| N-acetylgalactosamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.157 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a N-acetylgalactosamine kinase (EC 2.7.1.157) is an enzyme that catalyzes the chemical reaction
- ATP + N-acetyl-D-galactosamine ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
Thus, the two substrates of this enzyme are ATP and N-acetyl-D-galactosamine, whereas its two products are ADP and N-acetyl-alpha-D-galactosamine 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-acetyl-D-galactosamine 1-phosphotransferase. Other names in common use include GALK2, GK2, GalNAc kinase, and N-acetylgalactosamine (GalNAc)-1-phosphate kinase.
References
- Pastuszak I, Drake R, Elbein AD (1996). "Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation". J. Biol. Chem. 271 (34): 20776–82. doi:10.1074/jbc.271.34.20776. PMID 8702831.
- Pastuszak I, O'Donnell J, Elbein AD (1996). "Identification of the GalNAc kinase amino acid sequence". J. Biol. Chem. 271 (39): 23653–6. doi:10.1074/jbc.271.39.23653. PMID 8798585.
- Thoden JB, Holden HM (2005). "The molecular architecture of human N-acetyl galactosamine kinase". J. Biol. Chem. 280 (38): 32784–91. doi:10.1074/jbc.M505730200. PMID 16006554.
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