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The kinetic details of the irreversible inactivation of the Escherichia coli RTEM beta-lactamase by clavulanic acid have been elucidated. Clavulanate is destroyed by the enzyme and simultaneously inhibits it by producing two catalytically inactive forms. One of these is transiently stable and decomposes to free enzyme (k = 3.8 X 10(-3) S-1), while the other corresponds to an irreversibly inactivated form. The transient complex is formed from the Michaelis complex at a rate (k approximately 3 X 10(-2) S-1) which is some threefold faster than the rate of formation of the irreversibly inactivated complex. The transient complex is, therefore, the principle enzyme form present after short time periods. In the presence of excess clavulanate, however, all the enzyme accumulates into the irreversibly inactivated form. The number of clavulanate turnovers that occur prior to complete enzyme inactivation is 115.
J Fisher, and
R L Charnas, and
J R Knowles
May 1981,
Biochemistry,
J Fisher, and
R L Charnas, and
J R Knowles
November 1984,
Biochemistry,
J Fisher, and
R L Charnas, and
J R Knowles
November 1984,
Biochemistry,
J Fisher, and
R L Charnas, and
J R Knowles
June 1981,
Biochemistry,
J Fisher, and
R L Charnas, and
J R Knowles
May 1981,
Biochemistry,
J Fisher, and
R L Charnas, and
J R Knowles
June 1982,
Biochemistry,
J Fisher, and
R L Charnas, and
J R Knowles
January 1985,
Drugs under experimental and clinical research,
J Fisher, and
R L Charnas, and
J R Knowles
October 1987,
The Biochemical journal,
J Fisher, and
R L Charnas, and
J R Knowles
October 1978,
Biochimica et biophysica acta,
J Fisher, and
R L Charnas, and
J R Knowles
April 1979,
The Biochemical journal,
