NDLI: Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase.

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Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Blanco, Julio Moore, Roger A. Viola, Ronald E.
Description	Author Affiliation: Blanco J ( Department of Chemistry, University of Toledo, Toledo, OH 43606, USA.);
Abstract	The structural analysis of an enzymatic reaction intermediate affords a unique opportunity to study a catalytic mechanism in extraordinary detail. Here we present the structure of a tetrahedral intermediate in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Haemophilus influenzae at 2.0-A resolution. ASADH is not found in humans, yet its catalytic activity is required for the biosynthesis of essential amino acids in plants and microorganisms. Diaminopimelic acid, also formed by this enzymatic pathway, is an integral component of bacterial cell walls, thus making ASADH an attractive target for the development of new antibiotics. This enzyme is able to capture the substrates aspartate-beta-semialdehyde and phosphate as an active complex that does not complete the catalytic cycle in the absence of NADP. A distinctive binding pocket in which the hemithioacetal oxygen of the bound substrate is stabilized by interaction with a backbone amide group dictates the R stereochemistry of the tetrahedral intermediate. This pocket, reminiscent of the oxyanion hole found in serine proteases, is completed through hydrogen bonding to the bound phosphate substrate.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aspartate-Semialdehyde Dehydrogenase Chemistry Metabolism Amino Acid Sequence Amino Acids, Essential Biosynthesis Apoenzymes Binding Sites Catalysis Crystallography, X-Ray Haemophilus Influenzae Enzymology Models, Molecular Protein Conformation Recombinant Proteins Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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