Group I pyridoxal-dependent decarboxylases
| Glycine cleavage system P-protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of glycine decarboxylase (p-protein) of the glycine cleavage system, in apo form | |||||||||
| Identifiers | |||||||||
| 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 1.4.4.2 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 methylamine 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]- Group II pyridoxal-dependent decarboxylases
- Group III pyridoxal-dependent decarboxylases
- Group IV pyridoxal-dependent decarboxylases
References
[edit]- ^ 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.
- ^ 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.