title: Molecular cloning and nucleotide sequence of the complementary DNA for penicillolysin gene, plnC, and 18 kDa metalloendopeptidase gene from Penicillium citrinum.
abstract: A full-length cDNA encoding the penicillolysin, an 18 kDa metalloendopeptidase from Penicillium citrinum, was cloned. Analysis of the 1284 base pair nucleotide sequence of the cDNA revealed a single open reading frame coding for 351 amino acid residues. The coding region of penicillolysin gene, plnC, occupies 1053 base pairs of the cDNA. The sequence consists of a putative 19-residue signal sequence, a 155-residue propeptide segment, and the 177-residues of penicillolysin with a molecular weight of 18,529. The deduced primary structure of penicillolysin is unique and the enzyme is a member of a new metalloendopeptidase family. Two histidine residues, His-128 and His-132, and glutamic acid residue, Glu-65 in penicillolysin were assumed to correspond to zinc ligands in the homologous thermolysin.
authors.affiliation: Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Matsumoto
authors.forename: M
authors.initials: M
authors.lastname: Yamaguchi
authors.forename: E
authors.initials: E
authors.lastname: Ichishima
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry; D005798:Genes, Bacterial; D008666:Metalloendopeptidases / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D015345:Oligonucleotide Probes; D016366:Open Reading Frames; D010407:Penicillium / Q000201:enzymology* / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
chemical_list: D018076:DNA, Complementary; D015345:Oligonucleotide Probes; D008666:Metalloendopeptidases; C083042:penicillolysin