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Volumn 302, Issue 4-5, 2012, Pages 225-229

The glyoxalase pathway in protozoan parasites

Author keywords

Apicomplexan; Glyoxalase pathway; Methylglyoxal; Protozoan parasites; Trypanosomatids

Indexed keywords

GLYOXALASE; HYDROXYACYLGLUTATHIONE HYDROLASE; LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL; NICKEL;

EID: 84866632897     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2012.07.005     Document Type: Article
Times cited : (45)

References (39)
  • 1
    • 14944354773 scopus 로고    scopus 로고
    • Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts
    • Akoachere M., Iozef R., Rahlfs S., Deponte M., Mannervik B., Creighton D.J., Schirmer H., Becker K. Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts. Biol. Chem. 2005, 386:41-52.
    • (2005) Biol. Chem. , vol.386 , pp. 41-52
    • Akoachere, M.1    Iozef, R.2    Rahlfs, S.3    Deponte, M.4    Mannervik, B.5    Creighton, D.J.6    Schirmer, H.7    Becker, K.8
  • 2
    • 33645052721 scopus 로고    scopus 로고
    • Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme
    • Ariza A., Vickers T.J., Greig N., Armour K.A., Dixon M.J., Eggleston I.M., Fairlamb A.H., Bond C.S. Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme. Mol. Microbiol. 2006, 59:1239-1248.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1239-1248
    • Ariza, A.1    Vickers, T.J.2    Greig, N.3    Armour, K.A.4    Dixon, M.J.5    Eggleston, I.M.6    Fairlamb, A.H.7    Bond, C.S.8
  • 7
    • 0030927104 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping
    • Cameron A.D., Olin B., Ridderstrom M., Mannervik B., Jones T.A. Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping. EMBO J. 1997, 16:3386-3395.
    • (1997) EMBO J. , vol.16 , pp. 3386-3395
    • Cameron, A.D.1    Olin, B.2    Ridderstrom, M.3    Mannervik, B.4    Jones, T.A.5
  • 9
    • 0023837912 scopus 로고
    • D-Lactate production by Leishmania braziliensis through the glyoxalase pathway
    • Darling T.N., Blum J.J. d-Lactate production by Leishmania braziliensis through the glyoxalase pathway. Mol. Biochem. Parasitol. 1988, 28:121-127.
    • (1988) Mol. Biochem. Parasitol. , vol.28 , pp. 121-127
    • Darling, T.N.1    Blum, J.J.2
  • 10
    • 35348993113 scopus 로고    scopus 로고
    • Allosteric coupling of two different functional active sites in monomeric Plasmodium falciparum glyoxalase I
    • Deponte M., Sturm N., Mittler S., Harner M., Mack H., Becker K. Allosteric coupling of two different functional active sites in monomeric Plasmodium falciparum glyoxalase I. J. Biol. Chem. 2007, 282:28419-28430.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28419-28430
    • Deponte, M.1    Sturm, N.2    Mittler, S.3    Harner, M.4    Mack, H.5    Becker, K.6
  • 12
    • 24644494767 scopus 로고    scopus 로고
    • Protein glycation in Saccharomyces cerevisiae. Argpyrimidine formation and methylglyoxal catabolism
    • Gomes R.A., Sousa Silva M., Vicente Miranda H., Ferreira A.E., Cordeiro C.A., Freire A.P. Protein glycation in Saccharomyces cerevisiae. Argpyrimidine formation and methylglyoxal catabolism. FEBS J. 2005, 272:4521-4531.
    • (2005) FEBS J. , vol.272 , pp. 4521-4531
    • Gomes, R.A.1    Sousa Silva, M.2    Vicente Miranda, H.3    Ferreira, A.E.4    Cordeiro, C.A.5    Freire, A.P.6
  • 13
    • 58149170698 scopus 로고    scopus 로고
    • A comparative study of methylglyoxal metabolism in trypanosomatids
    • Greig N., Wyllie S., Patterson S., Fairlamb A.H. A comparative study of methylglyoxal metabolism in trypanosomatids. FEBS J. 2009, 276:376-386.
    • (2009) FEBS J. , vol.276 , pp. 376-386
    • Greig, N.1    Wyllie, S.2    Patterson, S.3    Fairlamb, A.H.4
  • 14
    • 33845190312 scopus 로고    scopus 로고
    • Trypanothione-dependent glyoxalase I in Trypanosoma cruzi
    • Greig N., Wyllie S., Vickers T.J., Fairlamb A.H. Trypanothione-dependent glyoxalase I in Trypanosoma cruzi. Biochem. J. 2006, 400:217-223.
    • (2006) Biochem. J. , vol.400 , pp. 217-223
    • Greig, N.1    Wyllie, S.2    Vickers, T.J.3    Fairlamb, A.H.4
  • 15
    • 0034254431 scopus 로고    scopus 로고
    • Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation
    • He M.M., Clugston S.L., Honek J.F., Matthews B.W. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry 2000, 39:8719-8727.
    • (2000) Biochemistry , vol.39 , pp. 8719-8727
    • He, M.M.1    Clugston, S.L.2    Honek, J.F.3    Matthews, B.W.4
  • 16
    • 0242710739 scopus 로고    scopus 로고
    • Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion
    • Iozef R., Rahlfs S., Chang T., Schirmer H., Becker K. Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion. FEBS Lett. 2003, 554:284-288.
    • (2003) FEBS Lett. , vol.554 , pp. 284-288
    • Iozef, R.1    Rahlfs, S.2    Chang, T.3    Schirmer, H.4    Becker, K.5
  • 17
    • 2542450775 scopus 로고    scopus 로고
    • Glyoxalase II of African trypanosomes is trypanothione-dependent
    • Irsch T., Krauth-Siegel R.L. Glyoxalase II of African trypanosomes is trypanothione-dependent. J. Biol. Chem. 2004, 279:22209-22217.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22209-22217
    • Irsch, T.1    Krauth-Siegel, R.L.2
  • 18
    • 84860341694 scopus 로고    scopus 로고
    • Low-molecular-mass antioxidants in parasites
    • Krauth-Siegel R.L., Leroux A.E. Low-molecular-mass antioxidants in parasites. Antioxid. Redox Signal. 2012, 17(4):583-607.
    • (2012) Antioxid. Redox Signal. , vol.17 , Issue.4 , pp. 583-607
    • Krauth-Siegel, R.L.1    Leroux, A.E.2
  • 21
    • 0038119479 scopus 로고
    • Enzymatic transformation of phosphoglyceric acid into pyruvic and phosphoric acid
    • Lohman K., Meyerhof O. über die enzymatische Umwandlung von Phosphoglyzerinsäure in Brenztraubensäure und Phosphorsäure. Biochem. Z. 1934, 273:60-72.
    • (1934) Biochem. Z. , vol.273 , pp. 60-72
    • Lohman, K.1    Meyerhof, O.2
  • 22
    • 0018710893 scopus 로고
    • Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources
    • Marmstal E., Aronsson A.C., Mannervik B. Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources. Biochem. J. 1979, 183:23-30.
    • (1979) Biochem. J. , vol.183 , pp. 23-30
    • Marmstal, E.1    Aronsson, A.C.2    Mannervik, B.3
  • 24
    • 0040896047 scopus 로고
    • Further investigations into the biochemical conversion of methylglyoxal into lactic acid together with observations on the formation of various natural lactic acids
    • Neuberg C. Further investigations into the biochemical conversion of methylglyoxal into lactic acid together with observations on the formation of various natural lactic acids. Biochem. Z. 1913, 51:484-508.
    • (1913) Biochem. Z. , vol.51 , pp. 484-508
    • Neuberg, C.1
  • 25
    • 0001739947 scopus 로고
    • The mechanism of action of glyoxalase
    • Racker E. The mechanism of action of glyoxalase. J. Biol. Chem. 1951, 190:685-696.
    • (1951) J. Biol. Chem. , vol.190 , pp. 685-696
    • Racker, E.1
  • 26
    • 37849007277 scopus 로고    scopus 로고
    • Catalysis and structural properties of Leishmania infantum glyoxalase II: trypanothione specificity and phylogeny
    • Silva M.S., Barata L., Ferreira A.E., Romao S., Tomas A.M., Freire A.P., Cordeiro C. Catalysis and structural properties of Leishmania infantum glyoxalase II: trypanothione specificity and phylogeny. Biochemistry 2008, 47:195-204.
    • (2008) Biochemistry , vol.47 , pp. 195-204
    • Silva, M.S.1    Barata, L.2    Ferreira, A.E.3    Romao, S.4    Tomas, A.M.5    Freire, A.P.6    Cordeiro, C.7
  • 27
    • 18944383472 scopus 로고    scopus 로고
    • Quantitative assessment of the glyoxalase pathway in Leishmania infantum as a therapeutic target by modelling and computer simulation
    • Sousa Silva M., Ferreira A.E., Tomas A.M., Cordeiro C., Ponces Freire A. Quantitative assessment of the glyoxalase pathway in Leishmania infantum as a therapeutic target by modelling and computer simulation. FEBS J. 2005, 272:2388-2398.
    • (2005) FEBS J. , vol.272 , pp. 2388-2398
    • Sousa Silva, M.1    Ferreira, A.E.2    Tomas, A.M.3    Cordeiro, C.4    Ponces Freire, A.5
  • 29
    • 9444245016 scopus 로고    scopus 로고
    • Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes
    • Sukdeo N., Clugston S.L., Daub E., Honek J.F. Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes. Biochem. J. 2004, 384:111-117.
    • (2004) Biochem. J. , vol.384 , pp. 111-117
    • Sukdeo, N.1    Clugston, S.L.2    Daub, E.3    Honek, J.F.4
  • 31
    • 0025298551 scopus 로고
    • The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley P.J. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 1990, 269:1-11.
    • (1990) Biochem. J. , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 32
    • 0030176306 scopus 로고    scopus 로고
    • Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification - a role in pathogenesis and antiproliferative chemotherapy
    • Thornalley P.J. Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification - a role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 1996, 27:565-573.
    • (1996) Gen. Pharmacol. , vol.27 , pp. 565-573
    • Thornalley, P.J.1
  • 33
    • 79955956732 scopus 로고    scopus 로고
    • The glyoxalase system of malaria parasites - implications for cell biology and general glyoxalase research
    • Urscher M., Alisch R., Deponte M. The glyoxalase system of malaria parasites - implications for cell biology and general glyoxalase research. Semin. Cell Dev. Biol. 2011, 22:262-270.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 262-270
    • Urscher, M.1    Alisch, R.2    Deponte, M.3
  • 34
    • 70349814275 scopus 로고    scopus 로고
    • Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis
    • Urscher M., Deponte M. Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis. Biol. Chem. 2009, 390:1171-1183.
    • (2009) Biol. Chem. , vol.390 , pp. 1171-1183
    • Urscher, M.1    Deponte, M.2
  • 35
    • 77950267914 scopus 로고    scopus 로고
    • Distinct subcellular localization in the cytosol and apicoplast, unexpected dimerization and inhibition of Plasmodium falciparum glyoxalases
    • Urscher M., Przyborski J.M., Imoto M., Deponte M. Distinct subcellular localization in the cytosol and apicoplast, unexpected dimerization and inhibition of Plasmodium falciparum glyoxalases. Mol. Microbiol. 2010, 76:92-103.
    • (2010) Mol. Microbiol. , vol.76 , pp. 92-103
    • Urscher, M.1    Przyborski, J.M.2    Imoto, M.3    Deponte, M.4
  • 37
    • 4444278762 scopus 로고    scopus 로고
    • A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major
    • Vickers T.J., Greig N., Fairlamb A.H. A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:13186-13191.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13186-13191
    • Vickers, T.J.1    Greig, N.2    Fairlamb, A.H.3
  • 38
    • 56549120525 scopus 로고    scopus 로고
    • Glyoxalase II does not support methylglyoxal detoxification but serves as a general trypanothione thioesterase in African trypanosomes
    • Wendler A., Irsch T., Rabbani N., Thornalley P.J., Krauth-Siegel R.L. Glyoxalase II does not support methylglyoxal detoxification but serves as a general trypanothione thioesterase in African trypanosomes. Mol. Biochem. Parasitol. 2009, 163:19-27.
    • (2009) Mol. Biochem. Parasitol. , vol.163 , pp. 19-27
    • Wendler, A.1    Irsch, T.2    Rabbani, N.3    Thornalley, P.J.4    Krauth-Siegel, R.L.5


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