Abstract
A cDNA clone for porcine liver proline-beta-naphthylamidase was isolated and sequenced. The deduced amino acid sequence of 567 residues was highly homologous with those of carboxylesterases (EC 3.1.1.1) previously reported for other species. In addition, proline-beta-naphthylamidase purified from porcine liver was shown to have strong activity towards p-nitrophenylacetate, a representative substrate for carboxylesterases. These results suggest that proline-beta-naphthylamidase is identical with carboxylesterase.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Aminopeptidases / chemistry
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Aminopeptidases / genetics*
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Aminopeptidases / isolation & purification
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Animals
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Base Sequence
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Carboxylesterase
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Carboxylic Ester Hydrolases / genetics*
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DNA / isolation & purification
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Microsomes, Liver / enzymology*
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Molecular Sequence Data
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Rabbits
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Rats
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Sequence Homology, Nucleic Acid*
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Substrate Specificity
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Swine
Substances
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DNA
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Carboxylic Ester Hydrolases
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Carboxylesterase
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Aminopeptidases
Associated data
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GENBANK/S62644
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GENBANK/S62648
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GENBANK/S62652
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GENBANK/S66780
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GENBANK/X58803
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GENBANK/X63322
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GENBANK/X63323
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GENBANK/X63567
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GENBANK/X63568
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GENBANK/X63569