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EcoSal Plus

Domain 3:

Metabolism

Glycerol and Methylglyoxal Metabolism

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  • Author: Ian R. Booth1
  • Editor: Valley Stewart2
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom; 2: University of California, Davis, Davis, CA
  • Received 02 December 2004 Accepted 10 January 2005 Published 29 March 2005
  • Address correspondence to Ian R. Booth i.r.booth@abdn.ac.uk
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  • Abstract:

    The metabolic connection between glycerol and methylglyoxal (MG) is principally that DHAP, which is an intermediate in the aerobic breakdown of glycerol, is also the major precursor of MG, being the substrate for methylglyoxal synthase (MGS). The synthesis of MG is a consequence of unbalanced metabolism related either to a limitation for phosphate or to excessive carbon flux through the pathways that have the capacity to generate significant pools of DHAP. Cells producing MG produce a poison as an intermediate strategy for survival of metabolic imbalance. Indeed the panoply of metabolic regulation in this sector of catabolism can be seen as a strategy to avoid death by self-poisoning. Glycerol entry into and serovar Typhimurium is facilitated by the aquaglyceroporin, GlpF. A homologous protein in serovar Typhimurium, PduF, facilitates the entry of 1,2-propanediol (Ppd) and is part of the Ppd metabolic pathway. MGS catalyzes the elimination of phosphate from DHAP, forming an enzyme-bound enediol(ate) intermediate that is released from the enzyme, followed by release of inorganic phosphate. The enzyme is highly specific for DHAP. Multiple MG detoxification pathways are found in both and serovar Typhimurium, but the dominant pathway is the GSH-dependent glyoxalase III system. The KefB and KefC systems have evolved to provide protection during detoxification of electrophiles. KefB and KefC are GSH-gated K efflux systems that are activated by the formation and binding of glutathione adducts that are generated during detoxification.

  • Citation: Booth I. 2005. Glycerol and Methylglyoxal Metabolism, EcoSal Plus 2005; doi:10.1128/ecosalplus.3.4.3

Key Concept Ranking

Amino Acid Synthesis
0.38402048
Glycerol Kinase
0.35774118
Klebsiella pneumoniae
0.3436198
0.38402048

References

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23. Mori K, Toraya T. 1999. Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor. Biochemistry 38:13170–13178. [PubMed][CrossRef]
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25. Hopper DJ, Cooper RA. 1972. The purification and properties of Escherichia coli methylglyoxal synthase. Biochem J 128:321–329.[PubMed]
26. MacLean MJ, Ness LS, Ferguson GP, Booth IR. 1998. The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli. Mol Microbiol 27:563–571. [PubMed][CrossRef]
27. Freedberg WB, Kistler WS, Lin EC. 1971. Lethal synthesis of methylglyoxal by Escherichia coli during unregulated glycerol metabolism. J Bacteriol 108:137–144.[PubMed]
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29. Totemeyer S, Booth NA, Nichols WW, Dunbar B, Booth IR. 1998. From famine to feast: the role of methylglyoxal production in Escherichia coli. Mol Microbiol 27:553–562. [PubMed][CrossRef]
30. Saadat D, Harrison DHT. 1998. Identification of catalytic bases in the active site of Escherichia coli methylglyoxal synthase: cloning, expression, and functional characterization of conserved aspartic acid residues. Biochemistry 37:10074–10086. [PubMed][CrossRef]
31. Saadat D, Harrison DHT. 1999. The crystal structure of methylglyoxal synthase from Escherichia coli. Structure 7:309–317. [PubMed][CrossRef]
32. Ackerman RS, Cozzarelli NR, Epstein W. 1974. Accumulation of toxic concentrations of methylglyoxal by wild-type Escherichia coli K-12. J Bacteriol 119:357–362.
33. Kadner RJ, Murphy GP, Stephens CM. 1992. Two mechanisms for growth inhibition by elevated transport of sugar phosphates in Escherichia coli. J Gen Microbiol 138:2007–2014.[PubMed]
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35. Misra K, Banerjee AB, Ray S, Ray M. 1995. Glyoxalase-III from Escherichia coli—a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem J 305:999–1003.[PubMed]
36. Grant AW, Steel G, Waugh H, Ellis EM. 2003. A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity. FEMS Microbiol Lett 218:93–99. [PubMed][CrossRef]
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38. Clugston SL, Barnard JF, Kinach R, Miedema D, Ruman R, Daub E, Honek JF. 1998. Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions. Biochemistry 37:8754–8763. [PubMed][CrossRef]
39. He MM, Clugston SL, Honek JF, Matthews BW. 2000. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry 39:8719–8727. [PubMed][CrossRef]
40. Clugston SL, Honek JF. 2000. Identification of sequences encoding the detoxification metalloisomerase Glyoxalase I in microbial genomes of several pathogenic organisms. J Mol Evol 50:491–495.[PubMed]
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42. Ferguson GP, Battista JR, Lee AT, Booth IR. 2000. Protection of the DNA during the exposure of Escherichia coli cells to a toxic metabolite: the role of the KefB and KefC potassium channels. Mol Microbiol 35:113–122. [PubMed][CrossRef]
43. Ferguson GP, Chacko AD, Lee C, Booth IR. 1996. The activity of the high-affinity K+ uptake system Kdp sensitizes cells of Escherichia coli to methylglyoxal. J Bacteriol 178:3957–3961.[PubMed]
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47. Booth IR. 2003. Bacterial ion channels, p 91–112. In Setlow JK (ed), Genetic Engineering: Principles and Methods, vol. 25. Kluwer Academic/Plenum Publishers, New York, N.Y.
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2005-03-29
2017-03-30

Abstract:

The metabolic connection between glycerol and methylglyoxal (MG) is principally that DHAP, which is an intermediate in the aerobic breakdown of glycerol, is also the major precursor of MG, being the substrate for methylglyoxal synthase (MGS). The synthesis of MG is a consequence of unbalanced metabolism related either to a limitation for phosphate or to excessive carbon flux through the pathways that have the capacity to generate significant pools of DHAP. Cells producing MG produce a poison as an intermediate strategy for survival of metabolic imbalance. Indeed the panoply of metabolic regulation in this sector of catabolism can be seen as a strategy to avoid death by self-poisoning. Glycerol entry into and serovar Typhimurium is facilitated by the aquaglyceroporin, GlpF. A homologous protein in serovar Typhimurium, PduF, facilitates the entry of 1,2-propanediol (Ppd) and is part of the Ppd metabolic pathway. MGS catalyzes the elimination of phosphate from DHAP, forming an enzyme-bound enediol(ate) intermediate that is released from the enzyme, followed by release of inorganic phosphate. The enzyme is highly specific for DHAP. Multiple MG detoxification pathways are found in both and serovar Typhimurium, but the dominant pathway is the GSH-dependent glyoxalase III system. The KefB and KefC systems have evolved to provide protection during detoxification of electrophiles. KefB and KefC are GSH-gated K efflux systems that are activated by the formation and binding of glutathione adducts that are generated during detoxification.

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Figures

Image of Figure 1
Figure 1

The major enzymatic routes in aerobic cells are indicated by solid arrows. A broken arrow is used to indicate the anaerobic Gly-3-P oxidation pathway. The methylglyoxal synthesis pathway is boxed to indicate the special nature of this aspect of the metabolism. Standard nomenclature is used to indicate the genes for the enzymatic steps.

Citation: Booth I. 2005. Glycerol and Methylglyoxal Metabolism, EcoSal Plus 2005; doi:10.1128/ecosalplus.3.4.3
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Image of Figure 2
Figure 2

Broken arrows are used to indicate the fates of the dihydroxyacetone phosphate and 1,3-propanediol. Gdh, glycerol dehydrogenase; GDHt, glycerol dehydratase; PDOR, 1,3-propanediol oxidoreductase; DHA kinase, PEP-dependent dihydroxyacetone kinase; PEP, phosphoenolpyruvate.

Citation: Booth I. 2005. Glycerol and Methylglyoxal Metabolism, EcoSal Plus 2005; doi:10.1128/ecosalplus.3.4.3
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Image of Figure 3
Figure 3

See text for explanation. A strong dotted line is used to indicate the activation of KefB by -lactoylglutathione. Fine dotted lines indicate the glutathione-independent methylglyoxal detoxification pathways. These two pathways (GlxIII and MGR) remain poorly characterized at the genetic level but appear to be quantitatively insignificant. Standard genetic acronyms are used for the genes encoding the major enzymes of the pathway. GSH, glutathione.

Citation: Booth I. 2005. Glycerol and Methylglyoxal Metabolism, EcoSal Plus 2005; doi:10.1128/ecosalplus.3.4.3
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