| First Author | Suematsu N | Year | 2002 |
| Journal | Acta Biochim Pol | Volume | 49 |
| Issue | 4 | Pages | 937-45 |
| PubMed ID | 12545200 | Mgi Jnum | J:81957 |
| Mgi Id | MGI:2450440 | Citation | Suematsu N, et al. (2002) Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolism: cDNA cloning, sequencing and functional expression. Acta Biochim Pol 49(4):937-45 |
| abstractText | 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. |
