Cloning and sequence analyses of cDNAs encoding aminoacylase I from porcine kidney.
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.
Jakob
M
M
Institut für Physiologische Chemie, Universität Marburg.
Miller
Y E
YE
Röhm
K H
KH
D000581:Amidohydrolases / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis*; D007668:Kidney / Q000201:enzymology*; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D013552:Swine
D000596:Amino Acids; D004247:DNA; D000581:Amidohydrolases; C019672:aminoacylase I