Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.430 extracted from

  • Vogl, M.; Brecker, L.
    Substrate binding to Candida tenuis xylose reductase during catalysis (2013), RSC Adv., 3, 25997-26004.
No PubMed abstract available
Search for more literature for 1.1.1.430

Organism

Organism UniProt Comment Textmining
Yamadazyma tenuis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,4'-dichloroacetophenone + NADH + H+ binding and transformation of unnatural 2,4-dichloroacetophenone is not as for good as natural substrates, although it is reduced with very high catalytic efficiency Yamadazyma tenuis ? + NAD+
-
 ?
D-glucose + NADPH + H+
-
 Yamadazyma tenuis ? + NADP+
-
 ?
D-xylose + NADH + H+
-
 Yamadazyma tenuis xylitol + NAD+
-
 ?
additional information substrates preferentially bind as alpha-anomers of the pyranose forms. The alpha-anomers are transformed faster, predominately leading to saturation transfer difference effects in the formed products, and can be better docked into the active site than the beta-anomer. The reduction is initiated by alpha-xylopyranose ring opening prior to hydride transfer from NADH Yamadazyma tenuis ?
-
 ?