1bwr: Difference between revisions
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Revision as of 15:53, 30 October 2007
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PROBING THE SUBSTRATE SPECIFICITY OF THE INTRACELLULAR BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE
OverviewOverview
Platelet-activating factor acetylhydrolases (PAF-AHs) are unique PLA2s, which hydrolyze the sn-2 ester linkage in PAF-like phospholipids with a, marked preference for very short acyl chains, typically acetyl. The recent, solution of the crystal structure of the alpha(1) catalytic subunit of, isoform Ib of bovine brain intracellular PAF-AH at 1.7 A resolution paved, the way for a detailed examination of the molecular basis of substrate, specificity in this enzyme. The crystal structure suggests that the side, chains of Thr103, Leu48 and Leu194 are involved in substrate recognition., Three single site mutants (L48A, T103S and L194A) were overexpressed and, their structures were solved to 2.3 A resolution or better by X-ray, diffraction methods. Enzyme kinetics showed that, compared with ... [(full description)]
About this StructureAbout this Structure
1BWR is a [Single protein] structure of sequence from [Bos taurus]. Active as [1-alkyl-2-acetylglycerophosphocholine esterase], with EC number [3.1.1.47]. Structure known Active Site: ZNB. Full crystallographic information is available from [OCA].
ReferenceReference
Probing the substrate specificity of the intracellular brain platelet-activating factor acetylhydrolase., Ho YS, Sheffield PJ, Masuyama J, Arai H, Li J, Aoki J, Inoue K, Derewenda U, Derewenda ZS, Protein Eng. 1999 Aug;12(8):693-700. PMID:10469831
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