| Literature DB >> 12545200 |
Naoya Suematsu1, Kazuki Okamoto, Fumihide Isohashi.
Abstract
A cytosolic acetyl-CoA hydrolase (CACH) cDNA has been isolated from mouse liver cDNA library and sequenced. Recombinant expression of the cDNA in insect cells resulted in overproduction of active acetyl-CoA hydrolyzing enzyme protein. The mouse CACH cDNA encoded a 556-amino-acid sequence that was 93.5% identical to rat CACH, suggesting a conserved role for this enzyme in the mammalian liver. Database searching shows no homology to other known proteins, but reveals homological cDNA sequences showing two single-nucleotide polymorphisms (SNPs) in the CACH coding region. The discovery of mouse CACH cDNA is an important step towards genetic studies on the functional analysis of this enzyme by gene-knockout and transgenic approaches.Entities:
Mesh:
Substances:
Year: 2002 PMID: 12545200
Source DB: PubMed Journal: Acta Biochim Pol ISSN: 0001-527X Impact factor: 2.149