The nucleotide and deduced amino acid sequences of porcine liver proline- beta-naphthylamidase. Evidence for the identity with carboxylesterase.
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.
Matsushima
M
M
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Inoue
H
H
Ichinose
M
M
Tsukada
S
S
Miki
K
K
Kurokawa
K
K
Takahashi
T
T
Takahashi
K
K
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D000818:Animals; D001483:Base Sequence; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000235:genetics*; D004247:DNA / Q000302:isolation & purification; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D011817:Rabbits; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity; D013552:Swine
D004247:DNA; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase; D000626:Aminopeptidases