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Pathway Description
Glycerol Metabolism
Escherichia coli ED1a
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2025-01-17
Last Updated: 2025-06-09
Glycerol metabolism starts with glycerol is introduced into the cytoplasm through a glycerol channel GlpF Glycerol is then phosphorylated through an ATP mediated glycerol kinase resulting in a Glycerol 3-phosphate. This compound can also be obtained through a glycerophosphodiester reacting with water through a glycerophosphoryl diester phosphodiesterase or it can also be introduced into the cytoplasm through a glycerol-3-phosphate:phosphate antiporter.
Glycerol 3-phosphate is then metabolized into a dihydroxyacetone phosphate in both aerobic or anaerobic conditions. In anaerobic conditions the metabolism is done through the reaction of glycerol 3-phosphate with a menaquinone mediated by a glycerol-3-phosphate dehydrogenase protein complex. In aerobic conditions, the metabolism is done through the reaction of glycerol 3-phosphate with ubiquinone mediated by a glycerol-3-phosphate dehydrogenase [NAD(P]+].
Dihydroxyacetone phosphate is then introduced into the fructose metabolism by turning a dihydroxyacetone into an isomer through a triosephosphate isomerase resulting in a D-glyceraldehyde 3-phosphate which in turn reacts with a phosphate through a NAD dependent Glyceraldehyde 3-phosphate dehydrogenase resulting in a glyceric acid 1,3-biphosphate. This compound is desphosphorylated by a phosphoglycerate kinase resulting in a 3-phosphoglyceric acid.This compound in turn can either react with a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase or a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase resulting in a 2-phospho-D-glyceric acid. This compound interacts with an enolase resulting in a phosphoenolpyruvic acid and water. Phosphoenolpyruvic acid can react either through a AMP driven phosphoenoylpyruvate synthase or a ADP driven pyruvate kinase protein complex resulting in a pyruvic acid. Pyruvic acid reacts with CoA through a NAD driven pyruvate dehydrogenase complex resulting in a carbon dioxide and a Acetyl-CoA which gets incorporated into the TCA cycle pathway.
References
Glycerol Metabolism References
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Pubmed: 1400248
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Sedivy JM, Daldal F, Fraenkel DG: Fructose bisphosphatase of Escherichia coli: cloning of the structural gene (fbp) and preparation of a chromosomal deletion. J Bacteriol. 1984 Jun;158(3):1048-53.
Pubmed: 6327623
Hamilton WD, Harrison DA, Dyer TA: Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene. Nucleic Acids Res. 1988 Sep 12;16(17):8707. doi: 10.1093/nar/16.17.8707.
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Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. doi: 10.1093/nar/23.12.2105.
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Alefounder PR, Perham RN: Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli. Mol Microbiol. 1989 Jun;3(6):723-32. doi: 10.1111/j.1365-2958.1989.tb00221.x.
Pubmed: 2546007
Maupin-Furlow JA, Rosentel JK, Lee JH, Deppenmeier U, Gunsalus RP, Shanmugam KT: Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli. J Bacteriol. 1995 Sep;177(17):4851-6. doi: 10.1128/jb.177.17.4851-4856.1995.
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Walkenhorst HM, Hemschemeier SK, Eichenlaub R: Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene. Microbiol Res. 1995 Nov;150(4):347-61. doi: 10.1016/S0944-5013(11)80016-9.
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Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. doi: 10.1093/dnares/3.3.137.
Pubmed: 8905232
Spring TG, Wold F: The purification and characterization of Escherichia coli enolase. J Biol Chem. 1971 Nov 25;246(22):6797-802.
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Dannelly HK, Duclos B, Cozzone AJ, Reeves HC: Phosphorylation of Escherichia coli enolase. Biochimie. 1989 Sep-Oct;71(9-10):1095-100. doi: 10.1016/0300-9084(89)90116-8.
Pubmed: 2513001
Chandran V, Luisi BF: Recognition of enolase in the Escherichia coli RNA degradosome. J Mol Biol. 2006 Apr 21;358(1):8-15. doi: 10.1016/j.jmb.2006.02.012. Epub 2006 Feb 21.
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Ohara O, Dorit RL, Gilbert W: Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli. Proc Natl Acad Sci U S A. 1989 Sep;86(18):6883-7. doi: 10.1073/pnas.86.18.6883.
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Hensel M, Shea JE, Baumler AJ, Gleeson C, Blattner F, Holden DW: Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12. J Bacteriol. 1997 Feb;179(4):1105-11. doi: 10.1128/jb.179.4.1105-1111.1997.
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Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. doi: 10.1093/dnares/3.6.363.
Pubmed: 9097039
Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. doi: 10.1093/dnares/3.6.379.
Pubmed: 9097040
Pettigrew DW, Ma DP, Conrad CA, Johnson JR: Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme. J Biol Chem. 1988 Jan 5;263(1):135-9.
Pubmed: 2826434
de Riel JK, Paulus H: Subunit dissociation in the allosteric regulation of Glycerol kinase from Escherichia coli. 3. Role in desensitization. Biochemistry. 1978 Nov 28;17(24):5146-50. doi: 10.1021/bi00617a012.
Pubmed: 31903
Weissenborn DL, Wittekindt N, Larson TJ: Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12. J Biol Chem. 1992 Mar 25;267(9):6122-31.
Pubmed: 1372899
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000931
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