Linked Life Data

7918616

Source:http://linkedlifedata.com/resource/pubmed/id/7918616

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-11-23
pubmed:abstractText
Escherichia coli cardiolipin synthase catalyzes the conversion of two phosphatidylglycerol molecules to cardiolipin and glycerol. This enzyme was amplified in strain BL21(DE3) bearing recombinant plasmid pLR3, which was itself constructed by inserting the cls gene downstream from a T7 RNA promoter. Membranes from BL21(DE3)/pLR3 have over 1200 times more cardiolipin synthase activity than do comparable membranes from wild type cells. The enzyme was purified to homogeneity by extraction with Triton X-114 and chromatography on DEAE-cellulose. The purified enzyme migrated as a single band (46 kDa) on SDS-PAGE. This, along with SDS-PAGE analysis of induced protein, supports the notion that cls is the structural gene for cardiolipin synthase. Cardiolipin synthase activity was determined in a mixed micelle assay in which phosphatidyl[2-3H]glycerol was the substrate. The enzyme is inhibited by the product of the reaction, cardiolipin, and by phosphatidate. However, it is not inhibited by two other anionic phosphoglycerides, phosphatidylinositol and bis-phosphatidate. Phosphatidylethanolamine partially offsets inhibition by cardiolipin but not by phosphatidate. Magnesium chloride has the opposite effect. Cardiolipin inhibition of cardiolipin synthase probably plays an important role in regulating cardiolipin synthesis in E. coli.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
1214
pubmed:geneSymbol
cls
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The effects of phosphoglycerides on Escherichia coli cardiolipin synthase.
pubmed:affiliation
Queens College, Department of Chemistry and Biochemistry, Flushing, NY 11367.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't