| Insights into the fatty acid chain length specificity of the carboxylesterase PA3859 from Pseudomonas aeruginosa: A combined structural, biochemical and computational study. | |
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MedLine Citation:
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PMID: 20850500 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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The open reading frame PA3859 of Pseudomonas aeruginosa encodes an intracellular carboxylesterase belonging to a group of microbial enzymes (EC 3.1.1.1) that catalyze the hydrolysis of aliphatic and aromatic esters with a broad substrate specificity. With few exceptions, for this class of enzymes, belonging to the α/β-hydrolase fold superfamily, very little information is available regarding their biochemical activity and in vivo function. The X-ray crystal structure of recombinant PA3859 has been determined for two crystal forms (space groups P2(1) and P2(1)2(1)2). The kinetic properties of the enzyme were studied using p-nitrophenyl esters as substrates and data fitted to a surface dilution mixed micelle kinetic model. Enzymatic assays and computational docking simulations, pinpointed the enzyme's preference for esters of palmitic and/or stearic acids and provided insights into the enzyme-substrate favorable binding modes. |
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Authors:
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Alessandro Pesaresi; Doriano Lamba |
Publication Detail:
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Type: Journal Article Date: 2010-09-17 |
Journal Detail:
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Title: Biochimie Volume: 92 ISSN: 1638-6183 ISO Abbreviation: Biochimie Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-12-06 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 1264604 Medline TA: Biochimie Country: France |
Other Details:
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Languages: eng Pagination: 1787-92 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier Masson SAS. All rights reserved. |
Affiliation:
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Istituto di Cristallografia, Consiglio Nazionale delle Ricerche, Area Science Park - Basovizza, S.S. 14, Km 163.5, I-34149 Trieste, Italy. alessandro.pesaresi@ts.ic.cnr.it |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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