| EC |
2.7.1.157 |
| Accepted name: |
N-acetylgalactosamine kinase |
| Reaction: |
ATP + N-acetyl-α-D-galactosamine = ADP + N-acetyl-α-D-galactosamine 1-phosphate |
| Other name(s): |
GALK2; GK2; GalNAc kinase; N-acetylgalactosamine (GalNAc)-1-phosphate kinase; ATP:N-acetyl-D-galactosamine 1-phosphotransferase |
| Systematic name: |
ATP:N-acetyl-α-D-galactosamine 1-phosphotransferase |
| Comments: |
The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose [2]. Requires Mg2+, Mn2+ or Co2+ for activity, with Mg2+ resulting in by far the greatest stimulation of enzyme activity. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Pastuszak, I., Drake, R. and Elbein, A.D. Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation. J. Biol. Chem. 271 (1999) 20776–20782. [DOI] [PMID: 8702831] |
| 2. |
Pastuszak, I., O'Donnell, J. and Elbein, A.D. Identification of the GalNAc kinase amino acid sequence. J. Biol. Chem. 271 (1996) 23653–23656. [DOI] [PMID: 8798585] |
| 3. |
Thoden, J.B. and Holden, H.M. The molecular architecture of human N-acetylgalactosamine kinase. J. Biol. Chem. 280 (2005) 32784–32791. [DOI] [PMID: 16006554] |
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| [EC 2.7.1.157 created 2005] |
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