메뉴 건너뛰기




Volumn 45, Issue 40, 2006, Pages 12366-12379

Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: A precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; CELL EXTRACTS; METHYLGLYOXAL;

EID: 33749509235     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061018a     Document Type: Article
Times cited : (39)

References (50)
  • 1
    • 2942563977 scopus 로고    scopus 로고
    • L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii
    • White, R. H. (2004) L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii, Biochemistry 43, 7618-7627.
    • (2004) Biochemistry , vol.43 , pp. 7618-7627
    • White, R.H.1
  • 2
    • 0037207137 scopus 로고    scopus 로고
    • Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: Implications for ligand binding and specificity
    • Mulichak, A. M., Bonin, C. P., Reiter, W. D., and Garavito, R. M. (2002) Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity, Biochemistry 41, 15578-15589.
    • (2002) Biochemistry , vol.41 , pp. 15578-15589
    • Mulichak, A.M.1    Bonin, C.P.2    Reiter, W.D.3    Garavito, R.M.4
  • 6
    • 0742321718 scopus 로고    scopus 로고
    • Glucose-6-phosphate isomerase from the hyperthermophilic archaeon Methanococcus jannaschii: Characterization of the first archaeal member of the phosphoglucose isomerase superfamily
    • Rudolph, B., Hansen, T., and Schonheit, P. (2004) Glucose-6-phosphate isomerase from the hyperthermophilic archaeon Methanococcus jannaschii: characterization of the first archaeal member of the phosphoglucose isomerase superfamily, Arch. Microbiol. 181, 82-87.
    • (2004) Arch. Microbiol. , vol.181 , pp. 82-87
    • Rudolph, B.1    Hansen, T.2    Schonheit, P.3
  • 8
    • 0030969906 scopus 로고    scopus 로고
    • Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli
    • Thoden, J. B., Hegeman, A. D., Wesenberg, G., Chapeau, M. C., Frey, P. A., and Holden, H. M. (1997) Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli, Biochemistry 36, 6294-6304.
    • (1997) Biochemistry , vol.36 , pp. 6294-6304
    • Thoden, J.B.1    Hegeman, A.D.2    Wesenberg, G.3    Chapeau, M.C.4    Frey, P.A.5    Holden, H.M.6
  • 9
    • 4544272017 scopus 로고    scopus 로고
    • Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea
    • Finn, M. W., and Tabita, F. R. (2004) Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea, J. Bacteriol. 186, 6360-6366.
    • (2004) J. Bacteriol. , vol.186 , pp. 6360-6366
    • Finn, M.W.1    Tabita, F.R.2
  • 10
    • 0035106495 scopus 로고    scopus 로고
    • Different glycolytic pathways for glucose and fructose in the halophilic archaeon Halococcus saccharolyticus
    • Johnsen, U., Selig, M., Xavier, K. B., Santos, H., and Schonheit, P. (2001) Different glycolytic pathways for glucose and fructose in the halophilic archaeon Halococcus saccharolyticus, Arch. Microbiol. 175, 52-61.
    • (2001) Arch. Microbiol. , vol.175 , pp. 52-61
    • Johnsen, U.1    Selig, M.2    Xavier, K.B.3    Santos, H.4    Schonheit, P.5
  • 11
    • 3042565616 scopus 로고    scopus 로고
    • Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Rashid, N., Imanaka, H., Fukui, T., Atomi, H., and Imanaka, T. (2004) Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis, J. Bacteriol. 186, 4185-4191.
    • (2004) J. Bacteriol. , vol.186 , pp. 4185-4191
    • Rashid, N.1    Imanaka, H.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5
  • 12
    • 4444268422 scopus 로고    scopus 로고
    • Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis
    • Rashid, N., Kanai, T., Atomi, H., and Imanaka, T. (2004) Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis, J. Bacteriol. 186, 6070-6076.
    • (2004) J. Bacteriol. , vol.186 , pp. 6070-6076
    • Rashid, N.1    Kanai, T.2    Atomi, H.3    Imanaka, T.4
  • 13
    • 33749505564 scopus 로고
    • Some properties of synthetic UDP(2)-fructose
    • Taniguchi, H., and Nakamura, M. (1972) Some properties of synthetic UDP(2)-fructose, Agric. Biol. Chem. 36, 2185-2194.
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 2185-2194
    • Taniguchi, H.1    Nakamura, M.2
  • 14
    • 0019888319 scopus 로고
    • The structure of "activation factor" for phosphofructokinase
    • Uyeda, K., Furuya, E., and Sherry, A. D. (1981) The structure of "activation factor" for phosphofructokinase, J. Biol. Chem. 256, 8679-8684.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8679-8684
    • Uyeda, K.1    Furuya, E.2    Sherry, A.D.3
  • 15
    • 0023884193 scopus 로고
    • Purification and characterization of myocardial fructose-6-phosphate,2- kinase and fructose-2,6-bisphosphatase
    • Kitamura, K., and Uyeda, K. (1988) Purification and characterization of myocardial fructose-6-phosphate,2-kinase and fructose-2,6-bisphosphatase, J. Biol. Chem. 263, 9027-9033.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9027-9033
    • Kitamura, K.1    Uyeda, K.2
  • 16
    • 0023140540 scopus 로고
    • Fructose 2-phosphate, an intermediate of the dephosphorylation of fructose 2,6-bisphosphate with a purified yeast enzyme
    • Purwin, C., Laux, M., and Holzer, H. (1987) Fructose 2-phosphate, an intermediate of the dephosphorylation of fructose 2,6-bisphosphate with a purified yeast enzyme, Eur. J. Biochem. 164, 27-30.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 27-30
    • Purwin, C.1    Laux, M.2    Holzer, H.3
  • 17
    • 0023214561 scopus 로고
    • Fructofuranose 2-phosphate is the product of dephosphorylation of fructose 2,6-bisphosphate
    • Purwin, C., Laux, M., and Holzer, H. (1987) Fructofuranose 2-phosphate is the product of dephosphorylation of fructose 2,6-bisphosphate, Eur. J. Biochem. 165, 543-545.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 543-545
    • Purwin, C.1    Laux, M.2    Holzer, H.3
  • 18
    • 0030200936 scopus 로고    scopus 로고
    • Method for determination of free intracellular and extracellular methylglyoxal in animal cells grown in culture
    • Chaplen, F. W., Fahl, W. E., and Cameron, D. C. (1996) Method for determination of free intracellular and extracellular methylglyoxal in animal cells grown in culture, Anal. Biochem. 238, 171-178.
    • (1996) Anal. Biochem. , vol.238 , pp. 171-178
    • Chaplen, F.W.1    Fahl, W.E.2    Cameron, D.C.3
  • 19
    • 0032703938 scopus 로고    scopus 로고
    • Methylglyoxal in living organisms: Chemistry, biochemistry, toxicology and biological implications
    • Kalapos, M. P. (1999) Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications, Toxicol. Lett. 110, 145-175.
    • (1999) Toxicol. Lett. , vol.110 , pp. 145-175
    • Kalapos, M.P.1
  • 20
  • 21
    • 0022356242 scopus 로고
    • Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae
    • Murata, K., Fukuda, Y., Simosaka, M., Watanabe, K., Saikusa, T., and Kimura, A. (1985) Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae, Eur. J. Biochem. 151, 631-636.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 631-636
    • Murata, K.1    Fukuda, Y.2    Simosaka, M.3    Watanabe, K.4    Saikusa, T.5    Kimura, A.6
  • 22
    • 0028605299 scopus 로고
    • Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with Na-acetylarginine, Na-acetylcysteine, and Na-acetyllysine, and bovine serum albumin
    • Lo, T. W., Westwood, M. E., McLellan, A. C., Selwood, T., and Thornalley, P. J. (1994) Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with Na-acetylarginine, Na-acetylcysteine, and Na-acetyllysine, and bovine serum albumin, J. Biol. Chem. 269, 32299-32305.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32299-32305
    • Lo, T.W.1    Westwood, M.E.2    McLellan, A.C.3    Selwood, T.4    Thornalley, P.J.5
  • 23
    • 12844281130 scopus 로고    scopus 로고
    • Methylglyoxal, a metabolite derived from glycolysis, functions as a signal initiator of the high osmolarity glycerol-mitogen-activated protein kinase cascade and calcineurin/Crzl-mediated pathway in Saccharomyces cerevisiae
    • Maeta, K., Izawa, S., and Inoue, Y. (2005) Methylglyoxal, a metabolite derived from glycolysis, functions as a signal initiator of the high osmolarity glycerol-mitogen-activated protein kinase cascade and calcineurin/Crzl-mediated pathway in Saccharomyces cerevisiae, J. Biol. Chem. 280, 253-260.
    • (2005) J. Biol. Chem. , vol.280 , pp. 253-260
    • Maeta, K.1    Izawa, S.2    Inoue, Y.3
  • 24
    • 33749536636 scopus 로고
    • Ketoaldehydes and cell devision
    • Szent-Gyorgyi, A. (1965) Ketoaldehydes and cell devision, Science 155, 529-541.
    • (1965) Science , vol.155 , pp. 529-541
    • Szent-Gyorgyi, A.1
  • 25
    • 0021471746 scopus 로고
    • Acid-base catalysis of the elimination and isomerization reactions of triose phosphates
    • Richard, J. P. (1984) Acid-base catalysis of the elimination and isomerization reactions of triose phosphates, J. Am. Chem. Soc. 106, 4926-4936.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 4926-4936
    • Richard, J.P.1
  • 26
    • 0025787465 scopus 로고
    • Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance
    • Richard, J. P. (1991) Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance, Biochemistry 30, 4581-4585.
    • (1991) Biochemistry , vol.30 , pp. 4581-4585
    • Richard, J.P.1
  • 27
    • 0034696583 scopus 로고    scopus 로고
    • Mirroring perfection: The structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate
    • Saadat, D., and Harrison, D. H. (2000) Mirroring perfection: the structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate, Biochemistry 39, 2950-2960.
    • (2000) Biochemistry , vol.39 , pp. 2950-2960
    • Saadat, D.1    Harrison, D.H.2
  • 28
    • 0014216330 scopus 로고
    • The conversion of acetoacetate to pyruvaldehyde
    • Mulligan, L. P., and Baldwin, R. L. (1967) The conversion of acetoacetate to pyruvaldehyde, J. Biol. Chem. 242, 1095-1101.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1095-1101
    • Mulligan, L.P.1    Baldwin, R.L.2
  • 29
    • 50549205066 scopus 로고
    • The metabolism of lactaldehyde VII. The oxidation of D-lactaldehyde in rat liver
    • Ting, S. M., Miller, O. N., and Sellinger, O. Z. (1967) The metabolism of lactaldehyde VII. The oxidation of D-lactaldehyde in rat liver, Biochim. Biophys. Acta 97, 407-415.
    • (1967) Biochim. Biophys. Acta , vol.97 , pp. 407-415
    • Ting, S.M.1    Miller, O.N.2    Sellinger, O.Z.3
  • 31
    • 0032731169 scopus 로고    scopus 로고
    • Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities
    • Mukhopadhyay, B., Johnson, E. F., and Wolfe, R. S. (1999) Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities, Appl. Environ. Microbiol. 65, 5059-5065.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5059-5065
    • Mukhopadhyay, B.1    Johnson, E.F.2    Wolfe, R.S.3
  • 33
    • 0016417438 scopus 로고
    • Glucose-6-phosphate isomerase from peas
    • Hizukuri, S., Takeda, Y., and Nikuni, Z. (1975) Glucose-6-phosphate isomerase from peas, Methods Enzymol. 41, 388-392.
    • (1975) Methods Enzymol. , vol.41 , pp. 388-392
    • Hizukuri, S.1    Takeda, Y.2    Nikuni, Z.3
  • 34
    • 0001311609 scopus 로고
    • A kinetic study of the phosphoglucomutase pathway
    • Ray, W. J., Jr., and Roscelli, G. A. (1964) A kinetic study of the phosphoglucomutase pathway, J. Biol. Chem. 239, 1228-1236.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1228-1236
    • Ray Jr., W.J.1    Roscelli, G.A.2
  • 35
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames, B. N. (1966) Assay of inorganic phosphate, total phosphate and phosphatases, Methods Enzymol. 8, 115-118.
    • (1966) Methods Enzymol. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 36
    • 0000322762 scopus 로고
    • Thymidine diphosphate 4-keto-6-deoxy-D-glucose, an intermediate in thymidine diphosphate L-rhamnose synthesis in Escherichia coli strains
    • Okazaki, R., Okazakit, Strominger, J. L., and Michelson, A. M. (1962) Thymidine diphosphate 4-keto-6-deoxy-D-glucose, an intermediate in thymidine diphosphate L-rhamnose synthesis in Escherichia coli strains, J. Biol. Chem. 237, 3014-3026.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3014-3026
    • Okazaki, R.1    Okazakit2    Strominger, J.L.3    Michelson, A.M.4
  • 37
    • 0034649430 scopus 로고    scopus 로고
    • Characterization of enzymatic processes by rapid mix-quench mass spectrometry: The case of dTDP-glucose 4,6-dehydratase
    • Gross, J. W., Hegeman, A. D., Vestling, M. M., and Frey, P. A. (2000) Characterization of enzymatic processes by rapid mix-quench mass spectrometry: the case of dTDP-glucose 4,6-dehydratase, Biochemistry 39, 13633-13640.
    • (2000) Biochemistry , vol.39 , pp. 13633-13640
    • Gross, J.W.1    Hegeman, A.D.2    Vestling, M.M.3    Frey, P.A.4
  • 38
    • 0030039967 scopus 로고    scopus 로고
    • Methylglyoxal assay in cells as 2-methylquinoxaline using 1,2-diaminobenzene as derivatizing reagent
    • Cordeiro, C., and Freire, A. P. (1996) Methylglyoxal assay in cells as 2-methylquinoxaline using 1,2-diaminobenzene as derivatizing reagent, Anal. Biochem. 234, 221-223.
    • (1996) Anal. Biochem. , vol.234 , pp. 221-223
    • Cordeiro, C.1    Freire, A.P.2
  • 39
    • 33845552346 scopus 로고
    • Chemical and enzymatic syntheses of 6-deoxyhexoses. Conversion to 2,5-dimethyl-4-hydroxy-2,3-dihydrofuran-3-one (Furaneol) and analogues
    • Wong, C.-H., Mazenod, F. P., and Whitesides, G. M. (1983) Chemical and enzymatic syntheses of 6-deoxyhexoses. Conversion to 2,5-dimethyl-4-hydroxy-2,3- dihydrofuran-3-one (Furaneol) and analogues, J. Org. Chem. 48, 3493-3497.
    • (1983) J. Org. Chem. , vol.48 , pp. 3493-3497
    • Wong, C.-H.1    Mazenod, F.P.2    Whitesides, G.M.3
  • 40
    • 84981946690 scopus 로고
    • Epimerization of carbohydroates catalyzed by molybdate ions
    • Bilik, V., Voelter, W., and Bayer, E. (1971) Epimerization of carbohydroates catalyzed by molybdate ions, Angew. Chem., Int. Ed. Engl. 10, 909.
    • (1971) Angew. Chem., Int. Ed. Engl. , vol.10 , pp. 909
    • Bilik, V.1    Voelter, W.2    Bayer, E.3
  • 43
    • 0021703678 scopus 로고
    • Identification of 6-deoxyallitol and 6-deoxygulitol in human urine. Electron-impact mass spectra of eight isomers of 6-deoxyhexitol
    • Niwa, T., Yamada, K., Ohki, T., Saito, A., and Mori, M. (1984) Identification of 6-deoxyallitol and 6-deoxygulitol in human urine. Electron-impact mass spectra of eight isomers of 6-deoxyhexitol, J. Chromatogr. 336, 345-350.
    • (1984) J. Chromatogr. , vol.336 , pp. 345-350
    • Niwa, T.1    Yamada, K.2    Ohki, T.3    Saito, A.4    Mori, M.5
  • 44
    • 4344692495 scopus 로고    scopus 로고
    • Genetic evidence identifying the true gluconeogenic fructose-1,6- bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles
    • Sato, T., Imanaka, H., Rashid, N., Fukui, T., Atomi, H., and Imanaka, T. (2004) Genetic evidence identifying the true gluconeogenic fructose-1,6- bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles, J. Bacteriol. 186, 5799-5807.
    • (2004) J. Bacteriol. , vol.186 , pp. 5799-5807
    • Sato, T.1    Imanaka, H.2    Rashid, N.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 45
    • 0019876998 scopus 로고
    • Formation of hydroxypyruvaldehyde phosphate in human erythrocytes
    • Cogoli-Greuter, M., and Christen, P. (1981) Formation of hydroxypyruvaldehyde phosphate in human erythrocytes, J. Biol. Chem. 256, 5708-5711.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5708-5711
    • Cogoli-Greuter, M.1    Christen, P.2
  • 46
    • 20444488776 scopus 로고    scopus 로고
    • Identification and characterization of the unique N-linked glycan common to the flagellins and 5-layer glycoprotein of Methanococcus voltae
    • Voisin, S., Houliston, R. S., Kelly, J., Brisson, J. R., Watson, D., Bardy, S. L., Jarrell, K. F., and Logan, S. M. (2005) Identification and characterization of the unique N-linked glycan common to the flagellins and 5-layer glycoprotein of Methanococcus voltae, J. Biol. Chem. 280, 16586-16593.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16586-16593
    • Voisin, S.1    Houliston, R.S.2    Kelly, J.3    Brisson, J.R.4    Watson, D.5    Bardy, S.L.6    Jarrell, K.F.7    Logan, S.M.8
  • 47
    • 0003740963 scopus 로고
    • The structure and chemical composition of the S-layer
    • Severina, L. O. (1995) The structure and chemical composition of the S-layer, Microbiology (Moscow) 64, 336-340.
    • (1995) Microbiology (Moscow) , vol.64 , pp. 336-340
    • Severina, L.O.1
  • 48
    • 0035800865 scopus 로고    scopus 로고
    • Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase
    • Siebers, B., Brinkmann, H., Dorr, C., Tjaden, B., Lilie, H., van der Oost, J., and Verhees, C. H. (2001) Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase, J. Biol. Chem. 276, 28710-28728.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28710-28728
    • Siebers, B.1    Brinkmann, H.2    Dorr, C.3    Tjaden, B.4    Lilie, H.5    Van Der Oost, J.6    Verhees, C.H.7
  • 50
    • 0027396022 scopus 로고
    • The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal
    • Phillips, S. A., and Thornalley, P. J. (1993) The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal, Eur. J. Biochem. 212, 101-105.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.