Molecular Cloning and Characterization of a Human Carboxylesterase Gene

doi:10.1006/geno.1993.1285

Genomics

Volume 17, Issue 1, July 1993, Pages 76-82

https://doi.org/10.1006/geno.1993.1285 Get rights and content

Abstract

A cDNA encoding human liver carboxylesterase and its gene were isolated. Nucleotide sequence analyses of the cDNA revealed that the predicted enzyme protein consists of 567 amino acids, including 18 amino acids of a putative signal peptide. Comparison of the deduced amino acid sequences of this enzyme with those of seven other carboxylesterases in various mammalian species, together with experimental data from several other laboratories, showed that these enzymes can be classified into three groups depending on the sequences at their carboxyl terminals and the presence or absence of one exon. A human carboxylesterase gene was found to span approximately 30 kb and to have 14 small exons. Alignments of this gene with those of human cholinesterase and rat cholesterol esterase indicated insertional sites at some introns and homologous amino acid sequences around them, although these genes have different numbers of exons. Thus the results supported the conclusion that these esterases evolved from a common ancestral gene.

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Citation Excerpt :
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Regular ArticleMolecular Cloning and Characterization of a Human Carboxylesterase Gene

Abstract

Regular Article
Molecular Cloning and Characterization of a Human Carboxylesterase Gene