Methylcobalamin as a substrate at a separate site on Escherichia coli B N5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference32 articles.
1. Escherichia coli B N5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase: Activation with S-adenosyl-l-methionine and the mechanism for methyl group transfer
2. Spectrophotometric evidence for the formation of an Escherichia coli B B12s methyltransferase
3. Escherichia coli B 5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase: Catalysis by a reconstituted methyl-14C-cobalamin holoenzyme and the function of S-adenosyl-l-methionine
4. Escherichia coli B 5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase: Resolution and reconstitution of holoenzyme
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1. Cobalamin-Dependent Methionine Synthase from Escherichia coli: Structure and Reactivity;Vitamin B12and B12-Proteins;2007-12-21
2. The Chemistry of Vitamin B12and Related Inorganic Model Systems;Progress in Inorganic Chemistry;2007-03-09
3. Making Methionine: A Love Affair with Folate;Chemistry and Biology of Pteridines and Folates;2002
4. Acetyl Coenzyme A Synthesis from Unnatural Methylated Corrinoids: Requirement for “Base-Off” Coordination at Cobalt;Journal of the American Chemical Society;2001-02-01
5. Cobalamin-Dependent Methionine Synthase from Escherichia coli: Involvement of Zinc in Homocysteine Activation;Biochemistry;1997-12-01
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