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.
Shakeri-Garakani A, Brinkkotter A, Schmid K, Turgut S, Lengeler JW.
Title
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.
Van der Heiden E, Delmarcelle M, Lebrun S, Freichels R, Brans A, Vastenavond CM, Galleni M, Joris B.
Title
A pathway closely related to the (D)-tagatose pathway of gram-negative enterobacteria identified in the gram-positive bacterium Bacillus licheniformis.
Van der Heiden E, Delmarcelle M, Simon P, Counson M, Galleni M, Freedberg DI, Thompson J, Joris B, Battistel MD.
Title
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.