If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Degradation/Utilization/Assimilation → Alcohols Degradation → Glycerol Degradation|
Glycerol uptake in bacteria is mediated by the glycerol diffusion facilitator, an integral membrane protein catalyzing the rapid equilibration of concentration gradients of glycerol across the cytoplasmic membrane [Beijer93]. Intracellular glycerol is converted to glycerol-3-Phosphate (Glycerol-3-P) by the enzyme glycerol kinase that uses ATP as phosphoryl donor. Glycerol-3-P is not a substrate of the glycerol diffusion facilitator and thus remains in the cell, where it is further metabolized. As a result, the driving force for the uptake of glycerol is generated by the phosphorylation of glycerol by glycerol kinase [Charrier97].
While Glycerol-3-P can not leave the cytoplasm, it can be imported into the cell by the GlpT transporter, a member of the major facilitator superfamily, that couples the import of glycerol-3-P into the cytoplasm to the export of inorganic phosphates from the cytoplasm to the periplasm [Ambudkar86, Huang03].
In addition, E. coli K12 possesses two systems the salvage of glycerophosphoryl diesters, the Glp system and the Ugp system.
In the Glp system, the glpQ gene encodes a periplasmic glycerophosphoryl diester phosphodiesterase (periplasmic GDP) which hydrolyzes deacylated phospholipids to an alcohol plus Glycerol-3-P . The Glycerol-3-P is then transported into the cell by the GlpT transporter. Periplasmic GDP is specific for the glycerophospho- moiety of the substrate, while the alcohol can be any one of several alcohols. This provides the cell with the capability of channeling a wide variety of glycerophosphodiesters into the glpQT-encoded dissimilatory system.
In the Ugp system the diesters are hydrolyzed during transport at the cytoplasmic side of the inner membrane to Glycerol-3-P plus alcohol by a cytoplasmic GDP, an enzyme encoded by the ugpQ gene. The Ugp system is induced when the cells are starved for inorganic phospate, which is generates phosphate by the system [Tommassen91].
In E. coli glycerol-3-P can be further metabolized to dihydroxyacetone phosphate (DHAP) by either of two membrane-bound enzymes, depending on the growth conditions. The presumed role of this process is the salvage of glycerol and glycerol phosphates generated by the breakdown of phospholipids and triacylglycerol. Under aerobic conditions, a homodimeric aerobic glycerol-3-P dehydrogenase (encoded by the glpD gene) is produced, which can accept either oxygen or nitrate as the electron acceptor [Schryvers78]. Under anaerobic conditions, a different glycerol-3-P dehydrogenase is preferentially expressed. This tri-heteromeric protein complex, which is encoded by the glpACB opron, channels the electrons from glycerol-3-P to either fumarate or nitrate [Cole88].
Variants: glycerol degradation V
Charrier97: Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A (1997). "Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue." J Biol Chem 272(22);14166-74. PMID: 9162046
Cole88: Cole ST, Eiglmeier K, Ahmed S, Honore N, Elmes L, Anderson WF, Weiner JH (1988). "Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12." J Bacteriol 1988;170(6);2448-56. PMID: 3286606
Schryvers78: Schryvers A, Lohmeier E, Weiner JH (1978). "Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli." J Biol Chem 253(3);783-8. PMID: 340460
Tommassen91: Tommassen J, Eiglmeier K, Cole ST, Overduin P, Larson TJ, Boos W (1991). "Characterization of two genes, glpQ and ugpQ, encoding glycerophosphoryl diester phosphodiesterases of Escherichia coli." Mol Gen Genet 1991;226(1-2);321-7. PMID: 1851953
Anderson07: Anderson MJ, DeLabarre B, Raghunathan A, Palsson BO, Brunger AT, Quake SR (2007). "Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 --> Asp obtained using microfluidic crystallization devices." Biochemistry 46(19);5722-31. PMID: 17441732
Applebee11: Applebee MK, Joyce AR, Conrad TM, Pettigrew DW, Palsson BO (2011). "Functional and metabolic effects of adaptive glycerol kinase (GLPK) mutants in Escherichia coli." J Biol Chem 286(26);23150-9. PMID: 21550976
Austin91: Austin D, Larson TJ (1991). "Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12." J Bacteriol 1991;173(1);101-7. PMID: 1987111
Bork92: Bork P, Sander C, Valencia A (1992). "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." Proc Natl Acad Sci U S A 89(16);7290-4. PMID: 1323828
Brzoska88: Brzoska P, Boos W (1988). "Characteristics of a ugp-encoded and phoB-dependent glycerophosphoryl diester phosphodiesterase which is physically dependent on the ugp transport system of Escherichia coli." J Bacteriol 1988;170(9);4125-35. PMID: 2842304
Bystrom99: Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ (1999). "Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion." Biochemistry 38(12);3508-18. PMID: 10090737
deRiel78: de Riel JK, Paulus H (1978). "Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidence." Biochemistry 1978;17(24);5141-6. PMID: 215195
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Ehrmann87a: Ehrmann M, Boos W, Ormseth E, Schweizer H, Larson TJ (1987). "Divergent transcription of the sn-glycerol-3-phosphate active transport (glpT) and anaerobic sn-glycerol-3-phosphate dehydrogenase (glpA glpC glpB) genes of Escherichia coli K-12." J Bacteriol 169(2);526-32. PMID: 3027032
Feese94: Feese M, Pettigrew DW, Meadow ND, Roseman S, Remington SJ (1994). "Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation." Proc Natl Acad Sci U S A 91(9);3544-8. PMID: 8170944
Feese98: Feese MD, Faber HR, Bystrom CE, Pettigrew DW, Remington SJ (1998). "Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation." Structure 6(11);1407-18. PMID: 9817843
Fujimoto12: Fujimoto N., Kosaka T., Yamada M. (2012). "Menaquinone as Well as Ubiquinone as a Crucial Component in the Escherichia coli Respiratory Chain." Chapter 10 in Chemical Biology, edited by D Ekinci, ISBN 978-953-51-0049-2.
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