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. 2002;49(4):937-45.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyl-CoA Hydrolase / chemistry
  • Acetyl-CoA Hydrolase / genetics*
  • Acetyl-CoA Hydrolase / metabolism*
  • Adenosine Diphosphate / pharmacology
  • Adenosine Triphosphate / pharmacology
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Cytosol / enzymology*
  • DNA, Complementary / genetics
  • Gene Expression
  • Lipid Metabolism*
  • Liver / enzymology
  • Mice
  • Molecular Sequence Data
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Spodoptera / cytology

Substances

  • DNA, Complementary
  • Recombinant Proteins
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Acetyl-CoA Hydrolase

Associated data

  • GENBANK/AA066584
  • GENBANK/AB078618
  • GENBANK/AI425375
  • GENBANK/AK004905