Glycine cleavage (Saccharomyces cerevisiae)

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In eukaryotes the mitochondrial glycine cleavage complex (glycine decarboxylase complex) is a loosely-associated multienzyme complex that catalyzes the oxidative cleavage of glycine to carbon dioxide, ammonia, and a methylene group, in a multistep reaction (in [Nakai05]). The methylene group, carried by 5,10-methylenetetrahydropteroyl mono-L-glutamate, enters cellular one-carbon metabolism. In mammals, it is the primary pathway for glycine catabolism [Hampson83].

The glycine cleavage complex is composed of four different proteins: the P-protein ( EC 1.4.4.2, glycine dehydrogenase (aminomethyl-transferring)); the T-protein ( EC 2.1.2.10, aminomethyltransferase); the L-protein ( EC 1.8.1.4, dihydrolipoyl dehydrogenase); and the H-protein (lipoyl-carrier protein, a non-enzyme that contains a lipoyl group that interacts successively with the three other components of the complex during the enzymatic reactions. The L-protein (also known as the E3 component) also participates in the pyruvate decarboxylation to acetyl CoA, the 2-oxoglutarate decarboxylation to succinyl-CoA, and the 2-oxoisovalerate decarboxylation to isobutanoyl-CoA multienzyme systems.

Description from [YeastPathways](https://pathway.yeastgenome.org/).