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General Comment |
Activation of long-chain fatty acids by the long-chain acyl-coenzyme A synthetase (LACS) is the first reaction in their
metabolism. Thus, this enzyme, which is also known as palmitoyl-CoA ligase (EC 6.2.1.3 ), plays a key role in both the
synthesis of cellular lipids and the degradation of fatty acids.
Tang et al 2001 reported the cloning and characterization of a
hormonally regulated rat long
chain acyl-CoA synthetase.
A previously unidentified gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS)
was cloned and characterized as a 79-kDa cytoplasmic protein expressed in Leydig cells of the
rat testis. GR-LACS shares sequence identity with two conserved regions of the LACS and luciferase families, including the ATP/AMP binding domain and the 25-aa fatty acyl-CoA
synthetase signature motif, but displays low overall amino acid similarities (23-28%). GR-LACS
mRNA is expressed abundantly in Leydig cells of the adult testis and to a lesser degree in the
seminiferous tubules in spermatogonia and Sertoli cells. It is also observed in ovary and brain.
GR-LACS may contribute to the
provision of energy requirements and to the biosynthesis of steroid precursors and could
participate through acyl-CoA's multiple functions in the regulation of the gonad.
NCBI Summary:
The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme is mainly present in brain, and its amino acid sequence is 85% identical to that of rat homolog.
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