Pancreatic phospholipase A(2): new views on old issues.
The recent development in the structure-function relationship of pancreatic phospholipase A(2) is reviewed. The results of extensive studies by a combination of site-directed mutagenesis, X-ray crystallography, and NMR have provided new insight into several old issues. In particular, we summarize current views on the active site, the interfacial binding site, the mechanism of interfacial activation, the roles of the hydrogen-bonding network and the catalytic dyad, and the conformational stability of the structure.
Yuan
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C
Department of Chemistry, Ohio State University, 100 West 18th Avenue, Columbus, OH 43210-1173, USA.
Tsai
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M
D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D004355:Drug Stability; D004789:Enzyme Activation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010179:Pancreas / Q000201:enzymology*; D010741:Phospholipases A / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D010741:Phospholipases A