메뉴 건너뛰기




Volumn 1794, Issue 10, 2009, Pages 1496-1504

Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix

Author keywords

LDH like MDH; Aeropyrum pernix; Crystal structure; Hyperthermophilic archaea; Malate dehydrogenase; Refolding

Indexed keywords

ARGININE; GUANIDINE; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN SUBUNIT; TARTARIC ACID DERIVATIVE;

EID: 69449093925     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.06.014     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 77956935111 scopus 로고
    • Malate dehydrogenase
    • Boyer P.D.E. (Ed), Academic Press, New York
    • rd ed. (1975), Academic Press, New York 369-396
    • (1975) rd ed. , pp. 369-396
    • Banaszak, L.J.1    Bradshaw, R.A.2
  • 2
    • 0019323530 scopus 로고
    • Malate dehydrogenase from thermophilic and mesophilic bacteria: molecular size, subunit structure, amino acid composition, immunochemical homology, and catalytic activity
    • Sundaram T.K., Wright I.P., and Wilkinson A.E. Malate dehydrogenase from thermophilic and mesophilic bacteria: molecular size, subunit structure, amino acid composition, immunochemical homology, and catalytic activity. Biochemistry 19 (1980) 2017-2022
    • (1980) Biochemistry , vol.19 , pp. 2017-2022
    • Sundaram, T.K.1    Wright, I.P.2    Wilkinson, A.E.3
  • 3
    • 0028113441 scopus 로고
    • Malate dehydrogenase: a model for structure, evolution, and catalysis
    • Goward C.R., and Nicholls D.J. Malate dehydrogenase: a model for structure, evolution, and catalysis. Protein Sci. 3 (1994) 1883-1888
    • (1994) Protein Sci. , vol.3 , pp. 1883-1888
    • Goward, C.R.1    Nicholls, D.J.2
  • 5
    • 0036100822 scopus 로고    scopus 로고
    • Molecular evolution within the l-malate and l-lactate dehydrogenase super-family
    • Madern D. Molecular evolution within the l-malate and l-lactate dehydrogenase super-family. J. Mol. Evol. 54 (2002) 825-840
    • (2002) J. Mol. Evol. , vol.54 , pp. 825-840
    • Madern, D.1
  • 6
    • 0023301203 scopus 로고
    • Crystalline NAD/NADP dependent-malate dehydrogenase; the enzyme from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • Hartl T., Grossebuter W., Gorisch H., and Stezowski J.J. Crystalline NAD/NADP dependent-malate dehydrogenase; the enzyme from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biol. Chem. Hoppe-Seyler 368 (1987) 259-267
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 259-267
    • Hartl, T.1    Grossebuter, W.2    Gorisch, H.3    Stezowski, J.J.4
  • 7
    • 0022730826 scopus 로고
    • Purification and properties of malate dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum
    • Grossebuter W., Hartl T., Gorisch H., and Stezowski J.J. Purification and properties of malate dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biol. Chem. Hoppe-Seyler 367 (1986) 457-463
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 457-463
    • Grossebuter, W.1    Hartl, T.2    Gorisch, H.3    Stezowski, J.J.4
  • 8
    • 0027195301 scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui
    • Cendrin F., Chroboczek J., Zaccai G., Eisenberg H., and Mevarech M. Cloning, sequencing and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry 32 (1993) 4308-4313
    • (1993) Biochemistry , vol.32 , pp. 4308-4313
    • Cendrin, F.1    Chroboczek, J.2    Zaccai, G.3    Eisenberg, H.4    Mevarech, M.5
  • 9
    • 0030829444 scopus 로고    scopus 로고
    • Properties and primary structure of a thermostable l-malate dehydrogenase from Archaeoglobus fulgidus
    • Langelandsvik A.S., Steen H., Birkeland N.K., and Lien T. Properties and primary structure of a thermostable l-malate dehydrogenase from Archaeoglobus fulgidus. Arch Microbiol. 168 (1997) 59-67
    • (1997) Arch Microbiol. , vol.168 , pp. 59-67
    • Langelandsvik, A.S.1    Steen, H.2    Birkeland, N.K.3    Lien, T.4
  • 10
    • 0035964362 scopus 로고    scopus 로고
    • Differences in the oligomeric states of the LDH-like l-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus
    • Madern D., Ebel C., Dale H.A., Lien T., Steen I.H., Birkeland N.K., and Zaccai G. Differences in the oligomeric states of the LDH-like l-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus. Biochemistry 40 (2001) 10310-10316
    • (2001) Biochemistry , vol.40 , pp. 10310-10316
    • Madern, D.1    Ebel, C.2    Dale, H.A.3    Lien, T.4    Steen, I.H.5    Birkeland, N.K.6    Zaccai, G.7
  • 11
    • 0033775447 scopus 로고    scopus 로고
    • The putative l-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent l-malate dehydrogenase
    • Madern D. The putative l-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent l-malate dehydrogenase. Mol. Microbiol. 37 (2000) 1515-1520
    • (2000) Mol. Microbiol. , vol.37 , pp. 1515-1520
    • Madern, D.1
  • 12
    • 34548359107 scopus 로고    scopus 로고
    • Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum
    • Yennaco L.J., Hu Y., and Holden J.F. Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum. Extremophiles 11 (2007) 741-746
    • (2007) Extremophiles , vol.11 , pp. 741-746
    • Yennaco, L.J.1    Hu, Y.2    Holden, J.F.3
  • 13
    • 0034620588 scopus 로고    scopus 로고
    • Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui
    • Richard S.B., Madern D., Garcin E., and Zaccai G. Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry 39 (2000) 992-1000
    • (2000) Biochemistry , vol.39 , pp. 992-1000
    • Richard, S.B.1    Madern, D.2    Garcin, E.3    Zaccai, G.4
  • 14
    • 0034620517 scopus 로고    scopus 로고
    • Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric l-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui
    • Madern D., Ebel C., Mevarech M., Richard S.B., Pfister C., and Zaccai G. Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric l-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui. Biochemistry 39 (2000) 1001-1010
    • (2000) Biochemistry , vol.39 , pp. 1001-1010
    • Madern, D.1    Ebel, C.2    Mevarech, M.3    Richard, S.B.4    Pfister, C.5    Zaccai, G.6
  • 15
    • 0035853289 scopus 로고    scopus 로고
    • Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases
    • Lee B.I., Chang C., Cho S.J., Eom S.H., Kim K.K., Yu Y.G., and Suh S.W. Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. J. Mol. Biol. 307 (2001) 1351-1362
    • (2001) J. Mol. Biol. , vol.307 , pp. 1351-1362
    • Lee, B.I.1    Chang, C.2    Cho, S.J.3    Eom, S.H.4    Kim, K.K.5    Yu, Y.G.6    Suh, S.W.7
  • 16
    • 0345118104 scopus 로고    scopus 로고
    • The 2.9 Å resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilization
    • Irimia A., Vellieux F.M., Madern D., Zaccai G., Karshikoff A., Tibbelin G., Ladenstein R., Lien T., and Birkeland N.K. The 2.9 Å resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilization. J. Mol. Biol. 335 (2004) 343-356
    • (2004) J. Mol. Biol. , vol.335 , pp. 343-356
    • Irimia, A.1    Vellieux, F.M.2    Madern, D.3    Zaccai, G.4    Karshikoff, A.5    Tibbelin, G.6    Ladenstein, R.7    Lien, T.8    Birkeland, N.K.9
  • 17
    • 0029826916 scopus 로고    scopus 로고
    • Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C
    • Sako Y., Nomura N., Uchida A., Ishida Y., Morii H., Koga Y., Hoaki T., and Maruyama T. Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C. Int. J. Syst. Bacteriol. 46 (1996) 1070-1077
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 1070-1077
    • Sako, Y.1    Nomura, N.2    Uchida, A.3    Ishida, Y.4    Morii, H.5    Koga, Y.6    Hoaki, T.7    Maruyama, T.8
  • 20
    • 0011726133 scopus 로고
    • Isolation and properties of malic dehydrogenase from ox-heart mitochondria
    • Davies D.D., and Kun E. Isolation and properties of malic dehydrogenase from ox-heart mitochondria. Biochem. J. 66 (1957) 307-316
    • (1957) Biochem. J. , vol.66 , pp. 307-316
    • Davies, D.D.1    Kun, E.2
  • 21
    • 0016836410 scopus 로고
    • Purification and properties of malate dehydrogenase from Pseudomonas testosteroni
    • You K.S., and Kaplan N.O. Purification and properties of malate dehydrogenase from Pseudomonas testosteroni. J. Bacteriol. 123 (1975) 704-716
    • (1975) J. Bacteriol. , vol.123 , pp. 704-716
    • You, K.S.1    Kaplan, N.O.2
  • 22
    • 0017224135 scopus 로고
    • Purification and properties of malate-NAD+ dehydrogenase of Moraxella lwoffi (N.C.I.B. 8250)
    • Fernandes R., Jones M., and King H.K. Purification and properties of malate-NAD+ dehydrogenase of Moraxella lwoffi (N.C.I.B. 8250). Biochem. Soc. Trans. 4 (1976) 1080
    • (1976) Biochem. Soc. Trans. , vol.4 , pp. 1080
    • Fernandes, R.1    Jones, M.2    King, H.K.3
  • 23
    • 0022630727 scopus 로고
    • Purification and characterization of malate dehydrogenase from the phototrophic bacterium, Rhodopseudomonas capslata
    • Ohshima T., and Sakuraba H. Purification and characterization of malate dehydrogenase from the phototrophic bacterium, Rhodopseudomonas capslata. Biochim. Biophys. Acta 869 (1986) 171-177
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 171-177
    • Ohshima, T.1    Sakuraba, H.2
  • 24
    • 0034572477 scopus 로고    scopus 로고
    • Glutamate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1: enzymatic characterization, identification of the encoding gene, and phylogenetic implications
    • Bhuiya M.W., Sakuraba H., Kujo C., Nunoura-Kominato N., Kawarabayasi Y., Kikuchi H., and Ohshima T. Glutamate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1: enzymatic characterization, identification of the encoding gene, and phylogenetic implications. Extremophiles 4 (2000) 333-341
    • (2000) Extremophiles , vol.4 , pp. 333-341
    • Bhuiya, M.W.1    Sakuraba, H.2    Kujo, C.3    Nunoura-Kominato, N.4    Kawarabayasi, Y.5    Kikuchi, H.6    Ohshima, T.7
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 28
    • 78651153791 scopus 로고
    • Disc electrophoresis-2. Method and application to human serum proteins
    • Davis B.J. Disc electrophoresis-2. Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 121 (1964) 404-427
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Leammli U.K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Leammli, U.K.1
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
  • 32
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution, density modification and model building
    • Terwilliger T. SOLVE and RESOLVE: automated structure solution, density modification and model building. J. Synchrotron. Radiat. 11 (2004) 49-52
    • (2004) J. Synchrotron. Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 33
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 34
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 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
  • 37
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: three related resources
    • Rodriguez R., Chinea G., Lopez N., Pons T., and Vriend G. Homology modeling, model and software evaluation: three related resources. Bioinformatics 14 (1998) 523-528
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 39
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • Lee B., and Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55 (1971) 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 40
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 42
    • 0026685776 scopus 로고
    • Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Implications for nucleotide specificity
    • Baker P.J., Britton K.L., Rice D.W., Rob A., and Stillman T.J. Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Implications for nucleotide specificity. J. Mol. Biol. 228 (1992) 662-671
    • (1992) J. Mol. Biol. , vol.228 , pp. 662-671
    • Baker, P.J.1    Britton, K.L.2    Rice, D.W.3    Rob, A.4    Stillman, T.J.5
  • 43
    • 0033555285 scopus 로고    scopus 로고
    • Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, α-ketomalonate and tetrahydroNAD
    • Chapman A.D.M., Cortes A., Dafforn T.R., Clarke A.R., and Brady R.L. Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, α-ketomalonate and tetrahydroNAD. J. Mol. Biol. 285 (1999) 703-712
    • (1999) J. Mol. Biol. , vol.285 , pp. 703-712
    • Chapman, A.D.M.1    Cortes, A.2    Dafforn, T.R.3    Clarke, A.R.4    Brady, R.L.5
  • 44
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan M.K., Mukund S., Kletzin A., Adams M.W., and Rees D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267 (1995) 1463-1469
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.4    Rees, D.C.5
  • 46
  • 47
    • 0028994307 scopus 로고
    • 2.0 Å structure of indol-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability
    • Henning M., Darimont B., Sterner R., Kirschner K., and Jansonius J.N. 2.0 Å structure of indol-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Science 3 (1995) 1295-1306
    • (1995) Science , vol.3 , pp. 1295-1306
    • Henning, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.