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methylmalonyl Coenzyme A mutase; succinyl CoA mutase; methylmalonyl CoA isomerase (MUT, MCM)

Function: - mitochondrial vitamin B12-dependent enzyme - role in degradation of several amino acids, odd-chain fatty acids & cholesterol via propionyl-CoA to the tricarboxylic acid cycle - converts methylmalonate (methylmalonyl CoA) to succinate (succinyl CoA) which enters the citric acid cycle - in humans, methylmalonyl CoA mutase is involved in the metabolism of propionate formed from catabolism of odd-chain fatty acids, cholesterol & the amino acids methionine & isoleucine (via propionyl CoA) - MCM has different functions in other species Cofactor: adenosylcobalamin - the 1st step is the homolytic cleavage of the carbon-cobalt bond in vitamin B12 generating cobalamin (Co+2) & 5'deoxyadenosyl (carbon) radical -CH2* - the 5'deoxyadenosyl radical -CH2* abstracts a hydrogen atom from the substrate generating 5'deoxyadenosine -(CH3) & a substrate radical which undergoes intramolecular rearrangement to form the product radical - the product radical then abstracts a hydrogen from 5'deoxyadenosine to form product (succinyl CoA) & the 5'deoxyadenosyl (carbon) radical -CH2* which in turn combines with cobalamin (Co+2) to regenerate adenosylcobalamin Structure: - homodimer - belongs to the methylmalonyl-CoA mutase family - contains 1 B12-binding domain Compartment: mitochondrial matrix Pathology: - defects in MUT are the cause of methylmalonicaciduria

Interactions

molecular events

Related

adenosylcobalamin; cobamamide (vitamin B12) methylmalonate; methylmalonic acid (MMA) succinate; succinic acid succinyl coenzyme A

General

mitochondrial protein mutase oligomerizing protein

Properties

CONFIGURATION: dimer SIZE: entity length = 750 aa MW = 83 kD COMPARTMENT: mitochondrial matrix MOTIF: active site MOTIF: cofactor-binding site [614-746] FOR-BINDING-OF: adenosylcobalamin

Database Correlations

OMIM 251000 UniProt P22033 PFAM correlations Entrez Gene 4594 Kegg hsa:4594 ENZYME 5.4.99.2

References

  1. Biochemistry, L. Stryer, WH Freeman & Co, New York, 1988 pg 508
  2. UniProt :accession P22033
  3. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=MUT
  4. Wikipedia: methylmalonyl coenzyme A mutase http://en.wikipedia.org/wiki/methylmalonyl_Coenzyme_A_mutase