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Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis.
Chem Biol Interact. 2001 Jan 30; 130-132(1-3):583-95.CB

Abstract

The primary structure of the aldose xylose reductase from Candida tenuis (CtAR) is shown to be 39% identical to that of human aldose reductase (hAR). The catalytic tetrad of hAR is completely conserved in CtAR (Tyr51, Lys80, Asp46, His113). The amino acid residues involved in binding of NADPH by hAR (D.K. Wilson, et al., Science 257 (1992) 81-84) are 64% identical in CtAR. Like hAR the yeast enzyme is specific for transferring the 4-pro-R hydrogen of the coenzyme. These properties suggest that CtAR is a member of the aldo/keto reductase superfamily. Unlike hAR the enzyme from C. tenuis has a dual coenzyme specificity and shows similar specificity constants for NADPH and NADH. It binds NADP(+) approximately 250 times less tightly than hAR. Typical turnover numbers for aldehyde reduction by CtAR (15-20 s(-1)) are up to 100-fold higher than corresponding values for hAR, probably reflecting an overall faster dissociation of NAD(P)(+) in the reaction catalyzed by the yeast enzyme.

Authors+Show Affiliations

Division of Biochemical Engineering, Institute of Food Technology, University of Agricultural Sciences, Muthgasse 18, A-1190, Vienna, Austria. nide@edv2.boku.ac.atNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

11306077

Citation

Nidetzky, B, et al. "Structural and Functional Properties of Aldose Xylose Reductase From the D-xylose-metabolizing Yeast Candida Tenuis." Chemico-biological Interactions, vol. 130-132, no. 1-3, 2001, pp. 583-95.
Nidetzky B, Mayr P, Neuhauser W, et al. Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis. Chem Biol Interact. 2001;130-132(1-3):583-95.
Nidetzky, B., Mayr, P., Neuhauser, W., & Puchberger, M. (2001). Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis. Chemico-biological Interactions, 130-132(1-3), 583-95.
Nidetzky B, et al. Structural and Functional Properties of Aldose Xylose Reductase From the D-xylose-metabolizing Yeast Candida Tenuis. Chem Biol Interact. 2001 Jan 30;130-132(1-3):583-95. PubMed PMID: 11306077.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis. AU - Nidetzky,B, AU - Mayr,P, AU - Neuhauser,W, AU - Puchberger,M, PY - 2001/4/18/pubmed PY - 2001/5/22/medline PY - 2001/4/18/entrez SP - 583 EP - 95 JF - Chemico-biological interactions JO - Chem. Biol. Interact. VL - 130-132 IS - 1-3 N2 - The primary structure of the aldose xylose reductase from Candida tenuis (CtAR) is shown to be 39% identical to that of human aldose reductase (hAR). The catalytic tetrad of hAR is completely conserved in CtAR (Tyr51, Lys80, Asp46, His113). The amino acid residues involved in binding of NADPH by hAR (D.K. Wilson, et al., Science 257 (1992) 81-84) are 64% identical in CtAR. Like hAR the yeast enzyme is specific for transferring the 4-pro-R hydrogen of the coenzyme. These properties suggest that CtAR is a member of the aldo/keto reductase superfamily. Unlike hAR the enzyme from C. tenuis has a dual coenzyme specificity and shows similar specificity constants for NADPH and NADH. It binds NADP(+) approximately 250 times less tightly than hAR. Typical turnover numbers for aldehyde reduction by CtAR (15-20 s(-1)) are up to 100-fold higher than corresponding values for hAR, probably reflecting an overall faster dissociation of NAD(P)(+) in the reaction catalyzed by the yeast enzyme. SN - 0009-2797 UR - https://www.unboundmedicine.com/medline/citation/11306077/Structural_and_functional_properties_of_aldose_xylose_reductase_from_the_D_xylose_metabolizing_yeast_Candida_tenuis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0009279700002854 DB - PRIME DP - Unbound Medicine ER -