Aminoacylase from Micrococcus agilis
Szwajcer, E.; Szewczuk, A.; Mordarski, M.
Acta Biochimica Polonica 27(2): 123-134
1980
ISSN/ISBN: 0001-527X PMID: 7435078 Document Number: 161350
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.