N-acetylgalactosamine kinase
Appearance
N-acetylgalactosamine kinase | |||||||||
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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 | ||||||||
PDBstructures | RCSB PDBPDBePDBsum | ||||||||
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Inenzymology,aN-acetylgalactosamine kinase(EC2.7.1.157) is anenzymethatcatalyzesthechemical reaction
- ATP + N-acetyl-D-galactosamineADP + N-acetyl- Alpha -D-galactosamine 1-phosphate
Thus, the twosubstratesof this enzyme areATPandN-acetyl-D-galactosamine,whereas its twoproductsareADPandN-acetyl- Alpha -D-galactosamine 1-phosphate.
This enzyme belongs to the family oftransferases,specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Thesystematic nameof this enzyme class isATP:N-acetyl-D-galactosamine 1-phosphotransferase.Other names in common use includeGALK2,GK2,GalNAc kinase,andN-acetylgalactosamine (GalNAc)-1-phosphate kinase.
References
[edit]- 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.PMID8702831.
- 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.PMID8798585.
- 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.PMID16006554.