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Literature summary extracted from

  • Nidetzky, B.; Mayr, P.; Neuhauser, W.; Puchberger, M.
    Structural and functional properties of alsode xylose reductase from the D-xylose-metabolizing Candida tenuis (2001), Chem. Biol. Interact., 130-132, 583-595.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.1.21 needs Tween for stability during purification Yamadazyma tenuis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.21 pyridoxal 5'-phosphate inhibits cofactor binding Yamadazyma tenuis
1.1.1.21 zopolrestat
-
Yamadazyma tenuis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.21 2
-
DL-glyceraldehyde
-
Yamadazyma tenuis
1.1.1.21 6.3
-
methylglyoxal
-
Yamadazyma tenuis
1.1.1.21 13
-
acrolein
-
Yamadazyma tenuis
1.1.1.21 76
-
D-xylose
-
Yamadazyma tenuis
1.1.1.21 228
-
D-galactose
-
Yamadazyma tenuis
1.1.1.21 365
-
propanal
-
Yamadazyma tenuis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.21 36000
-
2 * 36000, SDS-PAGE Yamadazyma tenuis
1.1.1.21 80000
-
gel filtration Yamadazyma tenuis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.21 Yamadazyma tenuis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.21 alditol + NAD(P)+ = aldose + NAD(P)H + H+ reaction mechanism Yamadazyma tenuis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.21 2-D-deoxy-2-fluoro-galactose + NADPH
-
Yamadazyma tenuis ?
-
r
1.1.1.21 2-D-deoxygalactose + NADPH
-
Yamadazyma tenuis ?
-
r
1.1.1.21 2-deoxy-2-fluoro-galactose + NADPH + H+
-
Yamadazyma tenuis ?
-
r
1.1.1.21 acrolein + NADPH
-
Yamadazyma tenuis 2-propen-1-ol + NADP+
-
?
1.1.1.21 alditol + NAD(P)+
-
Yamadazyma tenuis aldose + NAD(P)H
-
r
1.1.1.21 aldose + NAD(P)H wide specificity Yamadazyma tenuis alditol + NAD(P)+
-
r
1.1.1.21 D-galactose + NADPH + H+
-
Yamadazyma tenuis ?
-
r
1.1.1.21 D-xylose + NAD(P)H
-
Yamadazyma tenuis xylitol + NAD(P)+
-
r
1.1.1.21 DL-glyceraldehyde + NAD(P)H
-
Yamadazyma tenuis glycerol + NAD(P)+
-
r
1.1.1.21 methylglyoxal + NADPH
-
Yamadazyma tenuis ?
-
?
1.1.1.21 pentose + NADPH
-
Yamadazyma tenuis pentitol + NADP+
-
r
1.1.1.21 propanal + NADPH + H+
-
Yamadazyma tenuis n-propanol + NADP+
-
r
1.1.1.21 xylitol + NAD(P)+
-
Yamadazyma tenuis D-xylose + NAD(P)H + H+
-
r

Subunits

EC Number Subunits Comment Organism
1.1.1.21 dimer 2 * 36000, SDS-PAGE Yamadazyma tenuis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.21 0.183
-
2-deoxy-2-fluoro-galactose
-
Yamadazyma tenuis
1.1.1.21 0.283
-
D-xylose
-
Yamadazyma tenuis
1.1.1.21 1.1
-
D-galactose
-
Yamadazyma tenuis
1.1.1.21 2.4
-
acrolein
-
Yamadazyma tenuis
1.1.1.21 13
-
propanal
-
Yamadazyma tenuis
1.1.1.21 155
-
DL-glyceraldehyde
-
Yamadazyma tenuis
1.1.1.21 266
-
methylglyoxal
-
Yamadazyma tenuis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.21 NADH used in vivo Yamadazyma tenuis
1.1.1.21 NADPH NADPH-specific, pro-4R hydrogen is transferred from the nicotinamide ring of the coenzyme to the substrate Yamadazyma tenuis