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31P NMR studies with Cd(II) and Zn(II) chelates of adenosine 5'-O-(3-thiotriphosphate) (ATPgammaS) and the Cd(II) chelate of adenosine 5'-O-(2-thiotriphosphate) (ATPbetaS) indicate that these metal ions chelate to the sulfur atom of the thiophosphate group. Since Mg(II) chelates to oxygen of the thiophosphate group of diastereoisomer is equivalent to the configuration of the Cd(II) chelate of the opposite diastereoisomer. As a consequence, an inversion of the stereospecificity is observed when Cd(II) is substituted for Mg(II) in the phosphoryl transfer reactions catalyzed by yeast hexokinase and rabbit muscle pyruvate kinase. When Co(II) is the activating ion for yeast hexokinase with ATPbetaS as substrate, no stereospecificity is observed. Since the absolute configuration for the diastereoisomer of Co(III)(NH3)4ATP which is the active substrate for yeast hexokinase has been established by Cornelius and Cleland (Cornelius, R. D., and Cleland, W. W. (1978) Biochemistry, in press), the absolute stereochemistry of the Mg(II) complex of the B isomer of ATPbetaS is now established by its stereospecificity in the hexokinase reaction.
E K Jaffe, and
M Cohn
April 1976,
Biochemistry,
E K Jaffe, and
M Cohn
October 1979,
Biochemistry,
E K Jaffe, and
M Cohn
December 1993,
Biochemistry,
E K Jaffe, and
M Cohn
October 1978,
Proceedings of the National Academy of Sciences of the United States of America,
E K Jaffe, and
M Cohn
November 1987,
Biochemistry,
E K Jaffe, and
M Cohn
February 1980,
FEBS letters,
E K Jaffe, and
M Cohn
May 1978,
Proceedings of the National Academy of Sciences of the United States of America,
E K Jaffe, and
M Cohn
November 1970,
The Journal of biological chemistry,
E K Jaffe, and
M Cohn
July 1977,
Biochimica et biophysica acta,
E K Jaffe, and
M Cohn
April 1982,
Biochemistry,
