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Volumn 272, Issue 24, 2005, Pages 6266-6275

Mutagenesis of catalytically important residues of cupin type phosphoglucose isomerase from Archaeoglobus fulgidus

Author keywords

Archaeoglobus fulgidus; Cupin; Mutagenesis; Phosphoglucose isomerase

Indexed keywords

GLUCOSE 6 PHOSPHATE ISOMERASE; NICKEL;

EID: 29144498155     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.05007.x     Document Type: Article
Times cited : (11)

References (34)
  • 1
    • 77956945618 scopus 로고
    • Aldose-Ketose Isomerases
    • (Boyer, PD, ed.). Academic Press, New York
    • Noltmann EA (1972) Aldose-Ketose Isomerases. In The Enzymes (Boyer, PD, ed.), pp. 271-354. Academic Press, New York.
    • (1972) The Enzymes , pp. 271-354
    • Noltmann, E.A.1
  • 2
    • 0035036956 scopus 로고    scopus 로고
    • Novel type of glucose-6-phosphate isomerase in the hyperthermophilic archaeon Pyrococcus furiosus
    • Hansen T, Oehlmann M & Schönheit P (2001) Novel type of glucose-6-phosphate isomerase in the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 183, 3428-3435.
    • (2001) J Bacteriol , vol.183 , pp. 3428-3435
    • Hansen, T.1    Oehlmann, M.2    Schönheit, P.3
  • 4
    • 14244253114 scopus 로고    scopus 로고
    • Cupin-type phosphoglucose isomerases (Cupin-PGIs) constitute a novel metal-dependent PGI family representing a convergent line of PGI evolution
    • Hansen T, Schlichting B, Felgendreher M & Schönheit P (2005) Cupin-type phosphoglucose isomerases (Cupin-PGIs) constitute a novel metal-dependent PGI family representing a convergent line of PGI evolution. J Bacteriol 187, 1621-1631.
    • (2005) J Bacteriol , vol.187 , pp. 1621-1631
    • Hansen, T.1    Schlichting, B.2    Felgendreher, M.3    Schönheit, P.4
  • 5
    • 0347717806 scopus 로고    scopus 로고
    • Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily
    • Hansen T, Wendorff D & Schönheit P (2004) Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily. J Biol Chem 279, 2262-2272.
    • (2004) J Biol Chem , vol.279 , pp. 2262-2272
    • Hansen, T.1    Wendorff, D.2    Schönheit, P.3
  • 6
    • 0035798696 scopus 로고    scopus 로고
    • The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin superfamily
    • Verhees CH, Huynen MA, Ward DE, Schiltz E, De Vos WM & Van der Oost J (2001) The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin superfamily. J Biol Chem 276, 40926-40932.
    • (2001) J Biol Chem , vol.276 , pp. 40926-40932
    • Verhees, C.H.1    Huynen, M.A.2    Ward, D.E.3    Schiltz, E.4    De Vos, W.M.5    Van Der Oost, J.6
  • 7
    • 0037472632 scopus 로고    scopus 로고
    • Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis (1)
    • Jeong JJ, Fushinobu S, Ito S, Jeon BS, Shoun H & Wakagi T (2003) Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis (1). FEBS Lett 535, 200-204.
    • (2003) FEBS Lett , vol.535 , pp. 200-204
    • Jeong, J.J.1    Fushinobu, S.2    Ito, S.3    Jeon, B.S.4    Shoun, H.5    Wakagi, T.6
  • 8
    • 0035369540 scopus 로고    scopus 로고
    • The crystal structure of human phosphoglucose isomerase at 1.6 a resolution: Implications for catalytic mechanism, cytokine activity and haemolytic anaemia
    • Read J, Pearce J, Li X, Muirhead H, Chirgwin J & Davies C (2001) The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia. J Mol Biol 309, 447-463.
    • (2001) J Mol Biol , vol.309 , pp. 447-463
    • Read, J.1    Pearce, J.2    Li, X.3    Muirhead, H.4    Chirgwin, J.5    Davies, C.6
  • 9
    • 0035800048 scopus 로고    scopus 로고
    • Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate
    • Lee JH, Chang KZ, Patel V & Jeffery CJ (2001) Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate. Biochemistry 40, 7799-7805.
    • (2001) Biochemistry , vol.40 , pp. 7799-7805
    • Lee, J.H.1    Chang, K.Z.2    Patel, V.3    Jeffery, C.J.4
  • 10
    • 0038383074 scopus 로고    scopus 로고
    • The structure of human phosphoglucose isomerase complexed with a transition-state analogue
    • Davies C, Muirhead H & Chirgwin J (2003) The structure of human phosphoglucose isomerase complexed with a transition-state analogue. Acta Crystallogr D Biol Crystallogr 59, 1111-1113.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 1111-1113
    • Davies, C.1    Muirhead, H.2    Chirgwin, J.3
  • 11
    • 0037348344 scopus 로고    scopus 로고
    • Structure of native phosphoglucose isomerase from rabbit: Conformational changes associated with catalytic function
    • Davies C & Muirhead H (2003) Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function. Acta Crystallogr D Biol Crystallogr 59, 453-465.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 453-465
    • Davies, C.1    Muirhead, H.2
  • 12
    • 0036891696 scopus 로고    scopus 로고
    • Crystal structure of phosphoglucose isomerase from pig muscle and its complex with 5-phosphoarabinonate
    • Davies C & Muirhead H (2002) Crystal structure of phosphoglucose isomerase from pig muscle and its complex with 5-phosphoarabinonate. Proteins 49, 577-579.
    • (2002) Proteins , vol.49 , pp. 577-579
    • Davies, C.1    Muirhead, H.2
  • 13
    • 4444298888 scopus 로고    scopus 로고
    • The crystal structure of mouse phosphoglucose isomerase at 1.6 Å resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening
    • Graham Solomons JTG, Zimmerly EM, Burns S, Krishnamurthy N, Swan MK, Krings S, Muirhead H, Chirgwin J & Davies C (2004) The crystal structure of mouse phosphoglucose isomerase at 1.6 Å resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening. J Mol Biol 342, 847-860.
    • (2004) J Mol Biol , vol.342 , pp. 847-860
    • Graham Solomons, J.T.G.1    Zimmerly, E.M.2    Burns, S.3    Krishnamurthy, N.4    Swan, M.K.5    Krings, S.6    Muirhead, H.7    Chirgwin, J.8    Davies, C.9
  • 14
    • 4544243688 scopus 로고    scopus 로고
    • A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: Structural evidence at 1.16-Å resolution
    • Swan MK, Hansen T, Schonheit P & Davies C (2004) A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-Å resolution. J Biol Chem 279, 39838-39845.
    • (2004) J Biol Chem , vol.279 , pp. 39838-39845
    • Swan, M.K.1    Hansen, T.2    Schonheit, P.3    Davies, C.4
  • 17
    • 0344012458 scopus 로고    scopus 로고
    • Structural evidence for a hydride transfer mechanism of catalysis in phosphoglucose isomerase from Pyrococcus furiosus
    • Swan MK, Solomons JT, Beeson CC, Hansen T, Schönheit P & Davies C (2003) Structural evidence for a hydride transfer mechanism of catalysis in phosphoglucose isomerase from Pyrococcus furiosus. J Biol Chem 278, 47261-47268.
    • (2003) J Biol Chem , vol.278 , pp. 47261-47268
    • Swan, M.K.1    Solomons, J.T.2    Beeson, C.C.3    Hansen, T.4    Schönheit, P.5    Davies, C.6
  • 18
    • 0033545874 scopus 로고    scopus 로고
    • The crystal structure of a multifunctional protein: Phosphoglucose isomerase/autocrine motility factor/neuroleukin
    • Sun YJ, Chou CC, Chen WS, Wu RT, Meng M & Hsiao CD (1999) The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin. Proc Natl Acad Sci USA 96, 5412-5417.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5412-5417
    • Sun, Y.J.1    Chou, C.C.2    Chen, W.S.3    Wu, R.T.4    Meng, M.5    Hsiao, C.D.6
  • 19
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: The most functionally diverse protein superfamily?
    • Dunwell JM, Purvis A & Khuri S (2004) Cupins: the most functionally diverse protein superfamily? Phytochemistry 65, 7-17.
    • (2004) Phytochemistry , vol.65 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 21
    • 0035065222 scopus 로고    scopus 로고
    • Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins
    • Khuri S, Bakker FT & Dunwell JM (2001) Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins. Mol Biol Evol 18, 593-605.
    • (2001) Mol Biol Evol , vol.18 , pp. 593-605
    • Khuri, S.1    Bakker, F.T.2    Dunwell, J.M.3
  • 22
    • 0025974544 scopus 로고
    • A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubiginosus structures with xylitol and D-xylose
    • Whitlow M, Howard AJ, Finzel BC, Poulos TL, Winborne E & Gilliland GL (1991) A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubiginosus structures with xylitol and D-xylose. Proteins 9, 153-173.
    • (1991) Proteins , vol.9 , pp. 153-173
    • Whitlow, M.1    Howard, A.J.2    Finzel, B.C.3    Poulos, T.L.4    Winborne, E.5    Gilliland, G.L.6
  • 24
    • 0034096459 scopus 로고    scopus 로고
    • Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily
    • Dunwell JM, Khuri S & Gane PJ (2000) Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily. Microbiol Mol Biol Rev 64, 153-179.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 153-179
    • Dunwell, J.M.1    Khuri, S.2    Gane, P.J.3
  • 25
    • 8344246304 scopus 로고    scopus 로고
    • Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: A subtle difference between distantly related enzymes
    • Swan MK, Hansen T, Schonheit P & Davies C (2004) Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes. Biochemistry 43, 14088-14095.
    • (2004) Biochemistry , vol.43 , pp. 14088-14095
    • Swan, M.K.1    Hansen, T.2    Schonheit, P.3    Davies, C.4
  • 26
    • 0015209375 scopus 로고
    • Proportion of keto and aldehydo forms in solutions of sugars and sugar phosphates
    • Swenson CA & Barker R (1971) Proportion of keto and aldehydo forms in solutions of sugars and sugar phosphates. Biochemistry 10, 3151-3154.
    • (1971) Biochemistry , vol.10 , pp. 3151-3154
    • Swenson, C.A.1    Barker, R.2
  • 27
    • 8344246304 scopus 로고    scopus 로고
    • Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: A subtle difference between distantly related enzymes
    • Swan MK, Hansen T, Schonheit P & Davies C (2004) Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes. Biochemistry 43, 14088-14095.
    • (2004) Biochemistry , vol.43 , pp. 14088-14095
    • Swan, M.K.1    Hansen, T.2    Schonheit, P.3    Davies, C.4
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW & Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47, 110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F & Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25, 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA & Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D 53, 240-255.
    • (1997) Acta Cryst D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS & Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26, 283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barken Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer J, Kuettner HC, Zhang JK, Hedderich R & Metcalf WW (2002) Genetic analysis of the archaeon Methanosarcina barken Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc Natl Acad Sci USA 99, 5632-5637.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.W.5
  • 34
    • 0037027540 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: Expression of the g6pd gene and characterization of an extremely thermophilic enzyme
    • Hansen T, Schlichting B & Schönheit P (2002) Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: expression of the g6pd gene and characterization of an extremely thermophilic enzyme. FEMS Microbiol Lett 216, 249-253.
    • (2002) FEMS Microbiol Lett , vol.216 , pp. 249-253
    • Hansen, T.1    Schlichting, B.2    Schönheit, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.