Linked Life Data

2635863

Source:http://linkedlifedata.com/resource/pubmed/id/2635863

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1990-6-18
pubmed:abstractText
A novel phospholipid analogue, di (triethyleneglycol-n-tetradecylether) phosphate was synthesized and its activation ability for a phospholipid-requiring enzyme, Mycobacterium smegmatis malate dehydrogenase, was examined. The results showed that the newly-synthesized phospholipid analogue a high ability, nearly equal to that of natural beef heart cardiolipin, for the activation of the lipid-depleted inactive enzyme; whereas both simple di-n-octylphosphate and di-n-tetradecylphosphate were found to have poor activation abilities. These results strongly suggest that a slightly hydrophilic region between the phosphate group and the two alkyl chains of an anionic phospholipid is important for the best activation of M. smegmatis malate dehydrogenase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1277-86
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
FAD-dependent malate dehydrogenase from Mycobacterium smegmatis: activation of the lipid-depleted inactive enzyme by a phospholipid analogue, di (triethyleneglycoltetradecylether) phosphate.
pubmed:affiliation
Department of Chemistry, Rikkyo (St. Paul's) University, Tokyo, Japan.
pubmed:publicationType
Journal Article