Disease relevance of FRUCTOSE-16-DIPHOSPHATE

• Characterization of the purified chimeric enzymes showed that the C-terminus of the E. coli enzyme is relevant for the selectivity by FBP [1].
• A decrease of antibody binding in the presence of FDP was also obtained with S. sanguis, Actinomyces viscosus, and Lactobacillus casei lactate dehydrogenases, which reflects a similar mechanism of activation among lactic bacteria [2].
• Purification, crystallization and preliminary X-ray analysis of native and selenomethionine class I tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes [3].
• Fructose 1,6-bisphosphate (FBP) stimulates the reaction of Bacillus stearothermophilus acetate kinase (AK) [4].
• Clostridium thermocellum LDH was shown to catalyze a highly reversible reaction and to be an allosteric enzyme that is activated by fructose-1,6-diphosphate (FDP) [5].

High impact information on FRUCTOSE-16-DIPHOSPHATE

• In addition to CcpA, carbon catabolite activation of the pta gene therefore requires at least two other cofactors, FBP and either HPr or Crh, phosphorylated at Ser-46 by the ATP-dependent Hpr kinase [6].
• Restriction endonuclease mapping of pPC37 and pPC58 and DNA hybridization studies indicated that a 2.1-kb region of these two clones of C. acetobutylicum DNA encodes the FDP-activated LDH [7].
• Tagatose-1,6-bisphosphate aldolase (EC 4.1.2.40) is situated at the branching of the tagatose-6-phosphate and Embden-Meyerhof-Parnas (glycolysis) metabolic pathways, where it catalyzes the reversible cleavage of tagatose-1,6-bisphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate [3].
• The H. influenzae glycerol kinase is inhibited by FBP but not by IIA(Glc), in agreement with the prediction based on sequence comparison [8].
• The enzyme from Escherichia coli is an allosteric regulatory enzyme whose activity is inhibited by fructose 1,6-bisphosphate (FBP) and the glucose-specific phosphocarrier of the phosphoenolpyruvate:glycose phosphotransferase system, IIA(Glc) (previously termed III(Glc)) [8].

Biological context of FRUCTOSE-16-DIPHOSPHATE

• A model is presented to interpret the sigmoidal kinetics for ATP, the absence of cooperativity for FBP binding, and the allosteric activation by FBP of this enzyme [4].
• Comparison of its primary structure with that of the highly similar Haemophilus influenzae glycerol kinase reveals that the amino acid sequence for the binding site for FBP is conserved while the amino acid sequence for the binding site for IIA(Glc) contains differences that are predicted to prevent its inhibition [8].
• The DMHF concentration always correlated with the yeast cell count and D-fructose-1,6-diphosphate concentration [9].

Anatomical context of FRUCTOSE-16-DIPHOSPHATE

• We assume that at least the first step of the metabolism of D-fructose-1,6-diphosphate takes place in the cell wall or membrane of the yeast [9].

Associations of FRUCTOSE-16-DIPHOSPHATE with other chemical compounds

• The in vitro Ca-P compatibility in ready-for-use TPN solutions after the addition of different concentrations of inorganic phosphate or d-fructose-1,6-diphosphate (FDP) and calcium chloride was evaluated [10].
• 2,5-Dimethyl-4-hydroxy-3(2H)-furanone (DMHF) is an important aroma compound found in many fruits such as strawberries and pineapples and it is also produced by the soy-sauce-fermenting yeast Zygosaccharomyces rouxii after the addition of d-fructose-1,6-diphosphate to yeast-peptone-dextrose nutrient media [9].

Analytical, diagnostic and therapeutic context of FRUCTOSE-16-DIPHOSPHATE

• An enzyme-linked immunosorbent assay allowed detection of a 30% decrease in enzyme-antibody fixation when FDP was added [2].

References