The primary structure of porcine aminoacylase 1 deduced from cDNA sequence.

摘要: A cDNA encoding the complete amino acid sequence of aminoacylase 1 (N-acylamino aminohydrolase, ACY-1) [EC 3.5.1.14], a dimeric metalloprotein having two Zn2+ in molecule, which catalyzes deacylation N-acylated L-amino acids except L-aspartic acid, has been isolated from porcine kidney lambda gt10 library and sequenced. From analysis N- C-terminal analyses purified protein, it is deduced that ACY-1 consists identical subunits (M(r) 45,260), each single chain 406 with acetylalanine at N-terminus. liver was also cloned. The nucleotide to for ACY-1. Northern blot suggested more highly expressed than liver. Comparison those other Zn2+-binding metalloenzymes showed no significant homologies either overall or consensus sequences metal binding sites. This indicates new type metalloprotein.