Primary structure and tissue-specific expression of human β- hydroxyisobutyryl-coenzyme A hydrolase

John W. Hawes, Jerzy Jaskiewicz, Yoshiharu Shimomura, Boli Huang, Jamie Bunting, Edwin T. Harper, Robert A. Harris

Research output: Contribution to journalArticle

36 Scopus citations


β-Hydroxyisobutyryl-CoA (HIBYL-CoA) hydrolase is responsible for the specific hydrolysis of HIBYL-CoA, a saline catabolite, as well as the hydrolysis of β-hydroxypropionyl-CoA, an intermediate in a minor pathway of propionate metabolism. We have obtained the amino acid sequences of several tryptic peptides derived from purified rat liver HIBYL-CoA hydrolase, and the NH2-terminal peptize sequence was matched to the translated sequence of a human expressed sequence tag present in the data base of the IMAGE Consortium (Lawrence Livermore National Laboratory, Livermore, CA). The complete nucleotide sequence and the deduced amino acid sequence showed no similarity to the sequences of well known thioesterases but showed significant homology to the enoyl-CoA hydratase/isomerase enzyme family. The cDNA fragment corresponding to the mature (processed) protein was expressed in Escherichia coli. The purified recombinant enzyme displayed substrate specificity very similar to that of the rat enzyme and was specifically bound by polyclonal antibodies raised against purified rat liver HIBYL-CoA hydrolase. Northern and Western blot analyses with various human tissues indicated predominant expression in liver, heart, and kidney, with discrepancies occurring in the amounts of HIBYL-CoA hydrolase mRNA compared to stably expressed protein in several tissues.

Original languageEnglish (US)
Pages (from-to)26430-26434
Number of pages5
JournalJournal of Biological Chemistry
Issue number42
StatePublished - Oct 29 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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