NDLI: Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin.

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Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin.

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Year: 2001 Volume: 10 Issue: 4

Year: 2001 Volume: 10 Issue: 3

Year: 2001 Volume: 10 Issue: 2

Year: 2001 Volume: 10 Issue: 1

Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wajant, H. Lauble, H. Miehlich, B. Förster, S. Effenberger, F.
Description	Country affiliation: Germany Author Affiliation: Lauble H ( Institut für Organische Chemie der Universität Stuttgart, D-70569 Stuttgart, Germany. PeterLauble@t-online.de)
Abstract	The structure and function of hydroxynitrile lyase from Manihot esculenta (MeHNL) have been analyzed by X-ray crystallography and site-directed mutagenesis. The crystal structure of the MeHNL-S80A mutant enzyme has been refined to an R-factor of 18.0% against diffraction data to 2.1-A resolution. The three-dimensional structure of the MeHNL-S80A-acetone cyanohydrin complex was determined at 2.2-A resolution and refined to an R-factor of 18.7%. Thr11 and Cys81 involved in substrate binding have been substituted by Ala in site-directed mutagenesis. The kinetic measurements of these mutant enzymes are presented. Combined with structural data, the results support a mechanism for cyanogenesis in which His236 as a general base abstracts a proton from Ser80, thereby allowing proton transfer from the hydroxyl group of acetone cyanohydrin to Ser80. The His236 imidazolium cation then facilitates the leaving of the nitrile group by proton donating.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aldehyde-lyases Chemistry Metabolism Amino Acid Substitution Genetics Manihot Enzymology Nitriles Binding Sites Catalysis Catalytic Domain Crystallography, X-ray Hazardous Substances Kinetics Models, Molecular Mutation Protein Binding Protein Conformation Structure-activity Relationship Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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