Structural highlights
Function
[LIP_RHINI] Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
See Also
References
- ↑ Kohno M, Funatsu J, Mikami B, Kugimiya W, Matsuo T, Morita Y. The crystal structure of lipase II from Rhizopus niveus at 2.2 A resolution. J Biochem. 1996 Sep;120(3):505-10. PMID:8902613
