메뉴 건너뛰기




Volumn 69, Issue 10, 2005, Pages 1861-1870

Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis

Author keywords

Bacillus subtilis; Catalytic activity; Glutamate dehydrogenase; Random mutagenesis; Thermostability

Indexed keywords

AMINATION; BACTERIA; CATALYST ACTIVITY; CELLS; ENZYMES; ESCHERICHIA COLI; MOLECULAR STRUCTURE; MUTAGENESIS; REACTION KINETICS;

EID: 27644547321     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.69.1861     Document Type: Article
Times cited : (19)

References (42)
  • 1
    • 0003107498 scopus 로고
    • Glutamate dehydrogenases
    • ed. Boyer, P. D., Academic Press, New York
    • Frieden, C., Glutamate dehydrogenases. In "The Enzymes" 2nd ed. Vol. 7, ed. Boyer, P. D., Academic Press, New York, pp. 3-24 (1963).
    • (1963) "The Enzymes" 2nd Ed. , vol.7 , pp. 3-24
    • Frieden, C.1
  • 2
    • 0003450992 scopus 로고
    • Nomenclature committee of the IUB, Academic Press, New York
    • "Enzyme Nomenclature", Nomenclature committee of the IUB, Academic Press, New York (1992).
    • (1992) Enzyme Nomenclature
  • 3
    • 0027333040 scopus 로고
    • L-Glutamate dehydrogenases: Distribution, properties and mechanism
    • Hudson, R. C., and Daniel, R. M., L-Glutamate dehydrogenases: distribution, properties and mechanism. Comp. Biochem. Physiol., 106B, 767-792 (1993).
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 767-792
    • Hudson, R.C.1    Daniel, R.M.2
  • 4
    • 0025617067 scopus 로고
    • Biochemistry and biotechnology of amino acid dehydrogenases
    • Ohshima, T., and Soda, K., Biochemistry and biotechnology of amino acid dehydrogenases. Adv. Biochem. Eng. Biotechnol., 42, 187-189 (1990).
    • (1990) Adv. Biochem. Eng. Biotechnol. , vol.42 , pp. 187-189
    • Ohshima, T.1    Soda, K.2
  • 5
    • 0345817539 scopus 로고
    • Regeneration of nicotinamide cofactors for use in organic synthesis
    • Chenault, H. K., and Whitesides, G. M., Regeneration of nicotinamide cofactors for use in organic synthesis. Appl. Biochem. Biotechnol., 14, 147-197 (1987).
    • (1987) Appl. Biochem. Biotechnol. , vol.14 , pp. 147-197
    • Chenault, H.K.1    Whitesides, G.M.2
  • 6
    • 0032876690 scopus 로고    scopus 로고
    • The NAD-dependent glutamate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum: Cloning, sequencing, and expression of the enzyme gene
    • Kujo, C., Sakuraba, H., Nunoura, N., and Ohshima, T., The NAD-dependent glutamate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum: cloning, sequencing, and expression of the enzyme gene. Biochim. Biophys. Acta, 12, 365-371 (1999).
    • (1999) Biochim. Biophys. Acta , vol.12 , pp. 365-371
    • Kujo, C.1    Sakuraba, H.2    Nunoura, N.3    Ohshima, T.4
  • 8
    • 0029824741 scopus 로고    scopus 로고
    • Sequence analysis of the Bacillus subtilis chromosome region between the sera and kdg loci cloned in a yeast artificial chromosome
    • Sorokon, A., Azevedo, V., Zumstein, E., Galleron, N., Ehrlich, D., and Serror, P., Sequence analysis of the Bacillus subtilis chromosome region between the sera and kdg loci cloned in a yeast artificial chromosome. Microbiol., 142, 2005-2016 (1996).
    • (1996) Microbiol. , vol.142 , pp. 2005-2016
    • Sorokon, A.1    Azevedo, V.2    Zumstein, E.3    Galleron, N.4    Ehrlich, D.5    Serror, P.6
  • 9
    • 0026544783 scopus 로고
    • The glutamate dehydrogenase gene of Clostridium symbiosum: Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli
    • Teller, J. K., Smith, R. J., Mcpherson, M. J., Engel, P. C., and Guest, J. R., The glutamate dehydrogenase gene of Clostridium symbiosum: cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli. Eur. J. Biochem., 206, 151-159 (1992).
    • (1992) Eur. J. Biochem. , vol.206 , pp. 151-159
    • Teller, J.K.1    Smith, R.J.2    Mcpherson, M.J.3    Engel, P.C.4    Guest, J.R.5
  • 10
    • 0026063321 scopus 로고
    • Identification of the latex test-reactive protein of Clostridium difficile as glutamate dehydrogenase
    • Lyerly, D. M., Barroso, L. A., and Wilkins, T. D., Identification of the latex test-reactive protein of Clostridium difficile as glutamate dehydrogenase. J. Clin. Microbiol., 29, 2639-2642 (1991).
    • (1991) J. Clin. Microbiol. , vol.29 , pp. 2639-2642
    • Lyerly, D.M.1    Barroso, L.A.2    Wilkins, T.D.3
  • 11
    • 0027440899 scopus 로고
    • The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: Sequence, transcription and analysis of the deduced amino acid sequence
    • Eggen, R. I. L., Geerling, A. C. M., Waldkötter, K., Antranikian, G., and de Vos, W. M., The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence. Gene, 132, 143-148 (1991).
    • (1991) Gene , vol.132 , pp. 143-148
    • Eggen, R.I.L.1    Geerling, A.C.M.2    Waldkötter, K.3    Antranikian, G.4    De Vos, W.M.5
  • 12
    • 0030998944 scopus 로고    scopus 로고
    • Molecular cloning, nucleotide sequence and expression in Escherichia coli of hyperthermophilic glutamate dehydrogenase gene from Thermococcus profundus
    • Higuchi, S., Kobayashi, T., Kimura, K., Horikoshi, K., and Kudo, T., Molecular cloning, nucleotide sequence and expression in Escherichia coli of hyperthermophilic glutamate dehydrogenase gene from Thermococcus profundus. J. Ferment. Bioeng., 83, 405-411 (1997).
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 405-411
    • Higuchi, S.1    Kobayashi, T.2    Kimura, K.3    Horikoshi, K.4    Kudo, T.5
  • 13
    • 0031756184 scopus 로고    scopus 로고
    • Role and regulation of Bacillus subtilis glutamate dehydrogenase genes
    • Belitsky, B. R., and Abraham, L. S., Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J. Bacteriol., 180, 6298-6305 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 6298-6305
    • Belitsky, B.R.1    Abraham, L.S.2
  • 14
    • 2442669092 scopus 로고    scopus 로고
    • CcpA-dependent regulation of Bacillus subtilis glutamate dehydrogenase gene expression
    • Belitsky, B. R., Kim, H. J., and Abraham, L. S., CcpA-dependent regulation of Bacillus subtilis glutamate dehydrogenase gene expression. J. Bacteriol., 186, 3392-3398 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 3392-3398
    • Belitsky, B.R.1    Kim, H.J.2    Abraham, L.S.3
  • 15
    • 2442649038 scopus 로고    scopus 로고
    • Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase
    • Belitsky, B. R., and Abraham, L. S., Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase. J. Bacteriol., 186, 3399-3407 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 3399-3407
    • Belitsky, B.R.1    Abraham, L.S.2
  • 16
    • 0033621091 scopus 로고    scopus 로고
    • An enhancer element located downstream of the major glutamate dehydrogenase gene of Bacillus subtilis
    • Belitsky, B. R., and Abraham, L. S., An enhancer element located downstream of the major glutamate dehydrogenase gene of Bacillus subtilis. Proc. Natl. Acad. Sci., 96, 10290-10295 (1999).
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 10290-10295
    • Belitsky, B.R.1    Abraham, L.S.2
  • 17
    • 0020393389 scopus 로고
    • A new approach for molecular cloning in cyanobacteria: Cloning of an Anacystis nidulans met gene using a Tn901-induced mutant
    • Tandeau, M. N., Borrias, W. E., Kuhlemeier, C. J., Castets, A. M., van Arkel, G. A., and van den Hondel, C. A., A new approach for molecular cloning in cyanobacteria: cloning of an Anacystis nidulans met gene using a Tn901-induced mutant. Gene, 20, 111-119 (1982).
    • (1982) Gene , vol.20 , pp. 111-119
    • Tandeau, M.N.1    Borrias, W.E.2    Kuhlemeier, C.J.3    Castets, A.M.4    Van Arkel, G.A.5    Van Den Hondel, C.A.6
  • 19
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Lenug, D. W., Che, E., and Goeddel, D. V., A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique JMCMB, 1, 11-15 (1989).
    • (1989) Technique JMCMB , vol.1 , pp. 11-15
    • Lenug, D.W.1    Che, E.2    Goeddel, D.V.3
  • 21
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P., Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem., 262, 10035-10038 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 22
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantification of microgram quantities of protein using the principle for protein-dye binding
    • Bradford, M. A., Rapid and sensitive method for the quantification of microgram quantities of protein using the principle for protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.A.1
  • 23
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T. L., Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol., 234, 779-815 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 24
    • 0034671553 scopus 로고    scopus 로고
    • A new class of glutamate dehydrogenase (GDH): Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus
    • Minambres, B., Oliver, E. R., Jensen, R. A., and Luengo, J. M., A new class of glutamate dehydrogenase (GDH): biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. J. Biol. Chem., 275, 39529-39542 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 39529-39542
    • Minambres, B.1    Oliver, E.R.2    Jensen, R.A.3    Luengo, J.M.4
  • 25
    • 0027984543 scopus 로고
    • Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum
    • Tokyo
    • Sawa, Y., Tani, M., Murata, K., Shibata, H., and Ochiai, H., Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum. J. Biochem. (Tokyo), 116, 995-1000 (1994).
    • (1994) J. Biochem. , vol.116 , pp. 995-1000
    • Sawa, Y.1    Tani, M.2    Murata, K.3    Shibata, H.4    Ochiai, H.5
  • 26
    • 0033556161 scopus 로고    scopus 로고
    • Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum
    • Stillman, T. J., Migueis, A. M. B., Wang, X., Baker, P. J., Britton, K. L., Engel, P. C., and Rice, D. W., Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum. J. Mol. Biol., 285, 875-885 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 875-885
    • Stillman, T.J.1    Migueis, A.M.B.2    Wang, X.3    Baker, P.J.4    Britton, K.L.5    Engel, P.C.6    Rice, D.W.7
  • 28
    • 0032528267 scopus 로고    scopus 로고
    • Insights into the molecular basis of thermal stability from the analysis of ion-pair networks in the glutamate dehydrogenase family
    • Yip, K. S., Britton, K. L., Stillman, T. J., Lebbink, J., de Vos, W. M., Robb, F. T., Vetriani, C., Maeder, D. L., and Rice, D. W., Insights into the molecular basis of thermal stability from the analysis of ion-pair networks in the glutamate dehydrogenase family. Eur. J. Biochem., 255, 336-346 (1998).
    • (1998) Eur. J. Biochem. , vol.255 , pp. 336-346
    • Yip, K.S.1    Britton, K.L.2    Stillman, T.J.3    Lebbink, J.4    De Vos, W.M.5    Robb, F.T.6    Vetriani, C.7    Maeder, D.L.8    Rice, D.W.9
  • 29
    • 0032504088 scopus 로고    scopus 로고
    • Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II. Construction of a 16-residue ion-pair network at the subunit interface
    • Lebbink, J. H., Knapp, S., Van der Oost, J., Rice, D. W., Ladenstein, R., and de Vos, W. M., Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II. Construction of a 16-residue ion-pair network at the subunit interface. J. Mol. Biol., 280, 287-296 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 287-296
    • Lebbink, J.H.1    Knapp, S.2    Van Der Oost, J.3    Rice, D.W.4    Ladenstein, R.5    De Vos, W.M.6
  • 30
    • 0027120931 scopus 로고
    • Occurrence of cold labile NAD-specific glutamate dehydrogenase in Bacillus species
    • Jahns, T., Occurrence of cold labile NAD-specific glutamate dehydrogenase in Bacillus species. FEMS Microbiol. Lett., 96, 187-192 (1992).
    • (1992) FEMS Microbiol. Lett. , vol.96 , pp. 187-192
    • Jahns, T.1
  • 31
    • 0027278092 scopus 로고
    • +-specific glutamate dehydrogenase from Bacillus cereus DSM 31
    • +-specific glutamate dehydrogenase from Bacillus cereus DSM 31. J. G. Microbiol., 139, 775-780 (1993).
    • (1993) J. G. Microbiol. , vol.139 , pp. 775-780
    • Jahns, T.1    Kaltwasser, H.2
  • 32
    • 0029550717 scopus 로고
    • Refolding of glutamate dehydrogenase from Bacillus acidocaldarius after guanidinium chloride-induced unfolding
    • Consalvi, V., Millevoi, S., Chiaraluce, R., Rosa, M., and Scandurra, R., Refolding of glutamate dehydrogenase from Bacillus acidocaldarius after guanidinium chloride-induced unfolding. Biochem. Mol. Biol. Intl., 35, 397-407 (1995).
    • (1995) Biochem. Mol. Biol. Intl. , vol.35 , pp. 397-407
    • Consalvi, V.1    Millevoi, S.2    Chiaraluce, R.3    Rosa, M.4    Scandurra, R.5
  • 33
    • 0023992328 scopus 로고
    • The unfolding and refolding of glutamate dehydrogenases from bovine liver, baker's yeast and Clostridium symbiosum
    • West, S. M., and Price, N. C., The unfolding and refolding of glutamate dehydrogenases from bovine liver, baker's yeast and Clostridium symbiosum. Biochem. J., 251, 135-139 (1988).
    • (1988) Biochem. J. , vol.251 , pp. 135-139
    • West, S.M.1    Price, N.C.2
  • 34
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan, M. K., Mukund, S., Kietzin, A., Adams, M. W., and Rees, D. C., Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science, 267, 1463-1469 (1995).
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kietzin, A.3    Adams, M.W.4    Rees, D.C.5
  • 35
    • 0029644328 scopus 로고
    • Hyperthermophiles: Taking the heat and loving it
    • Rees, D. C., and Adams, M. W. W., Hyperthermophiles: taking the heat and loving it. Structure, 3, 251-254 (1995).
    • (1995) Structure , vol.3 , pp. 251-254
    • Rees, D.C.1    Adams, M.W.W.2
  • 37
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • Yip, K. S., Stillman, T. J., Britton, K. L., Artymiuk, P. J., Baker, P. J., Sedelnikova, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R., and Consalvi, V., The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure, 3, 1147-1158 (1995).
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.1    Stillman, T.J.2    Britton, K.L.3    Artymiuk, P.J.4    Baker, P.J.5    Sedelnikova, S.E.6    Engel, P.C.7    Pasquo, A.8    Chiaraluce, R.9    Consalvi, V.10
  • 38
    • 9644294199 scopus 로고    scopus 로고
    • The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum
    • Bhuiya, M. W., Sakuraba, H., Ohshima, T., Imagawa, T., Katunuma, N., and Tsuge, H., The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. J. Mol. Biol., 345, 325-337 (2005).
    • (2005) J. Mol. Biol. , vol.345 , pp. 325-337
    • Bhuiya, M.W.1    Sakuraba, H.2    Ohshima, T.3    Imagawa, T.4    Katunuma, N.5    Tsuge, H.6
  • 39
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumaer, S., Chung-Jung, T., and Ruth, N., Factors enhancing protein thermostability. Protein Eng., 13, 179-191 (2000).
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumaer, S.1    Chung-Jung, T.2    Ruth, N.3
  • 41
    • 0031564613 scopus 로고    scopus 로고
    • Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution
    • Knapp, S., de Vos, W. M., Rice, D. W., and Ladenstein, R., Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution. J. Mol. Biol., 267, 916-932 (1997).
    • (1997) J. Mol. Biol. , vol.267 , pp. 916-932
    • Knapp, S.1    De Vos, W.M.2    Rice, D.W.3    Ladenstein, R.4
  • 42
    • 0027769953 scopus 로고
    • Conformational flexibility in glutamate dehydrogenase: Role of water in substrate recognition and catalysis
    • Stillman, T. J., Baker, P. J., Britton, K. L., and Rice, D. W., Conformational flexibility in glutamate dehydrogenase: Role of water in substrate recognition and catalysis. J. Mol. Biol., 234, 1131-1139 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 1131-1139
    • Stillman, T.J.1    Baker, P.J.2    Britton, K.L.3    Rice, D.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.