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The method of competitive labelling with [(3)H]acetic anhydride as the labelling reagent was used to determine the properties of the active-centre lysine residue of rabbit muscle aldolase. This residue is much less reactive than a normal exposed lysine residue towards this reagent, and its reactive properties did not parallel the pH-activity profile for aldolase. At higher pH values it became reactive, but this was shown to be due to disruption of the enzyme structure. The binding of the competitive inhibitor phosphate did not alter the reactive properties. It is concluded that the active-centre lysine has an apparent pK(a) greater than 11.5 and probably is made nucleophilic during the catalytic process, perhaps by proton abstraction.
P J Anderson, and
H Kaplan
November 1976,
European journal of biochemistry,
P J Anderson, and
H Kaplan
July 1972,
Proceedings of the National Academy of Sciences of the United States of America,
P J Anderson, and
H Kaplan
July 1970,
European journal of biochemistry,
P J Anderson, and
H Kaplan
January 1972,
Acta biochimica et biophysica; Academiae Scientiarum Hungaricae,
P J Anderson, and
H Kaplan
September 1994,
Protein science : a publication of the Protein Society,
P J Anderson, and
H Kaplan
November 1967,
Biochemical and biophysical research communications,
P J Anderson, and
H Kaplan
March 1974,
Biochemical and biophysical research communications,
P J Anderson, and
H Kaplan
December 1972,
FEBS letters,
P J Anderson, and
H Kaplan
June 1975,
Archives of biochemistry and biophysics,
P J Anderson, and
H Kaplan
March 1974,
Science (New York, N.Y.),
