Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolism: cDNA cloning, sequencing and functional expression.

Naoya Suematsu; Kazuki Okamoto; Fumihide Isohashi

doi:10.18388/abp.2002_3753

Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolism: cDNA cloning, sequencing and functional expression.

Naoya Suematsu Department of Biochemistry, St Marianna University School of Medicine, Kanagawa, Japan.;
Kazuki Okamoto
Fumihide Isohashi

DOI: https://doi.org/10.18388/abp.2002_3753

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.

Published

2002-12-31

Issue

Vol. 49 No. 4 (2002)

Section

Articles

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