PMID: 16614482Apr 15, 2006Paper

Vitamin B12 and methionine synthesis: a critical review. Is nature's most beautiful cofactor misunderstood?

BioFactors
John I Toohey

Abstract

The mechanism by which Vitamin B12 prevents demyelination of nerve tissue is still not known. The evidence indicates that the critical site of B12 function in nerve tissue is in the enzyme, methionine synthase, in a system which requires S-adenosylmethionine. In recent years it has been recognized that S-adenosylmethionine gives rise to the deoxyadenosyl radical which catalyzes many reactions including the rearrangement of lysine to beta-lysine. Evidence is reviewed which suggests that there is an analogy between the two systems and that S-adenosyl methionine may catalyze a rearrangement of homocysteine on methionine synthase giving rise to iso- or beta-methionine. The rearranged product is readily degraded to CH3-SH, providing a mechanism for removing toxic homocysteine.

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Citations

Jul 22, 2010·Brain Research·Shingo MiyataMasaya Tohyama
Jan 24, 2014·Neural Plasticity·Ming ZhangHui Xu
Aug 26, 2014·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·John I Toohey, Arthur J L Cooper
Dec 18, 2013·Biochemical and Biophysical Research Communications·Michio OkamotoHideki Yoshikawa
Feb 10, 2012·Yonsei Medical Journal·Yang-Ki MinnIl-Nam Sunwoo
May 30, 2015·Nutrition Reviews·Doreen Gille, Alexandra Schmid
Oct 9, 2018·Current Medicinal Chemistry·Renata Kozyraki, Olivier Cases
Jun 19, 2021·Romanian Journal of Internal Medicine = Revue Roumaine De Médecine Interne·Adem KucukErdal Dogan

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