| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.1 Phosphotransferases with an alcohol group as acceptor |
| ID: | 2.7.1.157 | ||
|---|---|---|---|
| Description: | N-acetylgalactosamine kinase. | ||
| Alternative Name: |
N-acetylgalactosamine (GalNAc)-1-phosphate kinase. GK2. GalNAc kinase. GALK2. | ||
| Prosite: | PDOC00545; PDOC00099; | ||
| PDB: |
|
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| Cath: | 1.20.1440.340; 3.30.230.10; 3.30.70.3170; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.7.1.157 |
| BRENDA Enzyme Link: | BRENDA 2.7.1.157 |
| KEGG Enzyme Link: | KEGG2.7.1.157 |
| BioCyc Enzyme Link: | BioCyc 2.7.1.157 |
| ExPASy Enzyme Link: | ExPASy2.7.1.157 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.1.157 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.1.157 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.1.157 |
| IntEnz Enzyme Link: | IntEnz 2.7.1.157 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.1.157 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:12617 | ATP + N-acetyl-alpha-D-galactosamine = ADP + H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Identification of the GalNAc kinase amino acid sequence. | Pastuszak I, O'Donnell J, Elbein AD | 1996 Sep 27 | 8798585 |
| Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation. | Pastuszak I, Drake R, Elbein AD | 1996 Aug 23 | 8702831 |
| Mechanistic studies on human N-acetylgalactosamine kinase. | Agnew A, Timson D | 2010 Jun | 19874134 |
| The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine: a thermodynamic analysis. | Stockbridge RB, Wolfenden R | 2009 Aug 21 | 19531469 |
| The molecular architecture of human N-acetylgalactosamine kinase. | Thoden JB, Holden HM | 2005 Sep 23 | 16006554 |