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Literature summary for 1.1.1.307 extracted from

  • Petschacher, B.; Leitgeb, S.; Kavanagh, K.L.; Wilson, D.K.; Nidetzky, B.
    The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography (2005), Biochem. J., 385, 75-83 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
structures of enzyme bound to NADP+ and NAD+ show two different protein conformations capable of accommodating the presence or absence of the coenzyme 2'-phosphate group Yamadazyma tenuis

Protein Variants

Protein Variants Comment Organism
K274G mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity Yamadazyma tenuis
K274M mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity Yamadazyma tenuis
K274R mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity Yamadazyma tenuis
K274R/N276D mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity. Mutant exhibits a 5fold preference for NADH over NADPH Yamadazyma tenuis
N276D mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity Yamadazyma tenuis
R280H mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity Yamadazyma tenuis
S275A mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity Yamadazyma tenuis

Organism

Organism UniProt Comment Textmining
Yamadazyma tenuis O74237
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NADH + H+
-
 Yamadazyma tenuis xylitol + NAD+
-
 ?
D-xylose + NADPH + H+
-
 Yamadazyma tenuis xylitol + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
AKR2B5
-
 Yamadazyma tenuis
XYL1
-
 Yamadazyma tenuis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3 6 NADPH mutant K274M, pH 7, 25°C Yamadazyma tenuis
8
-
 NADH mutant K274R, pH 7, 25°C Yamadazyma tenuis
10
-
 NADPH mutant K274G, pH 7, 25°C Yamadazyma tenuis
11
-
 NADH wild-type, pH 7, 25°C Yamadazyma tenuis
12
-
 NADH mutant K274R/N276D, pH 7, 25°C Yamadazyma tenuis
13
-
 NADPH wild-type, pH 7, 25°C Yamadazyma tenuis
14
-
 NADH mutant N276D, pH 7, 25°C Yamadazyma tenuis
15
-
 NADH mutant K274G, pH 7, 25°C Yamadazyma tenuis
15
-
 NADPH mutant R280H , pH 7, 25°C Yamadazyma tenuis
19
-
 NADH mutant K274M, pH 7, 25°C Yamadazyma tenuis
21
-
 NADH mutant R280H , pH 7, 25°C Yamadazyma tenuis
24
-
 NADH mutant S275A, pH 7, 25°C Yamadazyma tenuis
26
-
 NADPH mutant K274R, pH 7, 25°C Yamadazyma tenuis
29
-
 NADPH mutant S275A, pH 7, 25°C Yamadazyma tenuis
30
-
 NADPH mutant K274R/N276D, pH 7, 25°C Yamadazyma tenuis
37
-
 NADPH mutant N276D, pH 7, 25°C Yamadazyma tenuis

Cofactor

Cofactor Comment Organism Structure
NADH NADPH is preferred approx. 33fold over NADH Yamadazyma tenuis
NADPH NADPH is preferred approx. 33fold over NADH Yamadazyma tenuis