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Literature DB >> 1959668

The nucleotide and deduced amino acid sequences of porcine liver proline- beta-naphthylamidase. Evidence for the identity with carboxylesterase.

M Matsushima¹, H Inoue, M Ichinose, S Tsukada, K Miki, K Kurokawa, T Takahashi, K Takahashi.

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.

Entities: Chemical Gene

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Year: 1991 PMID： 1959668 DOI： 10.1016/0014-5793(91)81147-z

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

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The nucleotide and deduced amino acid sequences of porcine liver proline- beta-naphthylamidase. Evidence for the identity with carboxylesterase.

1. Cloning and expression of a cDNA encoding a hepatic microsomal lipase that mobilizes stored triacylglycerol.

2. Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans.

3. Molecular cloning and characterization of a novel carboxylesterase-like protein that is physiologically present at high concentrations in the urine of domestic cats (Felis catus).

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