Michaelis-Menten Kinetics for Determining Enzymatic Activity of Lysostaphin

V. I. Surovtsev^*, T. V. Fedorov, and M. A. Borozdina

State Research Center of Applied Microbiology, Ministry of Public Health of Russian Federation, Obolensk 142279, Moscow Region, Russia; fax: (0967) 36-0010; E-mail: tfedorov@yandex.ru

^* To whom correspondence should be addressed.

Received August 5, 2003; Revision received November 10, 2003

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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.

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KEY WORDS: lysostaphin, lysis, immobilized substrate, Michaelis-Menten equation

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