MOLECULAR-CLONING AND NUCLEOTIDE-SEQUENCE OF THE COMPLEMENTARY-DNA FOR PENICILLOLYSIN GENE, PLNC, AN 18-KDA METALLOENDOPEPTIDASE GENE FROM PENICILLIUM-CITRINUM

A full-length cDNA encoding the penicillolysin, an 18 kDa metalloendop eptidase from Penicillium citrinum, was cloned. Analysis of the 1284 b ase pair nucleotide sequence of the cDNA revealed a single open readin g frame coding for 351 amino acid residues. The coding region of penic illolysin gene, plnC, occupies 1053 base pairs of the cDNA. The sequen ce consists of a putative 19-residue signal sequence, a 155-residue pr opeptide segment, and the 177-residues of penicillolysin with a molecu lar weight of 18529. The deduced primary structure of penicillolysin i s unique and the enzyme is a member of a new metalloendopeptidase fami ly. Two histidine residues, His-128 and His-132, and glutamic acid res idue, Glu-65 in penicillolysin were assumed to correspond to zinc liga nds in the homologous thermolysin.