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Tyr-51 is the proton donor-acceptor for NAD(H)-dependent interconversion of xylose and xylitol by Candida tenuis xylose reductase (AKR2B5).
FEBS Lett. 2008 Dec 10; 582(29):4095-9.FL

Abstract

Substitution of active-site Tyr-51 by Ala (Y51A) disrupted the activity of Candida tenuis xylose reductase by six orders of magnitude. External bromide brought about unidirectional rate enhancement (approximately 2x10(3)-fold at 300mM) for NAD(+)-dependent xylitol oxidation by Y51A. Activity of the wild-type reductase was dependent on a single ionizable protein group exhibiting a pK of 9.2+/-0.1 and 7.3+/-0.3 in the holo-enzyme bound with NADH and NAD(+), respectively. This group which had to be protonated for xylose reduction and unprotonated for xylitol oxidation was eliminated in Y51A, consistent with a catalytic acid-base function of Tyr-51. Bromide may complement the xylitol dehydrogenase activity of Y51A by partly restoring the original hydrogen bond between the reactive alcohol and the phenolate of Tyr-51.

Authors+Show Affiliations

Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, A-8010 Graz, 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

19026644

Citation

Pival, Simone L., et al. "Tyr-51 Is the Proton Donor-acceptor for NAD(H)-dependent Interconversion of Xylose and Xylitol By Candida Tenuis Xylose Reductase (AKR2B5)." FEBS Letters, vol. 582, no. 29, 2008, pp. 4095-9.
Pival SL, Klimacek M, Kratzer R, et al. Tyr-51 is the proton donor-acceptor for NAD(H)-dependent interconversion of xylose and xylitol by Candida tenuis xylose reductase (AKR2B5). FEBS Lett. 2008;582(29):4095-9.
Pival, S. L., Klimacek, M., Kratzer, R., & Nidetzky, B. (2008). Tyr-51 is the proton donor-acceptor for NAD(H)-dependent interconversion of xylose and xylitol by Candida tenuis xylose reductase (AKR2B5). FEBS Letters, 582(29), 4095-9. https://doi.org/10.1016/j.febslet.2008.11.003
Pival SL, et al. Tyr-51 Is the Proton Donor-acceptor for NAD(H)-dependent Interconversion of Xylose and Xylitol By Candida Tenuis Xylose Reductase (AKR2B5). FEBS Lett. 2008 Dec 10;582(29):4095-9. PubMed PMID: 19026644.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Tyr-51 is the proton donor-acceptor for NAD(H)-dependent interconversion of xylose and xylitol by Candida tenuis xylose reductase (AKR2B5). AU - Pival,Simone L, AU - Klimacek,Mario, AU - Kratzer,Regina, AU - Nidetzky,Bernd, Y1 - 2008/11/19/ PY - 2008/09/10/received PY - 2008/10/09/revised PY - 2008/11/04/accepted PY - 2008/11/26/pubmed PY - 2009/2/20/medline PY - 2008/11/26/entrez SP - 4095 EP - 9 JF - FEBS letters JO - FEBS Lett. VL - 582 IS - 29 N2 - Substitution of active-site Tyr-51 by Ala (Y51A) disrupted the activity of Candida tenuis xylose reductase by six orders of magnitude. External bromide brought about unidirectional rate enhancement (approximately 2x10(3)-fold at 300mM) for NAD(+)-dependent xylitol oxidation by Y51A. Activity of the wild-type reductase was dependent on a single ionizable protein group exhibiting a pK of 9.2+/-0.1 and 7.3+/-0.3 in the holo-enzyme bound with NADH and NAD(+), respectively. This group which had to be protonated for xylose reduction and unprotonated for xylitol oxidation was eliminated in Y51A, consistent with a catalytic acid-base function of Tyr-51. Bromide may complement the xylitol dehydrogenase activity of Y51A by partly restoring the original hydrogen bond between the reactive alcohol and the phenolate of Tyr-51. SN - 0014-5793 UR - https://www.unboundmedicine.com/medline/citation/19026644/Tyr_51_is_the_proton_donor_acceptor_for_NAD_H__dependent_interconversion_of_xylose_and_xylitol_by_Candida_tenuis_xylose_reductase__AKR2B5__ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-5793(08)00903-4 DB - PRIME DP - Unbound Medicine ER -