A number of phosphatidyltransferases, which are all involved in phospholipid
biosynthesis and that share the property of catalyzing the displacement of CMP
from a CDP-alcohol by a second alcohol with formation of a phosphodiester bond
and concomitant breaking of a phosphoride anhydride bond share a conserved
sequence region [1,2]. These enzymes are:
Ethanolaminephosphotransferase (EC 2.7.8.1) from yeast (gene EPT1).
Diacylglycerol cholinephosphotransferase (EC 2.7.8.2) from yeast (gene
CPT1).
Phosphatidylserine synthase (EC 2.7.8.8) (CDP-diacylglycerol--serine O-
phosphatidyltransferase) from yeast (gene CHO1) and from Bacillus subtilis
(gene pssA).
Phosphatidylinositol synthase (EC 2.7.8.11) (CDP-diacylglycerol--inositol
3-phosphatidyltransferase) from yeast (gene PIS).
These enzymes are proteins of from 200 to 400 amino acid residues. The
conserved region contains three aspartic acid residues and is located in the
N-terminal section of the sequences.
Last update:
December 2004 / Pattern and text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
References
1
Authors
Nikawa J.-I. Kodaki T. Yamashita S.
Title
Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae.
sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPT1 and EPT1 gene products.
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