| EC |
2.7.1.234 |
| Accepted name: |
D-tagatose-1-phosphate kinase |
| Reaction: |
ATP + D-tagatopyranose 1-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate |
| Other name(s): |
TagK |
| Systematic name: |
ATP:D-tagatopyranse-1-phosphate 6-phosphotransferase |
| Comments: |
The enzyme, which has been purified from the bacteria Klebsiella oxytoca and Bacillus licheniformis, is part of a D-tagatose catabolic pathway. The substrate, which occurs in a pyranose form in solution, undergoes a change to the furanose conformation after binding to the enzyme, in order permit phosphorylation at C6.The enzyme has been pruified from the bacterium Bacillus licheniformis and is part of a D-tagatose catabolic pathway. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Van der Heiden, E., Delmarcelle, M., Simon, P., Counson, M., Galleni, M., Freedberg, D.I., Thompson, J., Joris, B. and Battistel, M.D. Synthesis and physicochemical characterization of D-tagatose-1-phosphate: the substrate of the tagatose-1-phosphate kinase in the phosphotransferase system-mediated D-tagatose catabolic pathway of Bacillus licheniformis. J. Mol. Microbiol. Biotechnol. 25 (2015) 106–119. [DOI] [PMID: 26159072] |
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| [EC 2.7.1.234 created 2021] |
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