Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
1992-5-28
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M80544,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86250,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86251,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86252,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86253,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86254,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86255,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86256,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86257,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X61766
|
pubmed:abstractText |
Myristoyl-CoA:protein N-myristoyltransferase (NMT) has recently been identified as a target for antiviral and antifungal therapy. Candida albicans is a dimorphic, asexual yeast that is a major cause of systemic fungal infections in immunosuppressed humans. Metabolic labeling studies indicate that C. albicans synthesizes one principal 20-kDa N-myristoyl-protein. The single copy C. albicans NMT gene (ca-NMT1) was isolated and encodes a 451-amino acid protein that has 55% identity with Saccharomyces cerevisiae NMT. C. albicans NMT1 is able to complement the lethal phenotype of S. cerevisiae nmt1 null mutants by directing efficient acylation of the approximately 12 endogenous N-myristoylproteins produced by S. cerevisiae. C. albicans NMT was produced in Escherichia coli, a prokaryote with no endogenous NMT activity. In vitro studies of purified E. coli-derived S. cerevisiae and C. albicans NMTs revealed species-specific differences in the kinetic properties of synthetic octapeptide substrates derived from known N-myristoylproteins. Together these data indicate that C. albicans and S. cerevisiae NMTs have similar yet distinct substrate specificities which may be of therapeutic significance.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
267
|
pubmed:geneSymbol |
NMT
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
8591-8
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:1569105-Acyltransferases,
pubmed-meshheading:1569105-Amino Acid Sequence,
pubmed-meshheading:1569105-Base Sequence,
pubmed-meshheading:1569105-Candida albicans,
pubmed-meshheading:1569105-DNA, Fungal,
pubmed-meshheading:1569105-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1569105-Escherichia coli,
pubmed-meshheading:1569105-Gene Expression,
pubmed-meshheading:1569105-Kinetics,
pubmed-meshheading:1569105-Molecular Sequence Data,
pubmed-meshheading:1569105-Saccharomyces cerevisiae,
pubmed-meshheading:1569105-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1569105-Substrate Specificity
|
pubmed:year |
1992
|
pubmed:articleTitle |
The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli.
|
pubmed:affiliation |
Monsanto Corporate Research, Chesterfield, Missouri 63198.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|