Baboon carboxylesterases 1 and 2: Sequences, structures and phylogenetic relationships with human and other primate carboxylesterases

Roger S. Holmes, Jeremy P. Glenn, John L. Vandeberg, Laura A. Cox

    Research output: Contribution to journalArticle

    13 Scopus citations


    Background: Carboxylesterase (CES) is predominantly responsible for the detoxification of a wide range of drugs and narcotics, and catalyze several reactions in cholesterol and fatty acid metabolism. Studies of the genetic and biochemical properties of primate CES may contribute to an improved understanding of human disease, including atherosclerosis, obesity and drug addiction, for which non-human primates serve as useful animal models. Methods: We cloned and sequenced baboon CES1 and CES2 and used in vitro and in silico methods to predict protein secondary and tertiary structures, and examined evolutionary relationships for these enzymes with other primate and mouse CES orthologs. Results and Conclusions: We found that baboon CES1 and CES2 proteins retained extensive similarity with human CES1 and CES2, shared key structural features reported for human CES1, and showed family specific sequences consistent with their multimeric and monomeric subunit structures respectively.

    Original languageEnglish (US)
    Pages (from-to)27-38
    Number of pages12
    JournalJournal of medical primatology
    Issue number1
    StatePublished - Jan 28 2009



    • 3-D structure
    • Amino acid sequence
    • cDNA sequence

    ASJC Scopus subject areas

    • Animal Science and Zoology
    • veterinary(all)

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