The PLD superfamily: insights into catalysis

Authors
Citation
M. Waite, The PLD superfamily: insights into catalysis, BBA-MOL C B, 1439(2), 1999, pp. 187-197
Citations number
42
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
ISSN journal
13881981 → ACNP
Volume
1439
Issue
2
Year of publication
1999
Pages
187 - 197
Database
ISI
SICI code
1388-1981(19990730)1439:2<187:TPSIIC>2.0.ZU;2-6
Abstract
Knowledge of the PLD superfamily is rapidly expanding and new insights into the mechanism and regulation of the superfamily are rapidly emerging. The recent structural analysis and use of mutant proteins suggest a mechanism t hat involves two active sites acting in concert. While a number of residues are required for activity, it appears most likely that a histidine is the residue that becomes covalently linked to phosphatidate in catalysis. Evide nce for these proposals is covered in this article. (C) 1999 Elsevier Scien ce B.V. All rights reserved.