Human long-chain acyl-CoA synthetase: Structure and chromosomal location

Takaaki Abe, Takahiro Fujino, Ryuichi Fukuyama, Shinsei Minoshima, Nobuyoshi Shimizu, Hiroyuki Toh, Hiroyuki Suzuki, Tokuo Yamamoto

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50 Citations (Scopus)

Abstract

A complementary DNA clone encoding the entire human long-chain acyl-CoA synthetase was isolated and the total 698-amino acid sequence was deduced. The amino acid sequence of human long-chain acyl-CoA synthetase shows 84.9% identity to that of rat long-chain acyl-CoA synthetase. The nucleotide sequences of the protein coding regions between human and rat long-chain acyl-CoA synthetase mRNAs are highly conserved (85.6%), whereas those of the 3′ untranslated regions are less conserved (72%). The location of the human long-chain acyl-CoA synthetase gene was identified on chromosome 4 by spot hybridization of flow-sorted chromosomes. Computer-assisted homology search revealed a significant similarity of the enzyme with the enzymes of the luciferase family. Based on this similarity, the structure of human long-chain acyl-CoA synthetase can be divided into five domains: the N-terminus, two domains similar to those in enzymes of the luciferase family, a long gap region between the similar domains and the C-terminus.

Original languageEnglish
Pages (from-to)123-128
Number of pages6
JournalJournal of biochemistry
Volume111
Issue number1
DOIs
Publication statusPublished - 1992 Jan

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Abe, T., Fujino, T., Fukuyama, R., Minoshima, S., Shimizu, N., Toh, H., Suzuki, H., & Yamamoto, T. (1992). Human long-chain acyl-CoA synthetase: Structure and chromosomal location. Journal of biochemistry, 111(1), 123-128. https://doi.org/10.1093/oxfordjournals.jbchem.a123707