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    Acta Biochim Pol. 2006;53(3):553-61. Epub 2006 Sep 2.

    Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase.

    Suematsu N, Isohashi F.

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    Department of Biochemistry, St. Marianna University School of Medicine, Kanagawa, Japan. n2sue@marianna-u.ac.jp

    Abstract

    A cDNA encoding human cytosolic acetyl-CoA hydrolase (CACH) was isolated from a human liver cDNA library, sequenced and functionally expressed in insect cells. The human CACH cDNA encodes a 555-amino-acid sequence that is 81.4%/78.7% identical to those of the mouse/rat homologue, suggesting a conserved role for this enzyme in the human and rodent livers. Bioinformatical study further reveals a high degree of similarity among the human and rodent CACHs as follows: First, the gene is composed of 15 exons ranging in size from 56 to 157 bp. Second, the protein consists of two thioesterase regions and a C-terminal steroidogenic acute regulatory protein-related lipid transfer (START) domain. Third, the promoter region is GC-rich and contains GC boxes, but lacks both TATA and CCAAT boxes, the typical criteria of housekeeping genes. A consensus peroxisome proliferator responsive element (PPRE) present in the rodent CACH promoter regions supports marked CACH induction in rat liver by peroxisome proliferator (PP).

    PMID:
    16951743
    [PubMed - indexed for MEDLINE]
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