Linked Life Data

6361023

Source:http://linkedlifedata.com/resource/pubmed/id/6361023

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1984-2-14
pubmed:abstractText
CDP-diglyceride, the precursor of all the phospholipids in Escherichia coli, is cleaved in vitro to phosphatidic acid and CMP by a membrane-bound hydrolase. Since the physiological function of CDP-diglyceride hydrolase is unknown, we have explored the possibility that this enzyme acts in vivo as either a phosphatidyl- or cytidylyltransferase. To distinguish between these two alternatives, partially purified hydrolase was incubated with CDP-diglyceride in the presence of 50% H218O. Analysis of the reaction products by 31P NMR showed that 18O is incorporated exclusively into CMP, suggesting that the enzyme is a cytidylyltransferase. This conclusion is further supported by the following experimental results: (i) the hydrolase catalyzes the transfer of CMP from CDP-diglyceride to Pi; (ii) numerous phosphomonoesters, such as glycerol 3-phosphate, phosphoserine, and glucose 1-phosphate also function as CMP acceptors, but the corresponding compounds lacking the phosphate residues are not substrates for the enzyme; and (iii) CDP-diglyceride hydrolase exchanges [32P]phosphatidic acid for the phosphatidyl moiety of CDP-diglyceride and 32Pi for the beta-phosphate residue of CDP, indicating the involvement of a novel CMP-enzyme complex. These data suggest a biosynthetic role for CDP-diglyceride hydrolase, and extend the possible functions of CDP-diglyceride in the E. coli envelope.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14974-80
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Chloroform-soluble nucleotides in Escherichia coli. Role of CDP-diglyceride in the enzymatic cytidylylation of phosphomonoester acceptors.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't