rdf:type |
|
lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0024660,
umls-concept:C0033684,
umls-concept:C0035496,
umls-concept:C0205231,
umls-concept:C0330390,
umls-concept:C0337112,
umls-concept:C0679058,
umls-concept:C1123015,
umls-concept:C1334043,
umls-concept:C1519249,
umls-concept:C1524075,
umls-concept:C1547699,
umls-concept:C2697616,
umls-concept:C2700640
|
pubmed:issue |
1
|
pubmed:dateCreated |
1993-1-4
|
pubmed:databankReference |
|
pubmed:abstractText |
Sequence analysis of a 2-kilobase DNA fragment from Rhodococcus sp. NI86/21 revealed an open reading frame encoding a 476-amino-acid protein with striking homology to the rat and human propionyl-CoA carboxylase beta subunits. The nucleotide sequence of a corresponding prokaryotic gene has not yet been reported. Upstream, the C-terminal part of a putative beta-ketoacyl synthase was identified.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0378-1119
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
122
|
pubmed:geneSymbol |
pccB
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
199-202
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:1452030-3-Oxoacyl-(Acyl-Carrier-Protein) Synthase,
pubmed-meshheading:1452030-Amino Acid Sequence,
pubmed-meshheading:1452030-Animals,
pubmed-meshheading:1452030-Base Sequence,
pubmed-meshheading:1452030-Carboxy-Lyases,
pubmed-meshheading:1452030-DNA, Bacterial,
pubmed-meshheading:1452030-Genes, Bacterial,
pubmed-meshheading:1452030-Genetic Linkage,
pubmed-meshheading:1452030-Mammals,
pubmed-meshheading:1452030-Methylmalonyl-CoA Decarboxylase,
pubmed-meshheading:1452030-Molecular Sequence Data,
pubmed-meshheading:1452030-Open Reading Frames,
pubmed-meshheading:1452030-Rhodococcus,
pubmed-meshheading:1452030-Sequence Homology, Amino Acid
|
pubmed:year |
1992
|
pubmed:articleTitle |
Sequence of a Rhodococcus gene encoding a protein with extensive homology to the mammalian propionyl-CoA carboxylase beta chain.
|
pubmed:affiliation |
F.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee, Belgium.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|