Approaches for deciphering the structural basis of low temperature enzyme activity

Citation
Pp. Sheridan et al., Approaches for deciphering the structural basis of low temperature enzyme activity, BBA-PROT ST, 1543(2), 2000, pp. 417-433
Citations number
90
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
ISSN journal
01674838 → ACNP
Volume
1543
Issue
2
Year of publication
2000
Pages
417 - 433
Database
ISI
SICI code
0167-4838(200012)1543:2<417:AFDTSB>2.0.ZU;2-U
Abstract
An increasing number of enzymes active at low temperature are being studied to help determine the structural features important for cold-activity. Thi s review examines the diversity of prokaryotic cold-active enzymes and the features proposed to account for low temperature activity. We then consider the difficulty of identifying the key structural features needed for cold- activity and the need to compare enzymes having different temperature optim a from phylogenetically related organisms to determine features responsible for low temperature activity. In addition to studying naturally occurring enzymes, directed evolution experiments are discussed as methods for examin ing the proposed mechanisms influencing the thermal dependence of activity. (C) 2000 Elsevier Science B.V. All rights reserved.