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Journal of Zhejiang University SCIENCE B 2012 Vol.13 No.6 P.423-437


Role of vitamin B12 on methylmalonyl-CoA mutase activity

Author(s):  Tshiko Takahashi-Iiguez, Enrique Garca-Hernandez, Roberto Arregun-Espinosa, Mara Elena Flores

Affiliation(s):  Department of Molecular Biology and Biotechnology, Institute of Biomedical Research, National Autonomous University of Mexico, D.F. 04510, Mexico; more

Corresponding email(s):   toshikoti@biomedicas.unam.mx

Key Words:  Vitamin B12, Methylmalonyl-CoA mutase (MCM), MMAA, MeaB, Methylmalonic academia (MMA), Protectase, Reactivase

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Tshiko Takahashi-Iiguez, Enrique Garca-Hernandez, Roberto Arregun-Espinosa, Mara Elena Flores. Role of vitamin B12 on methylmalonyl-CoA mutase activity[J]. Journal of Zhejiang University Science B, 2012, 13(6): 423-437.

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journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

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%T Role of vitamin B12 on methylmalonyl-CoA mutase activity
%A Tshiko Takahashi-Iiguez
%A Enrique Garca-Hernandez
%A Roberto Arregun-Espinosa
%A Mara Elena Flores
%J Journal of Zhejiang University SCIENCE B
%V 13
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%D 2012
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1100329

T1 - Role of vitamin B12 on methylmalonyl-CoA mutase activity
A1 - Tshiko Takahashi-Iiguez
A1 - Enrique Garca-Hernandez
A1 - Roberto Arregun-Espinosa
A1 - Mara Elena Flores
J0 - Journal of Zhejiang University Science B
VL - 13
IS - 6
SP - 423
EP - 437
%@ 1673-1581
Y1 - 2012
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1100329

vitamin B12 is an organometallic compound with important metabolic derivatives that act as cofactors of certain enzymes, which have been grouped into three subfamilies depending on their cofactors. Among them, methylmalonyl-CoA mutase (MCM) has been extensively studied. This enzyme catalyzes the reversible isomerization of L-methylmalonyl-CoA to succinyl-CoA using adenosylcobalamin (AdoCbl) as a cofactor participating in the generation of radicals that allow isomerization of the substrate. The crystal structure of MCM determined in Propionibacterium freudenreichii var. shermanii has helped to elucidate the role of this cofactor AdoCbl in the reaction to specify the mechanism by which radicals are generated from the coenzyme and to clarify the interactions between the enzyme, coenzyme, and substrate. The existence of human methylmalonic acidemia (MMA) due to the presence of mutations in MCM shows the importance of its role in metabolism. The recent crystallization of the human MCM has shown that despite being similar to the bacterial protein, there are significant differences in the structural organization of the two proteins. Recent studies have identified the involvement of an accessory protein called MMAA, which interacts with MCM to prevent MCM’s inactivation or acts as a chaperone to promote regeneration of inactivated enzyme. The interdisciplinary studies using this protein as a model in different organisms have helped to elucidate the mechanism of action of this isomerase, the impact of mutations at a functional level and their repercussion in the development and progression of MMA in humans. It is still necessary to study the mechanisms involved in more detail using new methods.

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Lian-Sheng Ma@BPG<l.s.ma@wjgnet.com>

2012-07-05 03:49:40

We discovered that your Role of vitamin B12 on methylmalonyl-CoA mutase activity is novel interesting.

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