1xql: Difference between revisions

Revision as of 03:59, 28 July 2008

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File:1xql.png

Template:STRUCTURE 1xql

Effect of a Y265F Mutant on the Transamination Based Cycloserine Inactivation of Alanine RacemaseEffect of a Y265F Mutant on the Transamination Based Cycloserine Inactivation of Alanine Racemase

Template:ABSTRACT PUBMED 15807525

About this StructureAbout this Structure

1XQL is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase., Fenn TD, Holyoak T, Stamper GF, Ringe D, Biochemistry. 2005 Apr 12;44(14):5317-27. PMID:15807525

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-'''Effect of a Y265F Mutant on the Transamination Based Cycloserine Inactivation of Alanine Racemase'''
+===Effect of a Y265F Mutant on the Transamination Based Cycloserine Inactivation of Alanine Racemase===
-==Overview==
+<!--
-The requirement for d-alanine in the peptidoglycan layer of bacterial cell walls is fulfilled in part by alanine racemase (EC 5.1.1.1), a pyridoxal 5'-phosphate (PLP)-assisted enzyme. The enzyme utilizes two antiparallel bases focused at the C(alpha) position and oriented perpendicular to the PLP ring to facilitate the equilibration of alanine enantiomers. Understanding how this two-base system is utilized and controlled to yield reaction specificity is therefore a potential means for designing antibiotics. Cycloserine is a known alanine racemase suicide substrate, although its mechanism of inactivation is based on transaminase chemistry. Here we characterize the effects of a Y265F mutant (Tyr265 acts as the catalytic base in the l-isomer case) of Bacillus stearothermophilus alanine racemase on cycloserine inactivation. The Y265F mutant reduces racemization activity 1600-fold [Watanabe, A., Yoshimura, T., Mikami, B., and Esaki, N. (1999) J. Biochem. 126, 781-786] and only leads to formation of the isoxazole end product (the result of the transaminase pathway) in the case of d-cycloserine, in contrast to results obtained using the wild-type enzyme. l-Cycloserine, on the other hand, utilizes a number of alternative pathways in the absence of Y265, emphasizing the importance of Y265 in both the inactivation and racemization pathway. In combination with the kinetics of inactivation, these results suggest roles for each of the two catalytic bases in racemization and inactivation, as well as the importance of Y265 in "steering" the chemistry to favor one pathway over another.
+The line below this paragraph, {{ABSTRACT_PUBMED_15807525}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15807525 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15807525}}
 ==About this Structure==
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 [[Category: Cycloserine]]
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