N-acetylgalactosamine kinase
| N-acetylgalactosamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.157 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
N-acetylgalactosamine kinase (EC 2.7.1.157) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from kidney converts N-acetylgalactosamine to N-acetyl-α-D-galactosamine 1-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2][3]
This enzyme is a transferase, specifically one 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.[4]
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.
- ↑ Enzyme 2.7.1.157 at KEGG Pathway Database.
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