ReviewJournal of Zhejiang University. Science. B2012
Role of vitamin B12 on methylmalonyl-CoA mutase activity.
Review in Journal of Zhejiang University. Science. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 123 citations in OpenAlex.
- A functional evaluation of anti-fatigue and exercise performance improvement following vitamin B complex supplementation in healthy humans, a randomized double-blind trial.International journal of medical sciences · 2023Trial
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- B-vitamin supplementation unlocks DHA production of Aurantiochytrium limacinum on molasses-based fermentation residue.Applied microbiology and biotechnology · 2026Article
- Dietary Vitamin B-9 and B-12 Deficiencies Alter Gut Homeostasis in Sprague-Dawley Rats.The Journal of nutrition · 2026Article
- Multi-omics analysis reveals breed-specific differences in the quality and nutrition of goose eggs.Food chemistry: X · 2026Article
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
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- Cobalt nanoparticles protect against endocrine disruption in response to multiple abiotic stresses in fish.Frontiers in immunology · 2026Article
- Recent research advances in the biological function and molecular mechanism of methylmalonic acid.Journal of Zhejiang University. Science. B · 2025Review
- A flow equilibrium model controlling cytoplasmic transition metal cation pools and preventing mis-metalation as exemplified for zinc homeostasis.Journal of bacteriology · 2025Review
- The infection cycle of the haloarchaeal virus HFTV1 is tightly regulated and strongly inhibits motility of its host.mSystems · 2025Article
- RICTOR regulates an interspecies crosstalk that influences longevity through a novel methionine cycle-mitophagy axis.bioRxiv : the preprint server for biology · 2025Article
- The effect of parenteral vitamin BScientific reports · 2025Article
- Article
- Lettuce fortification through vitamin BJournal of the science of food and agriculture · 2025Article
- The Arg108Cys Variant of Methylmalonyl-CoA Mutase: Clinical Implications for the Mexican Population Based on Molecular Dynamics and Docking.International journal of molecular sciences · 2025Article
- Transcriptomic and proteomic changes associated with cobalamin-dependent propionate production by the rumen bacteriummSystems · 2024Article
- Identification of Shemin pathway genes for tetrapyrrole biosynthesis in bacteriophage sequences from aquatic environments.Nature communications · 2024Article
- The metal-binding GTPases CobW2 and CobW3 are at the crossroads of zinc and cobalt homeostasis inJournal of bacteriology · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vitamin B(12) 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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.