title: [Isolation and various properties of alpha-aminocaprolactam hydrolase from Klebsiella aerogenes].
abstract: L-alpha-aminocaprolactam hydrolase possessing the L lysine amidase activity was isolated from Klebsiella aerogenes and purified. The procedure of enzymes purification included cell destruction on USDN-I, fractionation by ammonium sulfate, gel chromatography on G-200. The preparation of the purified enzyme possessed specific activity of 50 mumol of lysin per 1 mg of protein per hour. Km was 2.6 mM in case of phosphate buffer (ph 7.2) for I-alpha-aminocaprolactam. Besides L-alpha-aminocaprolactam the enzyme hydrolyses lysine amide, leucine amide tryptophanamide. Magnesium ions are necessary for manifestation of catalytic activity of the enzyme.
authors.forename: T A
authors.initials: TA
authors.lastname: Kliment'eva
authors.forename: A K
authors.initials: AK
authors.lastname: Brel'
mesh_terms: D000581:Amidohydrolases / Q000302:isolation & purification* / Q000378:metabolism; D002384:Catalysis; D002413:Cations, Divalent; D002850:Chromatography, Gel; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D008274:Magnesium / Q000378:metabolism; D008345:Manganese / Q000378:metabolism
chemical_list: D002413:Cations, Divalent; D008345:Manganese; D000581:Amidohydrolases; C040276:lysine amidase; C076449:L-lysine-lactamase; D008274:Magnesium
vernacular_title: Vydelenie i nekotorye svoĭstva alpha-aminokaprolaktamgidrolazy iz Klebsiella aerogenes.