Open AccessOn the Mechanism of Action of Vitamin B 12 . Model Studies. Thermal Rearrangement of Methyl 3,3-Dimethylglycidate to Methyl Levulinate
Author(s) -
Paul Dowd,
Christopher S. Nakagawa
Publication year - 1972
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.5.1173
Subject(s) - mutase , mechanism of action , enzyme , chemistry , mechanism (biology) , stereochemistry , methyl group , cofactor , biochemistry , organic chemistry , philosophy , epistemology , in vitro , alkyl
The discovery that methyl 3,3-dimethylglycidate rearranges to methyl levulinate on heating is discussed in terms of its possible consequences for the mechanism of action of the coenzyme B12 -dependent enzymes: methylmalonyl-CoA mutase (EC 5.4.99.2), glutamate mutase (EC 5.4.99.1), anda -methyleneglutarate mutase. It is also suggested that the proposed mechanism may provide a unifying link between the mechanism of action of the above enzymes and that of the coenzyme B12 -dependent dioldehydrase and related enzymes.