| Autor: |
Yamada, Junji, Kurata, Akihiro, Hirata, Michiko, Taniguchi, Tomomi, Takama, Hirotaka, Furihata, Takao, Shiratori, Kenji, Iida, Noriko, Takagi-Sakuma, Mitsuhiro, Watanabe, Takafumi, Kurosaki, Kunihiko, Endo, Takahiko, Suga, Tetsuya |
| Předmět: |
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| Zdroj: |
Journal of Biochemistry; 1999, Vol. 126 Issue 6, p1013-1019, 7p |
| Abstrakt: |
An acyl-CoA hydrolase, referred to as hBACH, was purified from human brain cytosol. The enzyme had a molecular mass of 100 kDa and 43-kDa subunits, and was highly active with long-chain acyl-CoAs, e.g. a maximal velocity of 295 μimol/min/mg and Km of 6.4 /iM for palmitoyl-CoA. Acyl-CoAs with carbon chain lengths of C8-i8 were also good substrates. In human brain cytosol, 85% of palmitoyl-CoA hydrolase activity was titrated by an anti-BACH antibody, which accounted for over 75% of the enzyme activity found in the brain tissue. The cDNA isolated for hBACH, when expressed in Escherichia coli, directed the expression of palmitoyl-CoA hydrolase activity and a 44-kDa protein immunoreactive to the anti-BACH antibody, which in turn neutralized the hydrolase activity. The hBACH cDNA encoded a 338-amino acid sequence which was 95% identical to that of a rat homolog. The hBACH gene spanned about 130 kb and comprised 9 exons, and was mapped to 1p36.2 on the cytogenetic ideogram. These findings indicate that the long-chain acyl-CoA hydro-lase present in the brain is well conserved between man and the rat, suggesting a conserved role for this enzyme in the mammalian brain, and enabling genetic studies on the functional analysis of acyl-CoA hydrolase. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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