Publication Abstract from PubMed
The crystal and molecular structure of Lipase II from Rhizopus niveus was analyzed using X-ray single crystal diffraction data at a resolution of 2.2 A. The structure was refined to an R-factor of 0.19 for all available data. This lipase was purified and crystallized as Lipase I, which contains two polypeptide chains combined through non-covalent interaction. However, during crystal growth, Lipase I was converted to Lipase II, which consists of a single polypeptide chain of 269 amino acid residues, by limited proteolysis. The structure of Lipase II shows a typical alpha/beta hydrolase fold containing the so-called nucleophilic elbow. The catalytic center of this enzyme is analogous to those of other neutral lipases and serine proteases. This catalytic center is sheltered by an alpha-helix lid, which appears in neutral lipases, opening the active site at the oil-water interface.
The crystal structure of lipase II from Rhizopus niveus at 2.2 A resolution.,Kohno M, Funatsu J, Mikami B, Kugimiya W, Matsuo T, Morita Y J Biochem. 1996 Sep;120(3):505-10. PMID:8902613[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
