Aminoacylase from Micrococcus agilis.
Intracellular aminoacylase from Micrococcus agilis CCM 2131 was purified 430-fold with a 23% yield. The purified enzyme was homogeneous on polyacrylamide-gel electrophoresis and it smolecular weight was 58000. The enzyme hydrolysed stereospecifically a number of acylated L-amino acids. Its activity towards N-acetyl-L-phenylglycine was strongly inhibited by 1,10-phenanthroline, N-bromosuccinimide and mercaptoethanol, and was inhibited competitively by glycylglycine.
D000581:Amidohydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D000596:Amino Acids; D001974:Bromosuccinimide / Q000494:pharmacology; D003470:Culture Media; D046508:Culture Techniques; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005998:Glycine / Q000031:analogs & derivatives; D006033:Glycylglycine / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D008837:Micrococcus / Q000201:enzymology*; D010618:Phenanthrolines / Q000494:pharmacology
D000596:Amino Acids; D003470:Culture Media; D004791:Enzyme Inhibitors; D010618:Phenanthrolines; D006033:Glycylglycine; C027177:N-acetylphenylglycine; D008623:Mercaptoethanol; D000581:Amidohydrolases; C019672:aminoacylase I; D001974:Bromosuccinimide; D005998:Glycine