Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-2-13
pubmed:databankReference
pubmed:abstractText
The ppc gene, which encodes phosphoenolpyruvate carboxylase (PEPC) of an extreme thermophile, Thermus sp., was cloned and sequenced. The ppc gene had a high G+C content (69.2%). An open reading frame for a 857-amino-acid polypeptide was found in the gene. The calculated molecular mass was 95,632. The amino acid sequence of Thermus PEPC was 31-37% identical and 52-57% similar to those of 17 PEPCs from mesophilic organisms. No Cys residue was found in the polypeptide, demonstrating that this residue is not essential for the catalytic activity of PEPC. The cloned gene was expressed in Escherichia coli and thermostable PEPC was obtained.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
118
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
319-24
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Cloning and sequence analysis of the gene for phosphoenolpyruvate carboxylase from an extreme thermophile, Thermus sp.
pubmed:affiliation
Department of Chemistry, Faculty of Science, Kyoto University.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't