PMID: 3207698Oct 4, 1988

Acceleration of cleavage of the carbon-cobalt bond of sterically hindered alkylcobalamins by binding to apoprotein of diol dehydrase

Biochemistry
T Toraya, A Ishida

Abstract

Cleavage of the C-Co bond of sterically hindered alkylcobalamins bearing neither an adenine moiety nor functional groups, such as isobutylcobalamin, neopentylcobalamin, and cyclohexylcobalamin, was markedly accelerated by their interaction with apoprotein of diol dehydrase, although these cobalamins do not function as coenzyme. Acceleration of the conversion of alkylcobalamins to enzyme-bound hydroxocobalamin was stoichiometric and obeyed first-order reaction kinetics. These results, together with strong competitive inhibition by these alkylcobalamins with respect to adenosylcobalamin, indicate that acceleration of the C-Co bond cleavage by the apoenzyme is due to labilization of their C-Co bond by binding to the active site of the enzyme. This labilization is considered to be caused by a steric distortion of the corrin ring which is induced by specific tight interaction of the cobalamin moiety with apoprotein. The importance of such a labilizing effect for activation of the C-Co bond of adenosylcobalamin in enzymatic reactions is discussed.

References

May 1, 1979·Archives of Biochemistry and Biophysics·A A PoznanskajaS Fukui
Jan 5, 1977·Journal of the American Chemical Society·J F Endicott, C J Ferraudi
Nov 1, 1985·Archives of Biochemistry and Biophysics·T Toraya
Mar 10, 1971·Journal of the American Chemical Society·M K EssenbergR H Abeles
Aug 1, 1980·Archives of Biochemistry and Biophysics·T Toraya, R H Abeles

Citations

Related Concepts

3',4'-anhydroadenosylcobalamin
Allosteric Site
Apoproteins
Vitreous Carbon
Cobalt
Cobamides
Photodegradation
Propanediol Dehydratase
Eritron

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