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 summarize d here have addressed many facets of interfacial catalysis. These studies h ave revealed a fold and catalytic site common to other lipases. Different c onformations likely to correlate with interfacial activation of the enzyme were observed in different crystal forms. The structures of enzyme-inhibito r complexes have identified the binding site for the scissile fatty acyl ch ain, provided the basis for molecular modeling of triglyceride binding and provided insight into the structural basis of the common enantiopreferences shown by lipases. (C) 1999 Elsevier Science B.V. All rights reserved.