53798-20-2

Usage

Uses

Used in Pharmaceutical Industry:
Tagatose 6-phosphate is used as an intermediate in the metabolism of galactose, which is essential for the proper functioning of cells. It is used for the development of drugs targeting metabolic disorders related to galactose metabolism.
Used in Food Industry:
Tagatose 6-phosphate is used as a natural sweetener in the food industry due to its low-calorie content and prebiotic properties. It is used for developing healthier food products with reduced sugar content and improved gut health benefits.
Used in Biotechnology:
Tagatose 6-phosphate is used as a key compound in the production of bio-based materials and chemicals. It serves as a building block for the synthesis of various biopolymers and bioproducts, contributing to the development of sustainable and eco-friendly alternatives to petroleum-based products.
Used in Research and Development:
Tagatose 6-phosphate is used as a research tool for studying the metabolic pathways and regulatory mechanisms of galactose metabolism. It helps researchers understand the molecular basis of various diseases and develop targeted therapeutic strategies.

InChI:InChI=1/C6H13O9P/c7-2-6(10)5(9)4(8)3(15-6)1-14-16(11,12)13/h3-5,7-10H,1-2H2,(H2,11,12,13)/t3-,4+,5+,6+/m1/s1

Upstream product

• 87-81-0 D-tagatose 
• 71021-01-7 1,2:3,4-di-O-isopropylidene-β-D-psicofuranose 6-dihydrogenophosphate 

Relevant academic research and scientific papers

Characterization of a thermotolerant ROK-type mannofructokinase from Streptococcus mitis: application to the synthesis of phosphorylated sugars

Most of the “repressor, open reading frame, kinase” (ROK) proteins already characterized so far, and exhibiting a kinase activity, take restrictedly d-glucose as substrate. By exploring the sequenced bacterial diversity, 61 ATP-dependent kinases belonging to the ROK family have been identified and experimentally assayed for the phosphorylation of hexoses. These kinases were mainly found to be thermotolerant and highly active toward d-mannose and d-fructose with notable activities toward d-tagatose. Among them, the ATP-dependent kinase from the mesophile Streptococcus mitis (named ScrKmitis) was biochemically characterized and its substrate spectrum further studied. This enzyme possessed impressive catalytic efficiencies toward d-mannose and d-fructose of 1.5 106?s?1?M?1 and 2.7 105?s?1?M?1, respectively, but also significant ones toward d-tagatose (3.5 102?s?1?M?1) and the unnatural monosaccharides d-altrose (1.1 104?s?1?M?1) and d-talose (3.4 102?s?1?M?1). Specific activities measured for all hexoses showed a high stereopreference for d- over l-series. As proof of concept, 8 hexoses were phosphorylated in moderate to good yields, some of them described for the first time like l-sorbose-5-phosphate unusually phosphorylated in position 5. Its thermotolerance, its wide pH tolerance (from 7 to 10), and temperature range (> 85% activity between 40 and 70?°C) open the way to applications in the enzymatic synthesis of monophosphorylated hexoses.

Competitive inhibitors of type B ribose 5-phosphate isomerases: design, synthesis and kinetic evaluation of new d-allose and d-allulose 6-phosphate derivatives

This study reports syntheses of d-allose 6-phosphate (All6P), d-allulose (or d-psicose) 6-phosphate (Allu6P), and seven d-ribose 5-phosphate isomerase (Rpi) inhibitors. The inhibitors were designed as analogues of the 6-carbon high-energy intermediate pos