Affiliation:
1. Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, Texas 77025
Abstract
Cell-free extracts of
Salmonella typhimurium, Serratia marcescens, Enterobacter aerogenes
, and
Micrococcus cerificans
contained the following enzymatic activities related to phospholipid metabolism: cytidine 5′-diphospho-1,2-diacyl-
sn
-glycerol (CDP-diglyceride):
l
-serine
O
-phosphatidyltransferase (phosphatidylserine synthase), phosphatidylserine decarboxylase, CDP-diglyceride:
sn
-glycero-3-phosphate phosphatidyltransferase (phosphatidylglycerophosphate synthase), phosphatidylglycerophosphate phosphatase, and CDP-diglyceride hydrolase. The intracellular distribution of these enzymatic activities as determined by sucrose density gradient centrifugation of cell-free extracts was shown to be similar in each species investigated. The phosphatidylserine decarboxylase, phosphatidylglycerophosphate synthase, and CDP-diglyceride hydrolase activities were all associated with the cell envelope fraction, whereas the phosphatidylserine synthase activity was associated mainly with the ribosomal fraction. These enzymatic activities are comparable and have an intracellular distribution similar to those found in
Escherichia coli
cell-free extracts. Therefore, the pathways established for phospholipid biosynthesis in
E. coli
can also account for the synthesis of the major phospholipids (phosphatidylethanolamine and phosphatidylglycerol) in several other gram-negative organisms. In addition, the unusual ribosomal association of the phosphatidylserine synthase from
E. coli
(Raetz and Kennedy, J. Biol. Chem.
247:
2008–2014, 1972) appears to be a general property for this activity in several other bacterial species.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
48 articles.
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