Cloning and sequence analysis of a hamster liver cDNA encoding a novel putative carboxylesterase.
A full-length cDNA encoding for a putative carboxylesterase was isolated from a hamster liver cDNA library. The cDNA consisting of 1911 base pairs contained an open reading frame of 1683 base pairs encoding for a polypeptide of 561 amino-acid residues, including 27 N-terminal amino-acid residues for signal peptide. The deduced amino-acid sequence of the cDNA is in 67% homology with the amino-acid sequence of rabbit form 2 carboxylesterase, which has not yet been cloned. It also had many structural features highly conserved among carboxylesterase isozymes.
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Department of Toxicology, Faculty of Pharmaceutical Sciences, Setsunan University, Osaka, Japan.
Isobe
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Takabatake
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Wang
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CY
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D006224:Cricetinae; D018076:DNA, Complementary / Q000737:chemistry* / Q000302:isolation & purification; D015723:Gene Library; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase