Glycine dehydrogenase (decarboxylating)

In enzymology, a glycine dehydrogenase (decarboxylating) (EC number|1.4.4.2) is an enzyme that catalyzes the chemical reaction

:glycine + H-protein-lipoyllysine $ightleftharpoons$ 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.

tructural studies

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

References

*
*
*

External links

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

Gene Ontology (GO) codes