| Literature DB >> 1292507 |
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.Entities:
Mesh:
Substances:
Year: 1992 PMID: 1292507 DOI: 10.1515/bchm3.1992.373.2.1227
Source DB: PubMed Journal: Biol Chem Hoppe Seyler ISSN: 0177-3593