Group I pyridoxal-dependent decarboxylases

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Glycine cleavage system P-protein
PDB 1wyt EBI.jpg
crystal structure of glycine decarboxylase (p-protein) of the glycine cleavage system, in apo form
Symbol GDC-P
Pfam PF02347
Pfam clan CL0061
InterPro IPR020580

In molecular biology, the group I pyridoxal-dependent decarboxylases, also known as glycine cleavage system P-proteins, are a family of enzymes consisting of glycine cleavage system P-proteins (glycine dehydrogenase (decarboxylating)) EC from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex (GDC) also annotated as glycine cleavage system or glycine synthase. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor, carbon dioxide is released and the remaining methylamin moiety is then transferred to the lipoamide cofactor of the H protein. GDC consists of four proteins P, H, L and T.[1]

Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group I comprises glycine decarboxylases.[2]

See also[edit]


  1. ^ Stauffer LT, Fogarty SJ, Stauffer GV (May 1994). "Characterization of the Escherichia coli gcv operon". Gene. 142 (1): 17–22. doi:10.1016/0378-1119(94)90349-2. PMID 8181752. 
  2. ^ Sandmeier E, Hale TI, Christen P (May 1994). "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases". Eur. J. Biochem. 221 (3): 997–1002. doi:10.1111/j.1432-1033.1994.tb18816.x. PMID 8181483. 

This article incorporates text from the public domain Pfam and InterPro IPR020580