Aldo-keto reductase family 1 member B1

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: Aldo-keto reductase family 1 member B1


enzyme_display_name: Aldo-keto reductase family 1 member B10

substrate_name: GS-acrolein

proof_lines: kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as

enzyme: Aldo-keto reductase family 1 member B10

substrate: GS-acrolein


enzyme_display_name: Aldo-keto reductase family 1 member B15

substrate_name: 3-alpha,17-beta-androstandiol (tested with isoform 1 in the oxidative reaction)

assay_conditions_summary: cofactor CoA

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

enzyme: Aldo-keto reductase family 1 member B15


enzyme_display_name: Aldo-keto reductase family 1 member A1

proof_lines: kcat is 959 min(-1) for S-nitroso-CoA as substrate (PubMed:30538128). kcat is 604 min(-1) for D-glucuronate as substrate (PubMed:30538128). kcat is 306 min(-1) for D,L-glyceraldehyde as substrate (PubMed:30538128). kcat is 948 min(-1) for S

enzyme: Aldo-keto reductase family 1 member A1


enzyme_display_name: Carbonyl reductase [NADPH] 1

organism: Sus scrofa

substrate_name: 9,1 O-phenanthrene-quinone

proof_lines: kcats are 2 min(-1), 285 min(-1), 460 min(-1), 58 min(-1) for prostaglandin E2, menadione, 9,1 O-phenanthrene-quinone and 4-nitrobenzaldehyde as substrates, respectively.

enzyme: Carbonyl reductase [NADPH] 1

substrate: 9,1 O-phenanthrene-quinone


enzyme_display_name: glycerol dehydrogenase (NADP+)

organism: Trichoderma reesei

substrate_name: H+; NADPH; Dihydroxyacetone

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

assay_conditions_summary: cofactor NADP+

enzyme: glycerol dehydrogenase (NADP+)

substrate: H+; NADPH; Dihydroxyacetone


enzyme_display_name: Glycerol dehydrogenase

organism: Escherichia coli (strain K12)

proof_lines: The catalytic efficiency of the reverse reaction (dihydroxyacetone reduction) is more than 100-fold higher than that of the forward direction (glycerol oxidation).

enzyme: Glycerol dehydrogenase


enzyme_display_name: (S,S)-butanediol dehydrogenase

organism: Corynebacterium glutamicum

substrate_name: L-acetoin

proof_lines:
pH 6.0
Dixon plot
pH 8.0, 37°C

enzyme: (S,S)-butanediol dehydrogenase

substrate: L-acetoin


enzyme_display_name: glyoxylate reductase (NADP+)

substrate_name: H+; NADPH; 3-Hydroxypyruvate

enzyme: glyoxylate reductase (NADP+)

substrate: H+; NADPH; 3-Hydroxypyruvate


substrate_name: Glyoxylate; H+; NADH

substrate: Glyoxylate; H+; NADH


organism: Saccharomyces cerevisiae

substrate_name: NADPH; H+; Glyoxylate

substrate: NADPH; H+; Glyoxylate


organism: Escherichia coli

substrate_name: NADPH; Glyoxylate; H+

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

proof_lines: The catalytic efficiency is better for glyoxylate than hydroxypyruvate with NADPH as electron donor.

substrate: NADPH; Glyoxylate; H+


substrate_name: H+; NADPH; Glyoxylate

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: The catalytic efficiency is better for hydroxypyruvate than glyoxylate with NADPH as electron donor.

substrate: H+; NADPH; Glyoxylate


organism: Spinacia oleracea

substrate_name: Glyoxylate; H+; NADPH

substrate: Glyoxylate; H+; NADPH


organism: Arabidopsis thaliana


organism: Thermus thermophilus

substrate_name: NADH

assay_conditions_summary: pH 6.7; cofactor NADH

proof_lines: pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme

proof_lines: with glyoxylate as substrate, pH 6.7, 45°C

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 6.7; cofactor NADPH

substrate: NADPH


substrate_name: glyoxylate

proof_lines: pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme

proof_lines: pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme

substrate: glyoxylate


organism: Vitis vinifera

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: hydroxypyruvate reductase

substrate_name: 3-Hydroxypyruvate; NADH; H+

enzyme: hydroxypyruvate reductase

substrate: 3-Hydroxypyruvate; NADH; H+


substrate_name: NADPH; H+; 3-Hydroxypyruvate

substrate: NADPH; H+; 3-Hydroxypyruvate


substrate_name: 3-Hydroxypyruvate; NADPH; H+

substrate: 3-Hydroxypyruvate; NADPH; H+


organism: Hyphomicrobium methylovorum

substrate_name: NADH; 3-Hydroxypyruvate; H+

substrate: NADH; 3-Hydroxypyruvate; H+


organism: Blautia hydrogenotrophica

substrate_name: NAD+; Glycerate

substrate: NAD+; Glycerate


enzyme_display_name: malate dehydrogenase (NADP+)

organism: Methanocaldococcus jannaschii

substrate_name: NADPH; Oxaloacetate

enzyme: malate dehydrogenase (NADP+)

substrate: NADPH; Oxaloacetate


organism: Methanothermus fervidus


organism: Sorghum bicolor

substrate_name: Oxaloacetate; NADPH; H+

substrate: Oxaloacetate; NADPH; H+


organism: Pisum sativum

substrate_name: H+; NADPH; Oxaloacetate

substrate: H+; NADPH; Oxaloacetate


organism: Zea mays

substrate_name: NADPH; Oxaloacetate; H+

substrate: NADPH; Oxaloacetate; H+


substrate_name: NADP+; L-Malate

substrate: NADP+; L-Malate


organism: Glycine max


substrate_name: D-Malate; NAD+

substrate: D-Malate; NAD+


enzyme_display_name: Tartrate dehydrogenase/decarboxylase

organism: Pseudomonas putida

substrate_name: NAD(+) (for (+)-tartrate oxidation)

enzyme: Tartrate dehydrogenase/decarboxylase

substrate: NAD(+) (for (+)-tartrate oxidation)


enzyme_display_name: 3-isopropylmalate dehydrogenase

substrate_name: 3-Isopropylmalate; NAD+

enzyme: 3-isopropylmalate dehydrogenase

substrate: 3-Isopropylmalate; NAD+


organism: Sulfurisphaera tokodaii

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

assay_conditions_summary: pH 8

proof_lines:
pH 8.0
Raw SKiD Env: Temp=-----, pH=8

source_databases_merged: brenda skid


enzyme_display_name: 3-isopropylmalate dehydrogenase 2, chloroplastic

proof_lines: kcat is 373 min(-1) with 3-isopropylmalate as substrate (at pH 7.5) (PubMed:20840499, PubMed:21697089). kcat is 274 min(-1) with 3-isopropylmalate as substrate (at pH 7.5 and 25 degrees Celsius) (PubMed:27137927). kcat is 1 min(-1) with 3-(


enzyme_display_name: 3-isopropylmalate dehydrogenase 1, chloroplastic

proof_lines: kcat is 37 min(-1) with 3-isopropylmalate as substrate (PubMed:20840499, PubMed:21697089). kcat is 51 min(-1) with 3-(2'-methylthio)ethylmalate as substrate (PubMed:21697089).


enzyme_display_name: 3-isopropylmalate dehydrogenase 3, chloroplastic

proof_lines: kcat is 543 min(-1) with 3-isopropylmalate as substrate (PubMed:20840499, PubMed:21697089). kcat is 1 min(-1) with 3-(2'-methylthio)ethylmalate as substrate (PubMed:21697089).


enzyme_display_name: ketol-acid reductoisomerase

substrate_name: H+; 3-Hydroxypyruvate; NADPH

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: kcat is 7.2 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 3.1 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 0.11 min(-1) for reductoisomerase activity with

enzyme: ketol-acid reductoisomerase

substrate: H+; 3-Hydroxypyruvate; NADPH


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

organism: Corynebacterium glutamicum

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

enzyme: ketol-acid reductoisomerase (NADP+)


organism: Streptomyces viridifaciens

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


organism: Streptomyces avermitilis


organism: Streptomyces ambofaciens


organism: Spinacia oleracea

assay_conditions_summary: pH 8.2; 303.15 K; cofactor NADPH

proof_lines: pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate

proof_lines: pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-aceto-2-hydroxybutanoate as fixed substrate

proof_lines: pH 8.2, 30°C, (2S)-2-acetolactate as variable substrate, 0.250 mM NADPH as fixed substrate


enzyme_display_name: Ketol-acid reductoisomerase (NADP(+))

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: kcat is 12.5 sec(-1) for reductoisomerase activity with HP as substrate. kcat is 1.4 sec(-1) for reductoisomerase activity with S2AL as substrate.

enzyme: Ketol-acid reductoisomerase (NADP(+))


enzyme_display_name: homoisocitrate dehydrogenase

organism: Thermus thermophilus

substrate_name: Homoisocitrate; NAD+

enzyme: homoisocitrate dehydrogenase

substrate: Homoisocitrate; NAD+


organism: Saccharomyces cerevisiae

substrate_name: (2R,3S)-3-(4-pentenyl)malic acid

proof_lines: oxidate decarboxylation of homoisocitrate

substrate: (2R,3S)-3-(4-pentenyl)malic acid


enzyme_display_name: Homoisocitrate dehydrogenase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

enzyme: Homoisocitrate dehydrogenase


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Pseudomonas mevalonii

substrate_name: NAD+; Coenzyme A; Mevalonate

enzyme: hydroxymethylglutaryl-CoA reductase

substrate: NAD+; Coenzyme A; Mevalonate


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Lactobacillus plantarum

substrate_name: Benzyl alcohol; NAD+

enzyme: aryl-alcohol dehydrogenase

substrate: Benzyl alcohol; NAD+


enzyme_display_name: aryl-alcohol dehydrogenase (NADP+)

organism: Phanerodontia chrysosporium

substrate_name: Unknown

enzyme: aryl-alcohol dehydrogenase (NADP+)

substrate: Unknown


enzyme_display_name: aryl-alcohol dehydrogenase (NADP(+))

organism: Ralstonia sp.

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N15G/G37D/R38V/R39S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.3; 303.15 K; cofactor NADP+

enzyme: aryl-alcohol dehydrogenase (NADP(+))

substrate: NADP+


enzyme_display_name: tartrate dehydrogenase

organism: Sus scrofa

substrate_name: meso-Tartrate; NAD+

enzyme: tartrate dehydrogenase

substrate: meso-Tartrate; NAD+


substrate_name: NAD+; meso-Tartrate

substrate: NAD+; meso-Tartrate


substrate_name: isopropylmalate

substrate: isopropylmalate


organism: Escherichia coli

substrate_name: sn-glycerol 3-phosphate

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

substrate: sn-glycerol 3-phosphate


proof_lines: pH 7.4, 23°C, wild-type and feedback-resistant mutant enzyme

proof_lines: pH 7.4, 23°C, wild-type enzyme and feedback-resistant mutant enzyme


substrate_name: NAD(P)+

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: pH 7.4, 23°C, feedback-resistant mutant enzyme

substrate: NAD(P)+


organism: Escherichia coli (strain K12)

proof_lines: Essentially identical kinetic constants are found when NADH and NAD(+) are substituted for NADPH and NADP(+), respectively.


enzyme_display_name: phosphoglycerate dehydrogenase

substrate_name: 3-Phospho-D-glycerate; NAD+

proof_lines: kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25

enzyme: phosphoglycerate dehydrogenase

substrate: 3-Phospho-D-glycerate; NAD+


organism: Arabidopsis thaliana

substrate_name: H+; 3-Phosphohydroxypyruvate; NADH

substrate: H+; 3-Phosphohydroxypyruvate; NADH


organism: Homo sapiens

substrate_name: NADH; H+; 3-Phosphohydroxypyruvate

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

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: kcat is 4.5 min(-1) for 3-phosphoglycerate oxidation. kcat is 10.6 min(-1) for oxaloacetate reduction. kcat is 4.7 min(-1) for 2-oxoglutarate reduction.

source_databases_merged: sabio_rk skid uniprot

substrate: NADH; H+; 3-Phosphohydroxypyruvate


substrate_name: NAD+; 3-Phospho-D-glycerate

assay_conditions_summary: cofactor NAD+

substrate: NAD+; 3-Phospho-D-glycerate


assay_conditions_summary: pH 7.1; cofactor NAD+


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7; buffer 50 mM MOPS

proof_lines: in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication

proof_lines: in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D463A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


organism: Sulfurisphaera tokodaii

assay_conditions_summary: cofactor NADPH

proof_lines: value of phosphate against 3-phosphohydroxypyruvate


substrate_name: Acetoacetyl-CoA; H+; NADPH

substrate: Acetoacetyl-CoA; H+; NADPH


organism: Persea americana

substrate_name: acetoacetyl-[acyl-carrier protein]

substrate: acetoacetyl-[acyl-carrier protein]


enzyme_display_name: Fatty acid synthase

organism: Rattus norvegicus

enzyme: Fatty acid synthase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: beta-ketododecanoyl-CoA (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 4.3 sec(-1) with beta-ketododecanoyl-CoA as substrate. kcat is 3.5 sec(-1) with beta-ketooctanoyl-CoA as substrate. kcat is 1.9 sec(-1) with acetoacetyl-CoA as substrate. kcat is 2.6 sec(-1) with NADPH as substrate (PubMed:11932442)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: beta-keto-octanoyl-CoA

proof_lines: kcat is 1.14 sec(-1) with acetoacetyl-CoA as substrate. kcat is 5.72 sec(-1) with beta-keto-octanoyl-CoA as substrate.

substrate: beta-keto-octanoyl-CoA


enzyme_display_name: acylglycerone-phosphate reductase

organism: Mus musculus

substrate_name: 1-O-Hexadecyl glycerone phosphate; NADPH; H+

smiles: CCCCCCCCCCCCCCCCOCC(=O)COP(O)(O)=O

enzyme: acylglycerone-phosphate reductase


substrate_name: NADPH; H+; 1-O-Hexadecyl glycerone phosphate


organism: Saccharomyces cerevisiae

substrate_name: 1-O-Hexadecyl glycerone phosphate; NADPH


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: C18-3-oxosphinganine (at pH 6.9)

proof_lines: kcat is 64 min(-1) with C18-3-oxosphinganine as substrate (PubMed:16431155). kcat is 19 min(-1) with C12-3-oxosphinganine as substrate (PubMed:16431155). kcat is 13 min(-1) with C11-3-oxosphinganine as substrate (PubMed:16431155). kcat is 5

substrate: C18-3-oxosphinganine (at pH 6.9)


enzyme_display_name: L-threonine 3-dehydrogenase

substrate_name: NAD+; L-Threonine

enzyme: L-threonine 3-dehydrogenase

substrate: NAD+; L-Threonine


organism: Flavobacterium frigidimaris

substrate_name: L-Threonine; NAD+

substrate: L-Threonine; NAD+


organism: Pyrococcus horikoshii


organism: Cytophaga sp.

substrate_name: Unknown

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

proof_lines:
substrate NAD+, pH 9.0, 30°C
substrate L-threonine, pH 9.0, 30°C

substrate: Unknown


substrate_name: L-threonine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R180K to reconstruct the assayed variant sequence.

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

substrate: L-threonine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T237A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M333A to reconstruct the assayed variant sequence.


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)


enzyme_display_name: Dehydrogenase/reductase SDR family member 6

assay_conditions_summary: cofactor NADH

proof_lines: kcat is 19 sec(-1) for the NADH-dependent reduction of 4-oxo-L-proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of (R)-3-hydroxybutanoate.


proof_lines: kcat is 14 sec(-1) for the NADH-dependent reduction of 4-oxo-L-proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of (R)-3-hydroxybutanoate.

enzyme: Dehydrogenase/reductase SDR family member 6


enzyme_display_name: retinol dehydrogenase

substrate_name: NADPH; H+; all-trans-Retinal

assay_conditions_summary: pH 7.4; cofactor NADP+

column_label: PMID 14674758 Table 2, Kinetic Constants of the Membrane-Bound Wild-Type RalR1 and Purified RalR1-His6; row all-trans-retinal determined with NADPH; purified RalR1-His6 columns apparent Km=0.12 +/- 0.1 uM and apparent Vmax=506 +/- 13 nmol/min/mg. Results prose converts Vmax with a 35.4 kDa subunit mass to kcat=18 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1; km normalized_value=0.00012 normalized_unit=mM; vmax normalized_value=0.000008433333333333333 normalized_unit=mol*s^-1*g^-1.

raw_value_unit_evidence: Table 2 purified RalR1-His6 row all-trans-retinal with NADPH: apparent Km 0.12 +/- 0.1 uM; apparent Vmax 506 +/- 13 nmol/min/mg. Results prose: kcat 18 min^-1.

row_label: all-trans-retinal determined with NADPH / purified RalR1-His6

table_label: Table 2. Kinetic Constants of the Membrane-Bound Wild-Type RalR1 and Purified RalR1-His6

enzyme: retinol dehydrogenase

substrate: NADPH; H+; all-trans-Retinal


assay_conditions_summary: cofactor NADP+


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

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


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: NADH tested with dihydrotestosterone

substrate: NADH tested with dihydrotestosterone


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH7

substrate_name: 12-OH-dodecanoic acid (with 0.1 M sodium phosphate at pH 7.5)

smiles: OCCCCCCCCCCCC(=O)O

assay_conditions_summary: pH 7.5; buffer only


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase 13

enzyme: 17-beta-hydroxysteroid dehydrogenase 13


proof_lines: Vmax was measured using transfected cell lysates.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6