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/Assimilation → Alcohols Degradation → Glycerol Degradation|
Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655
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
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
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
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
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
Daniel95: 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
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
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
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
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