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Michaelis-menten kinetics for determining enzymatic activity of lysostaphin.

The rate of lysostaphin-catalyzed lysis of staphylococci follows the Michaelis-Menten equation at [E](0) << [S](0), i.e., the activity of the enzyme is proportional to its concentration. This equation is proposed for determining the specific activity of lysostaphin. The apparent activation energy of hydrolysis of pentaglycine bridges in Staphylococcus peptidoglycan is 77.9 kJ/ mol.[1]


  1. Michaelis-menten kinetics for determining enzymatic activity of lysostaphin. Surovtsev, V.I., Fedorov, T.V., Borozdina, M.A. Biochemistry Mosc. (2004) [Pubmed]
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