[Isolation and various properties of alpha-aminocaprolactam hydrolase from Klebsiella aerogenes]. / Vydelenie i nekotorye svoistva alpha-aminokaprolaktamgidrolazy iz Klebsiella aerogenes.

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.

[Catabolism of amino acids in bacteria of the genus Klebsiella]. / Katabolizm aminokislot u bakterii roda Klebsiella.

Propagation and activity level of 18 enzymes catalyzing deamination reactions of dicarboxylic and oxyamino acids and enzymes of amino acid reamination and amino acid N-acyl-derivatives' deacylation have been studied in Klebsiella bacteria. Klebsiella the most actively utilizes serin, threonine, aspartic and glutamic acids and aromatic amino acids. The first three amino acids are utilized by deamination, aromatic acids- in aminotransferase reaction with alpha-ketoglutaric acid, glutamic acid--by deamination and decarboxylation. Besides, Klebsiella actively deacylates N-acyl-derivatives of amino acids.

[Activity and properties of L-lysine amidase in Salmonella strains]. / Aktivnost' i svoistva L-lizinamidazy u shtammov roda Salmonella.

Distribution, activity level and properties of alpha-lysinamidase have been studied in Salmonella strains. The Km value for L-lysinamide was calculated to be 4.2 mM and for L-alpha-aminocaprolactame--5.1 mM. This enzyme, parallel with lysinamide, catalyzes hydrolysis of alpha-aminocaprolactam and leucinamide. Asparagine, glutamine, caprolactam, triptophanamide were not lysinamidase substrates.

[Isolation and properties of aminocaprolactam hydrolase from Providencia alcalifaciens]. / Poluchenie i svoistva aminokaprolaktamgidrolazy iz Providencia alcalifaciens.

L-alpha-aminocaprolactam hydrolase possessing the L-lysinamidase activity was isolated and purified from Providencia alcalifaciens. The purification procedure of enzymes included cell destruction on USDL-1, fractionation by ammonium sulfate, gel-chromatography on G-100, ion exchange chromatography on DEAE-cellulose. The purification resulted in a homogeneous enzyme which possessed the both activities. The enzyme molecular weight (180 kDa) was estimated by gel chromatography on Sephadex G-200. Km was 3.5 mM in the phosphate buffer (pH 7.2). L-alpha-aminocaprolactam hydrolase and L-lysinamidase may be related to metal-dependent enzymes requiring Mg++.