Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1998-6-15
|
pubmed:abstractText |
Following the complete sequencing of the Escherichia coli genome, it has been shown that the proposed second citrate synthase of this organism, recently described by the authors, is in fact a 2-methylcitrate synthase that possesses citrate synthase activity as a minor component. Whereas the hexameric citrate synthase is constitutively produced, the 2-methylcitrate synthase is induced during growth on propionate, and the catabolism of propionate to succinate and pyruvate via 2-methylcitrate is proposed. The citrate synthases of the psychrotolerant eubacterium DS2-3R, and of the thermophilic archaea Thermoplasma acidophilum and Pyrococcus furiosus, are approximately 40% identical in sequence to the Escherichia coli 2-methylcitrate synthase and also possess 2-methylcitrate synthase activity. The data are discussed with respect to the structure, function and evolution of citrate synthase and 2-methylcitrate synthase.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
1350-0872
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
144 ( Pt 4)
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
929-35
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading | |
pubmed:year |
1998
|
pubmed:articleTitle |
Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships.
|
pubmed:affiliation |
Department of Biology and Biochemistry, University of Bath, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|