title: [Various physico-chemical and kinetic properties of metalloproteinase from bacteriolytic lysoamidase preparation].
abstract: The amino acid composition of metalloproteinase was determined. It was shown that the enzyme is made up of four cysteinyl residues which makes it distinct from other known neutral metalloproteinases from Bacillus brevis, Bacillus subtilis and thermolysine that are devoid of cysteinyl residues. The inhibiting effect of amino acids and some di- and tripeptides on the metalloproteinase activity was studied. The pH-dependence of the Michaelis constant (pKm0) of native and diethylpyrocarbonate-modified metalloproteinase (pKm) suggests that the enzyme active center contains two imidazole groups of histidine with pK alpha 1 = 6.75 +/- 0.1 and pK alpha 2 = 5.4 +/- 0.1. The experimental results are compared to those obtained with other microbial metalloproteinases.
authors.forename: V I
authors.initials: VI
authors.lastname: Krupianko
authors.forename: A I
authors.initials: AI
authors.lastname: Severin
authors.forename: A I
authors.initials: AI
authors.lastname: Kudriavtseva
authors.forename: A Ia
authors.initials: AIa
authors.lastname: Valiakhmetov
authors.forename: A G
authors.initials: AG
authors.lastname: Kozlovskiĭ
authors.forename: I S
authors.initials: IS
authors.lastname: Kulaev
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000494:pharmacology; D007700:Kinetics; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000494:pharmacology; D011480:Protease Inhibitors; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000596:Amino Acids; D010455:Peptides; D011480:Protease Inhibitors; C060332:lysoamidase; D010447:Peptide Hydrolases; D008666:Metalloendopeptidases
vernacular_title: Nekotorye fiziko-khimicheskie i kineticheskie svoĭstva metalloproteinazy bakterioliticheskogo preparata lizoamidazy.