Inactivation of dioldehydrase in the presence of a coenzyme-B12 analog
- 1 August 1980
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 203 (1) , 174-180
- https://doi.org/10.1016/0003-9861(80)90166-6
Abstract
No abstract availableThis publication has 24 references indexed in Scilit:
- Role of peripheral side chains of vitamin B12 coenzymes in the reaction catalyzed by dioldehydraseBiochemistry, 1979
- Mechanism of action of adenosylcobalamin: hydrogen transfer in the inactivation of diol dehydratase by glycerolBiochemistry, 1978
- A convenient synthesis of 5′-deoxyribonucleosidesCarbohydrate Research, 1977
- Mechanism of action of adenosylcobalamin: glycerol and other substrate analogs as substrates and inactivators for propanediol dehydratase - kinetics, stereospecificity, and mechanismBiochemistry, 1977
- Substrate specificity of coenzyme B12-dependent diol dehydrase: Glycerol as both a good substrate and a potent inactivatorBiochemical and Biophysical Research Communications, 1976
- Coenzyme B12 dependent propanediol dehydratase system. Nature of cobalamin binding and some properties of apoenzyme-coenzyme B12 analog complexesBiochemistry, 1972
- Propanediol dehydratase system. Role of monovalent cations in binding of vitamin B12 coenzyme or its analogs to apoenzymeBiochemistry, 1971
- Mechanism of hydrogen transfer in the coenzyme B12 dependent dioldehydrase reaction. IIJournal of the American Chemical Society, 1971
- Direct halogenation of sugar moiety of nucleosidesTetrahedron Letters, 1971
- The Circular Dichroism and Absorption Spectra of Some Vitamin B12 Derivatives*Biochemistry, 1967