Active site and catalytic mechanism of phospholipase A2
نویسندگان
چکیده
منابع مشابه
Unique Water Entering Path into Secretary Phospholipase A2 Active Site
Secretory phospholipases A2 (sPLA2s) constitute a family of interfacially active mammalian enzymes that catalyze the cleavage of sn-2 ester bond of glycerophospholipid substrates resulting in lysophospholipid and free fatty acid [1]. sPLA2-IIA has proven to be especially interesting in therapeutic intervention since elevated levels of sPLA2-IIA is present in the microenvironment surrounding dif...
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A large number of I4kDa secreted phospholipases A, (sPLA,) have now been identified from venom and mammalian sources. Where solved, these enzymes show similar crystal structures including an active site containing a catalytic dyad of aspartic acid and histidine. In contrast to many lipases and serine proteases, a reactive serine is not utilised as part of the reaction mechanism and an acyl-enzy...
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Site-directed mutagenesis and high-resolution two-dimensional (2D) proton nuclear magnetic resonance (NMR) were used to probe the structural and functional roles of a highly conserved residue, Asp-49, in the interfacial catalysis by bovine pancreatic phospholipase A2 (PLA2, overexpressed in Escherichia coli). According to crystal structures, the side chain carboxylate of Asp-49, along with the ...
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The previous papers in this series (Crook, Mathias d& Rabin, 1960a, b; Herries, Mathias & Rabin, 1962; Findlay, Mathias & Rabin, 1962a, b; Ross, Mathias & Rabin, 1962) provide evidence that the catalytic site of ribonuclease contains two imidazole groups; one of these is required in the acid form and the other in the base form. For the hydrolysis of cytidine 2',3'-phosphate, the shifts in the p...
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ژورنال
عنوان ژورنال: Nature
سال: 1981
ISSN: 0028-0836,1476-4687
DOI: 10.1038/289604a0