-transparent.png){kind=logo}
Rabbit muscle aldolase was found to be inactivated in a slow, reversible manner by D-erythrulose 1-phosphate. This compound combined rapidly and reversibly with the enzyme to form an initial complex, which then only slowly (ki = 0.28 min-1) converted to a kinetically more stable form. This stable enzyme-ligand form was inactive toward the normal substrate of aldolase, fructose 1,6-bisphosphate. The inactive enzyme-ligand complex, however, could be decomposed (kr = 0.0041 min-1) to yield active enzyme once again by incubation in a solution devoid of D-erythrulose 1-phosphate.
Related Publications
E L Ferroni, and
E T Harper, and
W K Fife
November 1954,
The Journal of biological chemistry,
E L Ferroni, and
E T Harper, and
W K Fife
July 1967,
Archives of biochemistry and biophysics,
E L Ferroni, and
E T Harper, and
W K Fife
April 1997,
The Biochemical journal,
E L Ferroni, and
E T Harper, and
W K Fife
June 1976,
European journal of biochemistry,
E L Ferroni, and
E T Harper, and
W K Fife
January 1963,
The Journal of biological chemistry,
E L Ferroni, and
E T Harper, and
W K Fife
May 1960,
Biochimica et biophysica acta,
E L Ferroni, and
E T Harper, and
W K Fife
June 1975,
FEBS letters,
E L Ferroni, and
E T Harper, and
W K Fife
January 1969,
Acta biochimica et biophysica; Academiae Scientiarum Hungaricae,
E L Ferroni, and
E T Harper, and
W K Fife
November 1968,
Archives of biochemistry and biophysics,
E L Ferroni, and
E T Harper, and
W K Fife
June 1973,
Archives of biochemistry and biophysics,
