Methylmalonyl-CoA mutase
| Human L-methylmalonyl-CoA mutase | ||
|---|---|---|
|
||
| Belt model according to PDB 3BIC | ||
| Properties of human protein | ||
| Mass / length primary structure | 718 amino acids | |
| Secondary to quaternary structure | Homodimer | |
| Cofactor | Adenosylcobalamin (vitamin B12) | |
| Identifier | ||
| Gene names | MCM ; COURAGE; MUTA | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 5.4.99.2 , mutase | |
| Response type | Isomerization | |
| Substrate | L-methylmalonyl-CoA | |
| Products | Succinyl-CoA | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 4594 | 17850 |
| Ensemble | ENSG00000146085 | ENSMUSG00000023921 |
| UniProt | P22033 | P16332 |
| Refseq (mRNA) | NM_000255 | NM_008650 |
| Refseq (protein) | NP_000246 | NP_032676 |
| Gene locus | Chr 6: 49.43 - 49.46 Mb | Chr 17: 40.93 - 40.96 Mb |
| PubMed search | 4594 |
17850
|
Methylmalonyl-CoA mutase (MCM) is an enzyme that is required in the metabolism of all living things to break down several amino acids , fatty acids and cholesterol . MCM catalyzes the reaction step from L- methylmalonyl-CoA to succinyl-CoA , a rearrangement ; therefore MCM belongs to the isomerases . In some bacteria , it is part of the structure of propionate from citric acid cycle intermediates. In eukaryotes , MCM is localized in the mitochondria . MCM deficiency leads to hereditary and often fatal methylmalonic acidemia in humans .
Catalyzed reaction
L-methylmalonyl-CoA is rearranged to succinyl-CoA . In bacteria, the reaction takes place in the opposite direction.
The coenzyme of the reaction is vitamin B 12 ( cobalamin ).
Individual evidence
Web links
Wikibooks: Biochemistry and Pathobiochemistry: Degradation of Propionyl-CoA - Learning and Teaching Materials
