Methylmalonyl-CoA decarboxylase

From Wikipedia, the free encyclopedia

In enzymology, a methylmalonyl-CoA decarboxylase (EC 7.2.4.3) is an enzyme that catalyzes the chemical reaction

(S)-methylmalonyl-CoA propanoyl-CoA + CO2

Hence, this enzyme has one substrate, (S)-methylmalonyl-CoA, and two products, propanoyl-CoA and CO2. Along with this reaction, this enzyme transports sodium cations across the membrane, creating a gradient which can be used for synthesis of ATP, hence its classification as a translocase.[1]

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming). Other names in common use include propionyl-CoA carboxylase, propionyl coenzyme A carboxylase, methylmalonyl-coenzyme A decarboxylase, (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect], and (S)-methylmalonyl-CoA carboxy-lyase. This enzyme participates in propanoate metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1EF8 and 1EF9.

References

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