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Literature summary extracted from

  • Carbone, V.; Sumii, R.; Ishikura, S.; Asada, Y.; Hara, A.; El-Kabbani, O.
    Structure of monkey dimeric dihydrodiol dehydrogenase in complex with isoascorbic acid (2008), Acta Crystallogr. Sect. D, 64, 532-542.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.179 wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3) Macaca fascicularis
1.3.1.20 expressed in Escherichia coli BL21 (DE3) cells Macaca fuscata
1.3.1.20 wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3) Macaca fascicularis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.179 crystals are obtained at 19.9°C in a culture plate via the vapour-diffusion method, crystal structure of dimeric D-xylose dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution Macaca fascicularis
1.3.1.20 crystals are obtained at 19.9°C in a culture plate via the vapour-diffusion method, crystal structure of dimeric dihydrodiol dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution Macaca fascicularis
1.3.1.20 in complex with isoascorbic acid, vapour diffusion method with 2 M ammonium sulfate, 0.1 M sodium citrate buffer pH 5.0, at 20°C Macaca fuscata

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.179 A36D site-directed mutagenesis Macaca fascicularis
1.1.1.179 D280A by site-directed mutagenesis Macaca fascicularis
1.1.1.179 F154A by site-directed mutagenesis Macaca fascicularis
1.1.1.179 F279A by site-directed mutagenesis Macaca fascicularis
1.1.1.179 H76Q by site-directed mutagenesis Macaca fascicularis
1.1.1.179 H79Q by site-directed mutagenesis Macaca fascicularis
1.1.1.179 K97M by site-directed mutagenesis Macaca fascicularis
1.1.1.179 K97R by site-directed mutagenesis Macaca fascicularis
1.1.1.179 R37A site-directed mutagenesis Macaca fascicularis
1.1.1.179 R37D site-directed mutagenesis Macaca fascicularis
1.1.1.179 R41A by site-directed mutagenesis Macaca fascicularis
1.1.1.179 R41D by site-directed mutagenesis Macaca fascicularis
1.1.1.179 W125Y by site-directed mutagenesis Macaca fascicularis
1.1.1.179 W254A by site-directed mutagenesis Macaca fascicularis
1.1.1.179 W254Y by site-directed mutagenesis Macaca fascicularis
1.3.1.20 A36D shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 A36D production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 D280A shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 D280A production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 F154A shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 F154A production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 F279A shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 F279A production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 H76Q shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 H76Q production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 H79Q shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 H79Q production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 K97M shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 K97M production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 K97R shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 K97R production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 R37A shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 R37A production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 R37D shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 R37D production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 R41A shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 R41A production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 R41D shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 R41D production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 W125Y shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 W125Y production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 W254A shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 W254A production by site-directed mutagenesis Macaca fascicularis
1.3.1.20 W254Y shows a decreased kcat value compared to the wild type enzyme Macaca fuscata
1.3.1.20 W254Y production by site-directed mutagenesis Macaca fascicularis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.179 4-hydroxyacetophenone
-
 Macaca fascicularis
1.1.1.179 isoascorbic acid competitive inhibitor Macaca fascicularis
1.3.1.20 4-hydroxyacetophenone
-
 Macaca fascicularis
1.3.1.20 4-hydroxyacetophenone
-
 Macaca fuscata
1.3.1.20 isoascorbic acid competitive inhibitor Macaca fascicularis
1.3.1.20 isoascorbic acid
-
 Macaca fuscata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.179 2.4
-
 D-xylose oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 2.9
-
 D-xylose oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 3.4
-
 D-xylose oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 4.4
-
 D-xylose oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 8 9 D-xylose oxidation reaction of mutant F279A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 11
-
 D-xylose oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 14
-
 D-xylose oxidation reaction of mutant W254Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 15
-
 D-xylose oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 36
-
 D-xylose oxidation reaction of mutant F154A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 41
-
 D-xylose oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 65
-
 D-xylose oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 67
-
 D-xylose oxidation reaction of mutant W125Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.1.1.179 90
-
 D-xylose oxidation reaction of mutant W254A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose Macaca fascicularis
1.3.1.20 0.1
-
 Camphorquinone wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 0.84
-
 Camphorquinone mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 0.84
-
 Camphorquinone reduction reaction of mutant W254Y, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 1.5
-
 Camphorquinone mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 1.5
-
 Camphorquinone reduction reaction of mutant F154A, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 2.4
-
 Camphorquinone reduction reaction of mutant R41D, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 2.6
-
 Camphorquinone reduction reaction of mutant F279A, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 3.1
-
 Camphorquinone reduction reaction of mutant R37D, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 3.6
-
 Camphorquinone mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 3.6
-
 Camphorquinone reduction reaction of mutant W254A, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 4.4
-
 D-xylose wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 5.1
-
 Camphorquinone reduction reaction of mutant H76Q, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 5.2
-
 Camphorquinone reduction reaction of mutant R37A, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 8.1
-
 Camphorquinone reduction reaction of mutant A36D, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 11
-
 Camphorquinone reduction reaction of wild type enzyme, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 12
-
 Camphorquinone reduction reaction of mutant H79Q, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 13
-
 Camphorquinone mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 13
-
 Camphorquinone reduction reaction of mutant W125Y, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 14
-
 D-xylose mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 17
-
 Camphorquinone reduction reaction of mutant K97M, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 20
-
 D-xylose mutant enzyme F279A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 21
-
 Camphorquinone reduction reaction of mutant K79R, using 0.1 mM NADPH as coenzyme Macaca fascicularis
1.3.1.20 26
-
 Camphorquinone mutant enzyme F279A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 36
-
 D-xylose mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 67
-
 D-xylose mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 90
-
 D-xylose mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.179 D-xylose + NADP+ Macaca fascicularis enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase D-xylono-1,5-lactone + NADPH + H+
-
 ?
1.1.1.179 additional information Macaca fascicularis D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation ?
-
 ?
1.3.1.20 camphorquinone + NADPH + H+ Macaca fascicularis enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase ?
-
 ?
1.3.1.20 additional information Macaca fascicularis dihydrodiol dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.179 Macaca fascicularis Q9TQS6
-
-
1.3.1.20 Macaca fascicularis Q9TQS6
-
-
1.3.1.20 Macaca fuscata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.179 the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells Macaca fascicularis
1.3.1.20
-
 Macaca fuscata
1.3.1.20 the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells Macaca fascicularis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.179 D-xylose + NADP+ enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase Macaca fascicularis D-xylono-1,5-lactone + NADPH + H+
-
 ?
1.1.1.179 additional information D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation Macaca fascicularis ?
-
 ?
1.3.1.20 camphorquinone + NAD(P)H
-
 Macaca fuscata (1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
 ?
1.3.1.20 camphorquinone + NADPH + H+ enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase Macaca fascicularis ?
-
 ?
1.3.1.20 D-xylose + NADP+
-
 Macaca fuscata D-xylono-1,5-lactone + NADPH + H+
-
 ?
1.3.1.20 additional information dihydrodiol dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation Macaca fascicularis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.179 dimer
-
 Macaca fascicularis
1.3.1.20 dimer
-
 Macaca fascicularis
1.3.1.20 dimer x-ray crystallography Macaca fuscata

Synonyms

EC Number Synonyms Comment Organism
1.1.1.179 NADP+-dependent D-xylose dehydrogenase
-
 Macaca fascicularis
1.3.1.20 dihydrodiol dehydrogenase
-
 Macaca fuscata
1.3.1.20 dihydrodiol dehydrogenase
-
 Macaca fascicularis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.179 0.4
-
 D-xylose oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.1.1.179 0.45
-
 D-xylose oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.1.1.179 0.5
-
 D-xylose oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.1.1.179 0.9
-
 D-xylose oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.1.1.179 1
-
 D-xylose oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.1.1.179 1.2
-
 D-xylose oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.1.1.179 1.7
-
 D-xylose oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.1.1.179 2.6
-
 D-xylose oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose Macaca fascicularis
1.3.1.20 0.004
-
 Camphorquinone reduction reaction of mutant K79R, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 0.004
-
 Camphorquinone reduction reaction of mutant K97M, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 0.02
-
 Camphorquinone reduction oxidation reaction of mutant A36D, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 0.05
-
 Camphorquinone reduction oxidation reaction of mutante R37D, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 0.6
-
 Camphorquinone reduction reaction of mutant H79Q, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 0.9
-
 Camphorquinone oxidation reaction of mutant R41D, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 2.1
-
 Camphorquinone reduction reaction of mutant R37A, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 2.6
-
 D-xylose wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 3.6
-
 Camphorquinone reduction reaction of mutant H76Q, 0.1 mM NADPH Macaca fascicularis
1.3.1.20 20
-
 Camphorquinone wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata
1.3.1.20 20
-
 Camphorquinone reduction reaction of wild type enzyme, 0.1 mM NADPH Macaca fascicularis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.179 7.5
-
 assay at Macaca fascicularis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.179 NADP+
-
 Macaca fascicularis
1.3.1.20 NAD(P)H high affinity for NADP(H) Macaca fuscata
1.3.1.20 NADP+
-
 Macaca fascicularis
1.3.1.20 NADPH
-
 Macaca fascicularis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.3.1.20 0.00097
-
 wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata 4-hydroxyacetophenone
1.3.1.20 0.00097
-
 determined in the camphorquinone reduction, inhibitor is uncompetitive with respect to camphorquinone Macaca fascicularis 4-hydroxyacetophenone
1.3.1.20 0.006
-
 mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata 4-hydroxyacetophenone
1.3.1.20 0.006
-
 mutant W254Y Macaca fascicularis 4-hydroxyacetophenone
1.3.1.20 0.037
-
 wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata isoascorbic acid
1.3.1.20 0.038
-
 mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata isoascorbic acid
1.3.1.20 0.038
-
 determined in the camphorquinone reduction, inhibitor is uncompetitive with respect to camphorquinone Macaca fascicularis isoascorbic acid
1.3.1.20 0.038
-
 mutant W254Y Macaca fascicularis isoascorbic acid
1.3.1.20 0.066
-
 mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata isoascorbic acid
1.3.1.20 0.066
-
 mutant W254A Macaca fascicularis isoascorbic acid
1.3.1.20 0.075
-
 mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata 4-hydroxyacetophenone
1.3.1.20 0.075
-
 rmutant F279A Macaca fascicularis 4-hydroxyacetophenone
1.3.1.20 0.078
-
 mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata 4-hydroxyacetophenone
1.3.1.20 0.078
-
 mutant F154A Macaca fascicularis 4-hydroxyacetophenone
1.3.1.20 0.083
-
 mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata 4-hydroxyacetophenone
1.3.1.20 0.083
-
 mutant W254A Macaca fascicularis 4-hydroxyacetophenone
1.3.1.20 0.136
-
 mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata 4-hydroxyacetophenone
1.3.1.20 0.136
-
 mutant W125Y Macaca fascicularis 4-hydroxyacetophenone
1.3.1.20 0.288
-
 mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata isoascorbic acid
1.3.1.20 0.288
-
 mutant F154A Macaca fascicularis isoascorbic acid
1.3.1.20 3.94
-
 mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata isoascorbic acid
1.3.1.20 3.94
-
 mutant F279A Macaca fascicularis isoascorbic acid
1.3.1.20 4.176
-
 mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C Macaca fuscata isoascorbic acid
1.3.1.20 4.176
-
 mutant W125Y Macaca fascicularis isoascorbic acid