Structure-activity of cutinase, a small lipolytic enzyme

Citation
S. Longhi et C. Cambillau, Structure-activity of cutinase, a small lipolytic enzyme, BBA-MOL C B, 1441(2-3), 1999, pp. 185-196
Citations number
47
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
ISSN journal
13881981 → ACNP
Volume
1441
Issue
2-3
Year of publication
1999
Pages
185 - 196
Database
ISI
SICI code
1388-1981(19991123)1441:2-3<185:SOCASL>2.0.ZU;2-T
Abstract
Cutinase, a small lipolytic enzyme, is the smallest member of the alpha/bet a-hydrolase fold family, to which the other lipases belong. Cutinase has a catalytic activity comparable to that of pancreatic lipase on short chain t riglycerides, and retains a significant activity on long chain triglyceride s. Cutinase has been extensively studied using site-directed mutagenesis, a nd we have thoroughly characterized it from a structural point of view. Bes ides the native enzyme, tens of mutants and several inhibitor complexes hav e been solved, providing a complete and precise picture of the structure, d ynamics and catalytic machinery of cutinase. (C) 1999 Elsevier Science B.V. All rights reserved.