| Title : Structure and conformational flexibility of Candida rugosa lipase - Cygler_1999_Biochim.Biophys.Acta_1441_205 |
| Author(s) : Cygler M , Schrag JD |
| Ref : Biochimica & Biophysica Acta , 1441 :205 , 1999 |
| Abstract : 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. |
| ESTHER : Cygler_1999_Biochim.Biophys.Acta_1441_205 |
| PubMedSearch : Cygler_1999_Biochim.Biophys.Acta_1441_205 |
| PubMedID: 10570248 |
Cygler M, Schrag JD (1999)
Structure and conformational flexibility of Candida rugosa lipase
Biochimica & Biophysica Acta
1441 :205
Cygler M, Schrag JD (1999)
Biochimica & Biophysica Acta
1441 :205