Glycine dehydrogenase (decarboxylating)

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In enzymology, a glycine dehydrogenase (decarboxylating) (EC 1.4.4.2) 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.

Contents

[edit] Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1HPC, 1HTP, 1WYT, 1WYU, and 1WYV.

[edit] References

[edit] External links

The CAS registry number for this enzyme class is 37259-67-9.

[edit] Gene Ontology (GO) codes