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NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme.
Biochem J. 1997 Sep 15; 326 (Pt 3):683-92.BJ

Abstract

During growth on d-xylose the yeast Candida tenuis produces one aldose reductase that is active with both NADPH and NADH as coenzyme. This enzyme has been isolated by dye ligand and anion-exchange chromatography in yields of 76%. Aldose reductase consists ofa single 43 kDa polypeptide with an isoelectric point of 4.70. Initial velocity, product inhibition and binding studies are consistent with a compulsory-ordered, ternary-complex mechanism with coenzyme binding first and leaving last. The catalytic efficiency (kcat/Km) in d-xylose reduction at pH 7 is more than 60-fold higher than that in xylitol oxidation and reflects significant differences in the corresponding catalytic centre activities as well as apparent substrate-binding constants. The enzyme prefers NADP(H) approx. 2-fold to NAD(H), which is largely due to better apparent binding of the phosphorylated form of the coenzyme. NADP+ is a potent competitive inhibitor of the NADH-linked aldehyde reduction (Ki 1.5 microM), whereas NAD+ is not. Unlike mammalian aldose reductase, the enzyme from C. tenuis is not subject to oxidation-induced activation. Evidence of an essential lysine residue located in or near the coenzyme binding site has been obtained from chemical modification of aldose reductase with pyridoxal 5'-phosphate. The results are discussed in the context of a comparison of the enzymic properties of yeast and mammalian aldose reductase.

Authors+Show Affiliations

Division of Biochemical Engineering, Institute of Food Technology, Universität für Bodenkultur Wien, Muthgasse 18, A-1190 Vienna, Austria.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9307017

Citation

Neuhauser, W, et al. "NAD(P)H-dependent Aldose Reductase From the Xylose-assimilating Yeast Candida Tenuis. Isolation, Characterization and Biochemical Properties of the Enzyme." The Biochemical Journal, vol. 326 (Pt 3), 1997, pp. 683-92.
Neuhauser W, Haltrich D, Kulbe KD, et al. NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. Biochem J. 1997;326 (Pt 3):683-92.
Neuhauser, W., Haltrich, D., Kulbe, K. D., & Nidetzky, B. (1997). NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. The Biochemical Journal, 326 (Pt 3), 683-92.
Neuhauser W, et al. NAD(P)H-dependent Aldose Reductase From the Xylose-assimilating Yeast Candida Tenuis. Isolation, Characterization and Biochemical Properties of the Enzyme. Biochem J. 1997 Sep 15;326 (Pt 3):683-92. PubMed PMID: 9307017.
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TY - JOUR T1 - NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. AU - Neuhauser,W, AU - Haltrich,D, AU - Kulbe,K D, AU - Nidetzky,B, PY - 1997/10/23/pubmed PY - 1997/10/23/medline PY - 1997/10/23/entrez SP - 683 EP - 92 JF - The Biochemical journal JO - Biochem J VL - 326 (Pt 3) N2 - During growth on d-xylose the yeast Candida tenuis produces one aldose reductase that is active with both NADPH and NADH as coenzyme. This enzyme has been isolated by dye ligand and anion-exchange chromatography in yields of 76%. Aldose reductase consists ofa single 43 kDa polypeptide with an isoelectric point of 4.70. Initial velocity, product inhibition and binding studies are consistent with a compulsory-ordered, ternary-complex mechanism with coenzyme binding first and leaving last. The catalytic efficiency (kcat/Km) in d-xylose reduction at pH 7 is more than 60-fold higher than that in xylitol oxidation and reflects significant differences in the corresponding catalytic centre activities as well as apparent substrate-binding constants. The enzyme prefers NADP(H) approx. 2-fold to NAD(H), which is largely due to better apparent binding of the phosphorylated form of the coenzyme. NADP+ is a potent competitive inhibitor of the NADH-linked aldehyde reduction (Ki 1.5 microM), whereas NAD+ is not. Unlike mammalian aldose reductase, the enzyme from C. tenuis is not subject to oxidation-induced activation. Evidence of an essential lysine residue located in or near the coenzyme binding site has been obtained from chemical modification of aldose reductase with pyridoxal 5'-phosphate. The results are discussed in the context of a comparison of the enzymic properties of yeast and mammalian aldose reductase. SN - 0264-6021 UR - https://www.unboundmedicine.com/medline/citation/9307017/NAD_P_H_dependent_aldose_reductase_from_the_xylose_assimilating_yeast_Candida_tenuis__Isolation_characterization_and_biochemical_properties_of_the_enzyme_ L2 - https://portlandpress.com/biochemj/article-lookup/doi/10.1042/bj3260683 DB - PRIME DP - Unbound Medicine ER -