What is the role of the coenzyme vitamin B12 in the reaction catalyzed by Methylmalonyl CoA Mutase?
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.
Where does propionyl CoA come from?
Important sources of propionyl-CoA are the catabolism of isoleucine, valine, methionine, and threonine (Chapter 17). Cholesterol side chain oxidation also yields propionyl-CoA. Thus, propionyl-CoA is derived from the catabolism of lipids and proteins.
What does Methylmalonyl CoA Mutase do?
Methylmalonyl CoA mutase is responsible for a particular step in the breakdown of several protein building blocks (amino acids), specifically isoleucine, methionine, threonine, and valine. The enzyme also helps break down certain types of fats (lipids) and cholesterol.
What is Methylmalonyl-CoA Mutase deficiency?
Methylmalonyl-Coenzyme A mutase deficiency (MCM deficiency) is a type of methylmalonic acidemia caused by having too little methylmalonyl-CoA mutase. Methylmalonyl-CoA mutase (MCM) is one of the special proteins (enzymes) needed to breakdown certain amino acids found in the food we eat.
Why is propionyl-CoA toxic?
Bacterial metabolism Accumulation of propionyl-CoA can lead to toxic effects. tuberculosisis, is that since propionyl-CoA is produced by beta odd chain fatty acid catabolism, the methylcitrate cycle is activated subsequently to negate any potential toxicity, acting as a buffering mechanism.
What form of cobalamin is required for the enzyme Methylmalonyl-CoA Mutase?
MCM catalyzes the reversible isomerisation of l‐methylmalonyl‐CoA to succinyl‐CoA, requiring cobalamin (vitamin B12) in the form of adenosylcobalamin (AdoCbl) as a cofactor.
Is Phosphoglycerate Mutase an isomerase?
PGM is an isomerase enzyme, effectively transferring a phosphate group (PO43−) from the C-3 carbon of 3-phosphoglycerate to the C-2 carbon forming 2-phosphoglycerate.
Which is enzyme catalyzes the isomerization of methylmalonyl-CoA?
This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans. Mutations in MUT gene may lead to various types of methylmalonic aciduria. MCM was first identified in rat liver and sheep kidney in 1955. In its latent form, it is 750 amino acids in length.
What kind of enzyme is methylmalonyl CoA mutase?
Methylmalonyl-CoA mutase is a member of the isomerase subfamily of adenosylcobalamin-dependent enzymes. Furthermore, it is classified as class I, as it is a ‘DMB-off’/’His-on’ enzyme.
What is the function of methylmalonyl CoA in humans?
MMUT methylmalonyl-CoA mutase [ (human)] Summary. This gene encodes the mitochondrial enzyme methylmalonyl Coenzyme A mutase. In humans, the product of this gene is a vitamin B12-dependent enzyme which catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, while in other species this enzyme may have different functions.