Staphylococcal L-asparaginase: enzyme kinetics
Sobiś, M.; Mikucki, J.
Acta Microbiologica Polonica 40(3-4): 143-152
1991
ISSN/ISBN: 0137-1320 PMID: 1726615 Document Number: 382976
The ph optimum of purified staphylococcal L-asparaginase (EC 3.5.1.1) was found to be between 8.6 and 8.8. The temperature optimum was 30 degree -32 degree and the highest reaction rate occurred at 30 degree C. The K-M of the enzyme calculated from Lineweaver-Burk plot was 3.71 times 10-2M. Besides L-asparaginase, the substrate specificity of enzyme was restricted to N-alpha-acetyl-L-asparagine. D-asparagine, L-asparatic acid and D-glutamtic acid were competitive inhibitors. Hg-2+ and Cu-2+ cations strongly inhibited the enzyme while Na+ and K+ cations strongly stimulated activity. Two SH-groups could be detected after enzyme denaturation with guanidine.