Structure and conformational flexibility of Candida rugosa lipase.
Three-dimensional structures of a number of lipases determined in the past decade have provided a solid structural foundation for our understanding of lipase function. The structural studies of Candida rugosa lipase summarized here have addressed many facets of interfacial catalysis. These studies have revealed a fold and catalytic site common to other lipases. Different conformations likely to correlate with interfacial activation of the enzyme were observed in different crystal forms. The structures of enzyme-inhibitor complexes have identified the binding site for the scissile fatty acyl chain, provided the basis for molecular modeling of triglyceride binding and provided insight into the structural basis of the common enantiopreferences shown by lipases.
Cygler
M
M
Biotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montreal, Quebec, Canada. mirek.cygler@bri.nrc.ca
Schrag
J D
JD
D001665:Binding Sites; D002175:Candida / Q000201:enzymology*; D004789:Enzyme Activation; D015870:Gene Expression; D008049:Lipase / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D011487:Protein Conformation; D013237:Stereoisomerism; D013379:Substrate Specificity
D008049:Lipase