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MetaCyc Pathway: glycerol degradation V
Inferred from experiment

Pathway diagram: glycerol degradation V

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/AssimilationAlcohols DegradationGlycerol Degradation

Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655

Expected Taxonomic Range: Bacteria , Eukaryota

Glycerol dissimilation in Escherichia coli K-12 is usually initiated by the ATP-dependent glycerol kinase (encoded by glpK), which phosphorylates glycerol to sn-glycerol 3-phosphate. However, upon inactivation of the kinase, it may be replaced by the gldA NAD+-linked L-1,2-propanediol dehydrogenase / glycerol dehydrogenase [Tang82]. This enzyme is cryptic in the wild type, and is only activated by mutation. It exhibits broad substrate specificity (it has a lower Km value for (S)-propane-1,2-diol than for glycerol) and its true physiological role remains uncertain [Blattner93, Jin83].

Variants: glycerol and glycerophosphodiester degradation, glycerol degradation I, glycerol degradation II, glycerol degradation III, glycerophosphodiester degradation, superpathway of glycerol degradation to 1,3-propanediol

Unification Links: EcoCyc:GLYCEROLMETAB-PWY

Created 01-Apr-1994 by Riley M, Marine Biological Laboratory


Blattner93: Blattner FR, Burland V, Plunkett G, Sofia HJ, Daniels DL (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 1993;21(23);5408-17. PMID: 8265357

Jin83: Jin RZ, Tang JC, Lin EC (1983). "Experimental evolution of a novel pathway for glycerol dissimilation in Escherichia coli." J Mol Evol 1983;19(6);429-36. PMID: 6361270

Tang82: Tang JC, Forage RG, Lin EC (1982). "Immunochemical properties of NAD+-linked glycerol dehydrogenases from Escherichia coli and Klebsiella pneumoniae." J Bacteriol 1982;152(3);1169-74. PMID: 6183251

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

ASNIS53: ASNIS RE, BRODIE AF (1953). "A glycerol dehydrogenase from Escherichia coli." J Biol Chem 203(1);153-9. PMID: 13069498

Bachler05: Bachler C, Flukiger-Bruhwiler K, Schneider P, Bahler P, Erni B (2005). "From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases." J Biol Chem 280(18);18321-5. PMID: 15753087

Bachler05a: Bachler C, Schneider P, Bahler P, Lustig A, Erni B (2005). "Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR." EMBO J 24(2);283-93. PMID: 15616579

Beutler01: Beutler R, Kampfer U, Schaller J, Erni B (2001). "Heterodimeric dihydroxyacetone kinase from a ptsI mutant of Escherichia coli." Microbiology 147(Pt 2);249-50. PMID: 11158340

Campbell73: Campbell RL, Dekker EE (1973). "Formation of D-1-amino-2-propanol from L-threonine by enzymes from Escherichia coli K-12." Biochem Biophys Res Commun 53(2);432-8. PMID: 4577583

Campbell78: Campbell RL, Swain RR, Dekker EE (1978). "Purification, separation, and characterization of two molecular forms of D-1-amino-2-propanol:NAD+ oxidoreductase activity from extracts of Escherichia coli K-12." J Biol Chem 253(20);7282-8. PMID: 359547

Cintolesi12: Cintolesi A, Clomburg JM, Rigou V, Zygourakis K, Gonzalez R (2012). "Quantitative analysis of the fermentative metabolism of glycerol in Escherichia coli." Biotechnol Bioeng 109(1);187-98. PMID: 21858785

Daniel95a: Daniel R, Stuertz K, Gottschalk G (1995). "Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii." J Bacteriol 177(15);4392-401. PMID: 7635824

Dharmadi06: Dharmadi Y, Murarka A, Gonzalez R (2006). "Anaerobic fermentation of glycerol by Escherichia coli: a new platform for metabolic engineering." Biotechnol Bioeng 94(5);821-9. PMID: 16715533

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

Durnin09: Durnin G, Clomburg J, Yeates Z, Alvarez PJ, Zygourakis K, Campbell P, Gonzalez R (2009). "Understanding and harnessing the microaerobic metabolism of glycerol in Escherichia coli." Biotechnol Bioeng 103(1);148-61. PMID: 19189409

Erni06: Erni B, Siebold C, Christen S, Srinivas A, Oberholzer A, Baumann U (2006). "Small substrate, big surprise: fold, function and phylogeny of dihydroxyacetone kinases." Cell Mol Life Sci 63(7-8);890-900. PMID: 16505971

GarciaAlles04: Garcia-Alles LF, Siebold C, Nyffeler TL, Flukiger-Bruhwiler K, Schneider P, Burgi HB, Baumann U, Erni B (2004). "Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism." Biochemistry 43(41);13037-45. PMID: 15476397

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Gonzalez08: Gonzalez R, Murarka A, Dharmadi Y, Yazdani SS (2008). "A new model for the anaerobic fermentation of glycerol in enteric bacteria: trunk and auxiliary pathways in Escherichia coli." Metab Eng 10(5);234-45. PMID: 18632294

Gutknecht01: Gutknecht R, Beutler R, Garcia-Alles LF, Baumann U, Erni B (2001). "The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor." EMBO J 20(10);2480-6. PMID: 11350937

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jin84: Jin RZ, Lin EC (1984). "An inducible phosphoenolpyruvate: dihydroxyacetone phosphotransferase system in Escherichia coli." J Gen Microbiol 130(1);83-8. PMID: 6368745

Kelley84: Kelley JJ, Dekker EE (1984). "D-1-amino-2-propanol:NAD+ oxidoreductase. Purification and general properties of the large molecular form of the enzyme from Escherichia coli K12." J Biol Chem 1984;259(4);2124-9. PMID: 6365902

Showing only 20 references. To show more, press the button "Show all references".

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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