If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: galactitol catabolism
|Superclasses:||Degradation/Utilization/Assimilation → Secondary Metabolites Degradation → Sugar Derivatives Degradation → Sugar Alcohols Degradation|
Of the six existing hexitols, only three (D-mannitol, D-sorbitol [glucitol], and galactitol [owing to symmetry, D- and L-galactitol are identical]) occur naturally, and each of these can be utilized by E. coli K-12 as a total source of carbon and energy. Each enters the cell via a specific phosphotransferase system, so the first intracellular species is the 6-phospho-derivative (in the case of galactitol, D-galactitol-1-phosphate and D-galactitol-6-phosphate are identical). In all three cases, this sugar alcohol phosphate becomes the substrate for a dehydrogenase that oxidizes its 2-alcohol group to a keto group. In the cases of mannitol and sorbitol, the resulting keto sugar phosphate is D-fructose-6-phosphate, an intermediate of glycolysis and hence it flows through the pathways of central metabolism to satisfy the cell's need for precursor metabolites, reducing power, and metabolic energy. In the case of galactitol-1-phosphate, however, the product of the dehydrogenation is tagatose-6-phosphate, which becomes the substrate of a kinase and subsequently an aldolase (in a pair of reactions that parallel those of glycolysis) before it is converted into intermediates (D-glyceraldehde-3-phosphate and dihydroxy-acetone-phosphate) of glycolysis.
Review: Mayer, C. and W. Boos, Hexose/Pentose and Hexitol/Pentitol Metabolism. EcoSal Module 3.4.1 [ECOSAL]
Superpathways: superpathway of hexitol degradation (bacteria)
Baez08: Baez M, Merino F, Astorga G, Babul J (2008). "Uncoupling the MgATP-induced inhibition and aggregation of Escherichia coli phosphofructokinase-2 by C-terminal mutations." FEBS Lett 582(13);1907-12. PMID: 18501195
Baez09: Baez M, Babul J (2009). "Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability." FEBS Lett 583(12);2054-60. PMID: 19465020
Baez11: Baez M, Wilson CA, Babul J (2011). "Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization." FEBS Lett 585(14);2158-64. PMID: 21627967
Baez12: Baez M, Wilson CA, Ramirez-Sarmiento CA, Guixe V, Babul J (2012). "Expanded monomeric intermediate upon cold and heat unfolding of phosphofructokinase-2 from Escherichia coli." Biophys J 103(10);2187-94. PMID: 23200052
Baez13: Baez M, Cabrera R, Pereira HM, Blanco A, Villalobos P, Ramirez-Sarmiento CA, Caniuguir A, Guixe V, Garratt RC, Babul J (2013). "A Ribokinase Family Conserved Monovalent Cation Binding Site Enhances the MgATP-induced Inhibition in E. coli Phosphofructokinase-2." Biophys J 105(1);185-93. PMID: 23823238
Benavente15: Benavente R, Esteban-Torres M, Kohring GW, Cortes-Cabrera Á, Sanchez-Murcia PA, Gago F, Acebron I, de Las Rivas B, Munoz R, Mancheno JM (2015). "Enantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 71(Pt 7);1540-54. PMID: 26143925
Bochkareva02: Bochkareva ES, Girshovich AS, Bibi E (2002). "Identification and characterization of the Escherichia coli stress protein UP12, a putative in vivo substrate of GroEL." Eur J Biochem 269(12);3032-40. PMID: 12071968
Brinkkotter00: Brinkkotter A, Kloss H, Alpert C, Lengeler JW (2000). "Pathways for the utilization of N-acetyl-galactosamine and galactosamine in Escherichia coli." Mol Microbiol 2000;37(1);125-35. PMID: 10931310
Cabrera02: Cabrera R, Guixe V, Alfaro J, Rodriguez PH, Babul J (2002). "Ligand-dependent structural changes and limited proteolysis of Escherichia coli phosphofructokinase-2." Arch Biochem Biophys 406(2);289-95. PMID: 12361717
Cabrera06: Cabrera R, Caniuguir A, Ambrosio AL, Guixe V, Garratt RC, Babul J (2006). "Crystallization and preliminary crystallographic analysis of the tetrameric form of phosphofructokinase-2 from Escherichia coli, a member of the ribokinase family." Acta Crystallogr Sect F Struct Biol Cryst Commun 62(Pt 9);935-7. PMID: 16946484
Cabrera08: Cabrera R, Ambrosio AL, Garratt RC, Guixe V, Babul J (2008). "Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition." J Mol Biol 383(3);588-602. PMID: 18762190
Cabrera10: Cabrera R, Babul J, Guixe V (2010). "Ribokinase family evolution and the role of conserved residues at the active site of the PfkB subfamily representative, Pfk-2 from Escherichia coli." Arch Biochem Biophys 502(1);23-30. PMID: 20599671
Cabrera11: Cabrera R, Baez M, Pereira HM, Caniuguir A, Garratt RC, Babul J (2011). "The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-phosphate: kinetic and structural analysis of the allosteric ATP inhibition." J Biol Chem 286(7);5774-83. PMID: 21147773
Caniuguir05: Caniuguir A, Cabrera R, Baez M, Vasquez CC, Babul J, Guixe V (2005). "Role of Cys-295 on subunit interactions and allosteric regulation of phosphofructokinase-2 from Escherichia coli." FEBS Lett 579(11);2313-8. PMID: 15848164
Daldal83: Daldal F (1983). "Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme." J Mol Biol 1983;168(2);285-305. PMID: 6310120
Showing only 20 references. To show more, press the button "Show all references".
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493