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

Baboon carboxylesterases 1 and 2: sequences, structures and phylogenetic relationships with human and other primate carboxylesterases.
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DOI:
10.1111/j.1600-0684.2008.00315.x
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发表时间:
2009-02
影响因子:
0.7
通讯作者:
Cox LA
Cox LA
中科院分区:
农林科学4区
文献类型:
--
作者:
Holmes RS;Glenn JP;VandeBerg JL;Cox LA

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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. 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. 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.
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