|Jmol-3D images||Image 1|
|Molar mass||823.60 g/mol|
| (what is: / ?)
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Metabolism in animals 
There are several different ways in which it is formed:
- It is formed as a product of beta-oxidation of odd-chain fatty acids.
- It is also a product of metabolism of isoleucine and valine.
- It is a product of alpha-ketobutyric acid, which in turn is a product of digestion of threonine and methionine.
Metabolic fate 
(R)-Methylmalonyl-CoA is converted to succinyl-CoA, an intermediate in the tricarboxylic acid cycle, by methylmalonyl-CoA mutase, an enzyme requiring cobalamin to catalyze the carbon-carbon bond migration.
The methylmalonyl-CoA mutase mechanism begins with the cleavage of the bond between the 5' CH2- of 5'-deoxyadenosyl and the cobalt, which is in its 3+ oxidation state (III), which produces a 5'-deoxyadenosyl radical and cabalamin in the reduced Co(II) oxidation state.
Next, this radical abstracts a hydrogen atom from the methyl group of methylmalonyl-CoA, which generates a methylmalonyl-CoA radical. It is believed that this radical forms a carbon-cobalt bond to the coenzyme, which is then followed by the rearrangement of the substrate's carbon skeleton, thus producing a succinyl-CoA radical. This radical then goes on to abstract a hydrogen from the previously produced 5'-deoxyadenosine, again creating a deoxyadenosyl radical, which attacks the coenzyme to reform the initial complex.
A defect in methylmalonyl-CoA mutase enzyme results in methylmalonic aciduria, a dangerous disorder that causes a lowering of blood pH.
Metabolism in plants and insects 
In plants and insects propionyl-CoA is metabolized to acetate in a very different way, similar to beta-oxidation.
This is metabolized with loss of carbon 1 of 3-hydroxypropionyl-CoA as carbon dioxide, while carbon 3 becomes carbon 1 of acetate.
- Halarnkar P, Blomquist G (1989). "Comparative aspects of propionate metabolism". Comp. Biochem. Physiol., B 92 (2): 227–31. doi:10.1016/0305-0491(89)90270-8. PMID 2647392.