Glycine dehydrogenase (decarboxylating)

In enzymology, a glycine dehydrogenase (decarboxylating) is an enzyme that catalyzes the chemical reaction


 * glycine + H-protein-lipoyllysine $$\rightleftharpoons$$ H-protein-S-aminomethyldihydrolipoyllysine + CO2

Thus, the two substrates of this enzyme are glycine and H-protein-lipoyllysine, whereas its two products are H-protein-S-aminomethyldihydrolipoyllysine and CO2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating, acceptor-amino-methylating). Other names in common use include P-protein, glycine decarboxylase, glycine-cleavage complex, glycine:lipoylprotein oxidoreductase (decarboxylating and, acceptor-aminomethylating), and protein P1. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes, , , , and.