| 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 to permit phosphorylation at C-6. |
| References: |
| 1. |
Shakeri-Garakani, A., Brinkkotter, A., Schmid, K., Turgut, S. and Lengeler, J.W. The genes and enzymes for the catabolism of galactitol, D-tagatose, and related carbohydrates in Klebsiella oxytoca M5a1 and other enteric bacteria display convergent evolution. Mol. Genet. Genomics 271 (2004) 717–728. [DOI] [PMID: 15257457] |
| 2. |
Van der Heiden, E., Delmarcelle, M., Lebrun, S., Freichels, R., Brans, A., Vastenavond, C.M., Galleni, M. and Joris, B. A pathway closely related to the (D)-tagatose pathway of gram-negative enterobacteria identified in the gram-positive bacterium Bacillus licheniformis. Appl. Environ. Microbiol. 79 (2013) 3511–3515. [DOI] [PMID: 23524682] |
| 3. |
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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