Literature DB >> 1292507

Cloning and sequence analyses of cDNAs encoding aminoacylase I from porcine kidney.

M Jakob1, Y E Miller, K H Röhm.   

Abstract

cDNAs encoding L-aminoacylase (EC 3.5.1.14) were isolated from a lambda gt10 cDNA library derived from porcine kidney mRNA. The clones were identified by hybridization with a synthetic oligonucleotide probe based on partial peptide sequences, or with a DNA probe encoding human aminoacylase I. Several cDNA clones isolated from the library had a length of about 1.3 kbp. They contained an open reading frame of 1218 bp encoding a polypeptide of 406 amino acids. The deduced amino-acid sequence contains the known peptide sequences; in addition, M(r) (45.3 kDa) and amino-acid composition of the predicted polypeptide match those of purified aminoacylase I. Data base searches did not reveal significant sequence homologies of aminoacylase I with other well-known amidases.

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Year:  1992        PMID: 1292507     DOI: 10.1515/bchm3.1992.373.2.1227

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  3 in total

1.  Aminoacylase I from porcine kidney: identification and characterization of two major protein domains.

Authors:  G J Palm; K H Röhm
Journal:  J Protein Chem       Date:  1995-05

2.  Dissecting the pretransitional conformational changes in aminoacylase I thermal denaturation.

Authors:  Jing-Tan Su; Sung-Hye Kim; Yong-Bin Yan
Journal:  Biophys J       Date:  2006-10-27       Impact factor: 4.033

3.  Gene cloning, sequence analysis, purification, and characterization of a thermostable aminoacylase from Bacillus stearothermophilus.

Authors:  V Sakanyan; L Desmarez; C Legrain; D Charlier; I Mett; A Kochikyan; A Savchenko; A Boyen; P Falmagne; A Pierard
Journal:  Appl Environ Microbiol       Date:  1993-11       Impact factor: 4.792

  3 in total

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