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Glycine dehydrogenase (decarboxylating)
Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia
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Glycine decarboxylase also known as glycine cleavage system P protein or glycine dehydrogenase is an enzyme that in humans is encoded by the GLDC gene.[5][6][7]
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Reaction
Glycine decarboxylase (EC 1.4.4.2) is an enzyme that catalyzes the following chemical reaction:
- glycine + H-protein-lipoyllysine 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.[8]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a disulfide as acceptor. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
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Function
Glycine decarboxylase is the P-protein of the glycine cleavage system in eukaryotes. The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor. Carbon dioxide is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Degradation of glycine is brought about by the glycine cleavage system, which is composed of four mitochondrial protein components: P protein (a pyridoxal phosphate-dependent glycine decarboxylase), H protein (a lipoic acid-containing protein), T protein (a tetrahydrofolate-requiring enzyme), and L protein (a lipoamide dehydrogenase).[7]
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Clinical significance
Glycine encephalopathy is due to defects in GLDC or AMT of the glycine cleavage system.[7]
References
Further reading
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