메뉴 건너뛰기




Volumn 89, Issue 3, 2011, Pages 673-684

Salt-dependent thermo-reversible α-amylase: Cloning and characterization of halophilic α-amylase from moderately halophilic bacterium, Kocuria varians

Author keywords

Amylase; Amylase inhibitor; Acidic protein; Halophilic; Moderate halophile; Reversibility

Indexed keywords

ACIDIC AMINO ACIDS; ACIDIC PROTEINS; CATALYTIC DOMAINS; CULTURE MEDIUM; FUSION PARTNERS; FUSION PROTEINS; HALOPHILIC; HALOPHILIC BACTERIA; MODERATE HALOPHILE; NEGATIVE ELECTROSTATIC POTENTIAL; RAW STARCH; REVERSIBILITY; STARCH BINDING DOMAIN; TANDEM REPEATS; THERMAL REVERSIBILITY; TIME-DEPENDENT;

EID: 79251597820     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2882-y     Document Type: Article
Times cited : (42)

References (44)
  • 1
    • 0031910806 scopus 로고    scopus 로고
    • Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
    • 1:CAS:528:DyaK1cXhvV2lurk%3D 10.1002/pro.5560070304
    • N Aghajari G Feller C Gerday R Haser 1998 Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor Protein Sci 7 564 572 1:CAS:528: DyaK1cXhvV2lurk%3D 10.1002/pro.5560070304
    • (1998) Protein Sci , vol.7 , pp. 564-572
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 2
    • 1942521068 scopus 로고    scopus 로고
    • Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins
    • 1:CAS:528:DC%2BD2cXjtlaltbo%3D 10.2174/0929866043478220
    • T Arakawa M Tokunaga 2004 Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins Protein Pept Lett 11 125 132 1:CAS:528:DC%2BD2cXjtlaltbo%3D 10.2174/0929866043478220
    • (2004) Protein Pept Lett , vol.11 , pp. 125-132
    • Arakawa, T.1    Tokunaga, M.2
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modeling
    • 1:CAS:528:DC%2BD28XovVCltw%3D%3D 10.1093/bioinformatics/bti770
    • K Arnold L Bordoli J Kopp T Schwede 2006 The SWISS-MODEL Workspace: a web-based environment for protein structure homology modeling Bioinformatics 22 195 201 1:CAS:528:DC%2BD28XovVCltw%3D%3D 10.1093/bioinformatics/bti770
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 0034128816 scopus 로고    scopus 로고
    • The alpha-amylase gene amyH of the moderate halophile Halomonas meridiana: Cloning and molecular characterization
    • 1:CAS:528:DC%2BD3cXislOjsL4%3D
    • M-J Coronado C Vargas E Mellado G Tegos C Drainas JJ Nieto A Ventosa 2000 The alpha-amylase gene amyH of the moderate halophile Halomonas meridiana: cloning and molecular characterization Microbiology 146 861 868 1:CAS:528:DC%2BD3cXislOjsL4%3D
    • (2000) Microbiology , vol.146 , pp. 861-868
    • Coronado, M.-J.1    Vargas, C.2    Mellado, E.3    Tegos, G.4    Drainas, C.5    Nieto, J.J.6    Ventosa, A.7
  • 5
    • 0026646179 scopus 로고
    • Biochemical, structural, and molecular genetic aspects of halophilism
    • 1:CAS:528:DyaK3sXhs1Ckt7c%3D 10.1016/S0065-3233(08)60553-7
    • H Eisenberg M Mevarech G Zaccai 1992 Biochemical, structural, and molecular genetic aspects of halophilism Adv Protein Chem 43 1 62 1:CAS:528:DyaK3sXhs1Ckt7c%3D 10.1016/S0065-3233(08)60553-7
    • (1992) Adv Protein Chem , vol.43 , pp. 1-62
    • Eisenberg, H.1    Mevarech, M.2    Zaccai, G.3
  • 6
    • 0034099450 scopus 로고    scopus 로고
    • Cloning and expression of alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in the moderately halophilic bacterium Halomonas elongata
    • 1:CAS:528:DC%2BD3cXis1ekt74%3D 10.1046/j.1365-2672.2000.00988.x
    • S Frillingos A Linden F Niehaus C Vargas JJ Nieto A Ventosa G Antranikian C Drainas 2000 Cloning and expression of alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in the moderately halophilic bacterium Halomonas elongata J Appl Microbiol 88 495 503 1:CAS:528: DC%2BD3cXis1ekt74%3D 10.1046/j.1365-2672.2000.00988.x
    • (2000) J Appl Microbiol , vol.88 , pp. 495-503
    • Frillingos, S.1    Linden, A.2    Niehaus, F.3    Vargas, C.4    Nieto, J.J.5    Ventosa, A.6    Antranikian, G.7    Drainas, C.8
  • 7
    • 14644442998 scopus 로고    scopus 로고
    • Organic solvent tolerance of halophilic alpha-amylase from a Haloarchaeon, Haloarcula sp. strain S-1
    • 1:CAS:528:DC%2BD2MXhtF2gs7g%3D 10.1007/s00792-004-0423-2
    • T Fukushima T Mizuki A Echigo A Inoue R Usami 2005 Organic solvent tolerance of halophilic alpha-amylase from a Haloarchaeon, Haloarcula sp. strain S-1 Extremophiles 9 85 89 1:CAS:528:DC%2BD2MXhtF2gs7g%3D 10.1007/s00792-004- 0423-2
    • (2005) Extremophiles , vol.9 , pp. 85-89
    • Fukushima, T.1    Mizuki, T.2    Echigo, A.3    Inoue, A.4    Usami, R.5
  • 8
    • 0028783450 scopus 로고
    • Osmoadaptation in bacteria
    • 1:STN:280:DyaK287is1WgtA%3D%3D
    • EA Galinski 1995 Osmoadaptation in bacteria Adv Microb Physiol 37 272 328 1:STN:280:DyaK287is1WgtA%3D%3D
    • (1995) Adv Microb Physiol , vol.37 , pp. 272-328
    • Galinski, E.A.1
  • 9
    • 29244438994 scopus 로고    scopus 로고
    • Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica
    • 1:CAS:528:DC%2BD2MXhtlClu7jL 10.1007/s00792-005-0471-2
    • GW Hutcheon N Vasisht A Bolhuis 2005 Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica Extremophiles 9 487 495 1:CAS:528:DC%2BD2MXhtlClu7jL 10.1007/s00792-005-0471-2
    • (2005) Extremophiles , vol.9 , pp. 487-495
    • Hutcheon, G.W.1    Vasisht, N.2    Bolhuis, A.3
  • 10
    • 0035953042 scopus 로고    scopus 로고
    • Identification of the protein product of the Coch gene (hereditary deafness gene) as the major component of bovine inner ear protein
    • 1:CAS:528:DC%2BD3MXitF2qsrk%3D
    • T Ikezono A Omori S Ichinose R Pawankar A Watanabe T Yagi 2001 Identification of the protein product of the Coch gene (hereditary deafness gene) as the major component of bovine inner ear protein Biochim Biophys Acta 1535 258 265 1:CAS:528:DC%2BD3MXitF2qsrk%3D
    • (2001) Biochim Biophys Acta , vol.1535 , pp. 258-265
    • Ikezono, T.1    Omori, A.2    Ichinose, S.3    Pawankar, R.4    Watanabe, A.5    Yagi, T.6
  • 11
    • 0042885986 scopus 로고    scopus 로고
    • Activation of halophilic nucleoside diphosphate kinase by a non-ionic osmolyte, trimethylamine N-oxide
    • 1:CAS:528:DC%2BD3sXmsFejsrc%3D 10.1023/A:1025338106922
    • M Ishibashi K Sakashita H Tokunaga T Arakawa M Tokunaga 2003 Activation of halophilic nucleoside diphosphate kinase by a non-ionic osmolyte, trimethylamine N-oxide J Protein Chem 22 345 351 1:CAS:528:DC%2BD3sXmsFejsrc%3D 10.1023/A:1025338106922
    • (2003) J Protein Chem , vol.22 , pp. 345-351
    • Ishibashi, M.1    Sakashita, K.2    Tokunaga, H.3    Arakawa, T.4    Tokunaga, M.5
  • 12
    • 0017889038 scopus 로고
    • Flocculation and adsorption of enzymes during growth of a moderate halophile, Micrococcus varians var. halophilus
    • 1:CAS:528:DyaE1cXksFKgtLc%3D 10.1139/m78-118
    • M Kamekura H Onishi 1978 Flocculation and adsorption of enzymes during growth of a moderate halophile, Micrococcus varians var. halophilus Can J Microbiol 24 703 709 1:CAS:528:DyaE1cXksFKgtLc%3D 10.1139/m78-118
    • (1978) Can J Microbiol , vol.24 , pp. 703-709
    • Kamekura, M.1    Onishi, H.2
  • 13
    • 0026951651 scopus 로고
    • Purification and some properties of a Haim-sensitive α-amylase from newly isolated Bacillus sp. No. 195
    • 1:CAS:528:DyaK3sXjsV2isQ%3D%3D 10.1271/bbb.56.1792
    • T Kawaguchi H Nagae S Murao M Arai 1992 Purification and some properties of a Haim-sensitive α-amylase from newly isolated Bacillus sp. No. 195 Biosci Biotechnol Biochem 56 1792 1796 1:CAS:528:DyaK3sXjsV2isQ%3D%3D 10.1271/bbb.56.1792
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1792-1796
    • Kawaguchi, T.1    Nagae, H.2    Murao, S.3    Arai, M.4
  • 14
    • 37449020231 scopus 로고    scopus 로고
    • Production of surfactant and detergent-stable, halophilic, and alkalitolerant alpha-amylase by a moderately halophilic Bacillus sp. Strain TSCVKK
    • 1:CAS:528:DC%2BD2sXhsVaisrbN 10.1007/s00253-007-1250-z
    • KK Kiran TS Chandra 2008 Production of surfactant and detergent-stable, halophilic, and alkalitolerant alpha-amylase by a moderately halophilic Bacillus sp. Strain TSCVKK Appl Microbiol Biotechnol 77 1023 1031 1:CAS:528: DC%2BD2sXhsVaisrbN 10.1007/s00253-007-1250-z
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 1023-1031
    • Kiran, K.K.1    Chandra, T.S.2
  • 15
    • 0022650238 scopus 로고
    • Production, purification, and characterization of an amylase from the moderate halophile, Micrococcus varians subspecies halophilus
    • 1:CAS:528:DyaL28XlsVylsrY%3D
    • T Kobayashi M Kamekura W Kanlayakrit H Onishi 1986 Production, purification, and characterization of an amylase from the moderate halophile, Micrococcus varians subspecies halophilus Microbios 46 165 177 1:CAS:528:DyaL28XlsVylsrY%3D
    • (1986) Microbios , vol.46 , pp. 165-177
    • Kobayashi, T.1    Kamekura, M.2    Kanlayakrit, W.3    Onishi, H.4
  • 16
    • 0002415242 scopus 로고
    • The halobacteriaceae
    • 1:CAS:528:DyaL2MXltlyis7Y%3D
    • DJ Kushner 1985 The halobacteriaceae Bacteria 8 171 214 1:CAS:528:DyaL2MXltlyis7Y%3D
    • (1985) Bacteria , vol.8 , pp. 171-214
    • Kushner, D.J.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 1:CAS:528:DC%2BD3MXlsFags7s%3D 10.1038/227680a0
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685 1:CAS:528:DC%2BD3MXlsFags7s%3D 10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • OH Lowry NJ Rosebrough AL Farr RJ Randall 1951 Protein measurement with the folin phenol reagent J Biol Chem 193 265 275 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 19
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • 1:CAS:528:DC%2BD3cXjt1Clu7o%3D 10.1007/s007920050142
    • D Madern C Ebel G Zaccai 2000 Halophilic adaptation of enzymes Extremophiles 4 91 98 1:CAS:528:DC%2BD3cXjt1Clu7o%3D 10.1007/s007920050142
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 20
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • 1:CAS:528:DC%2BD3cXlvV2ksbY%3D 10.1016/S0301-4622(00)00126-5
    • M Mevarech F Frolow LM Gloss 2000 Halophilic enzymes: proteins with a grain of salt Biophys Chem 86 155 164 1:CAS:528:DC%2BD3cXlvV2ksbY%3D 10.1016/S0301-4622(00)00126-5
    • (2000) Biophys Chem , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 21
    • 0036667421 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of an alpha-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme
    • 1:CAS:528:DC%2BD38XmslSqs7c%3D
    • BN Mijts BK Patel 2002 Cloning, sequencing and expression of an alpha-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme Microbiology 148 2343 2349 1:CAS:528:DC%2BD38XmslSqs7c%3D
    • (2002) Microbiology , vol.148 , pp. 2343-2349
    • Mijts, B.N.1    Patel, B.K.2
  • 22
    • 23944462637 scopus 로고    scopus 로고
    • How to be moderately halophilic with broad salt tolerance: Clues from the genome of Chromohalobacter salexigens
    • 1:CAS:528:DC%2BD2MXntVehsL8%3D 10.1007/s00792-005-0442-7
    • A Oren F Larimer P Richardson A Lapidus LN Csonka 2005 How to be moderately halophilic with broad salt tolerance: clues from the genome of Chromohalobacter salexigens Extremophiles 9 275 279 1:CAS:528: DC%2BD2MXntVehsL8%3D 10.1007/s00792-005-0442-7
    • (2005) Extremophiles , vol.9 , pp. 275-279
    • Oren, A.1    Larimer, F.2    Richardson, P.3    Lapidus, A.4    Csonka, L.N.5
  • 24
    • 0019877658 scopus 로고
    • Structure stability of halophilic proteins
    • 1:CAS:528:DyaL3MXlvF2htLo%3D 10.1021/bi00526a004
    • JKM Rao P Argos 1981 Structure stability of halophilic proteins Biochemistry 20 6536 6543 1:CAS:528:DyaL3MXlvF2htLo%3D 10.1021/bi00526a004
    • (1981) Biochemistry , vol.20 , pp. 6536-6543
    • Rao, J.K.M.1    Argos, P.2
  • 25
    • 61349198759 scopus 로고    scopus 로고
    • Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran
    • 1:CAS:528:DC%2BD1MXitlWrsbc%3D 10.1007/s10295-008-0500-0
    • R Rohban MA Amoozegar A Ventosa 2009 Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran J Ind Microbiol Biotechnol 36 333 340 1:CAS:528:DC%2BD1MXitlWrsbc%3D 10.1007/s10295-008-0500-0
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 333-340
    • Rohban, R.1    Amoozegar, M.A.2    Ventosa, A.3
  • 26
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • 1:CAS:528:DyaF3sXks1emtro%3D 10.1016/0926-6550(63)90386-4
    • H Saito K Miura 1963 Preparation of transforming deoxyribonucleic acid by phenol treatment Biochim Biophys Acta 72 619 629 1:CAS:528:DyaF3sXks1emtro%3D 10.1016/0926-6550(63)90386-4
    • (1963) Biochim Biophys Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 27
    • 33646205656 scopus 로고    scopus 로고
    • Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition
    • 1:CAS:528:DC%2BD28XksFaqsr0%3D 10.1016/j.febslet.2006.04.017
    • N Sivakumar N Li JW Tang BK Patel K Swaminathan 2006 Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition FEBS Lett 580 2646 2652 1:CAS:528:DC%2BD28XksFaqsr0%3D 10.1016/j.febslet.2006.04.017
    • (2006) FEBS Lett , vol.580 , pp. 2646-2652
    • Sivakumar, N.1    Li, N.2    Tang, J.W.3    Patel, B.K.4    Swaminathan, K.5
  • 29
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • 1:CAS:528:DyaG38XivFegsw%3D%3D
    • M Somogyi 1952 Notes on sugar determination J Biol Chem 195 19 23 1:CAS:528:DyaG38XivFegsw%3D%3D
    • (1952) J Biol Chem , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 30
    • 34248392177 scopus 로고    scopus 로고
    • Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis
    • 1:CAS:528:DC%2BD2sXltVGqtrc%3D 10.1007/s00792-007-0062-5
    • S Srimathi G Jayaraman G Feller B Danielsson PR Narayanan 2007 Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis Extremophiles 11 505 515 1:CAS:528:DC%2BD2sXltVGqtrc%3D 10.1007/s00792-007-0062-5
    • (2007) Extremophiles , vol.11 , pp. 505-515
    • Srimathi, S.1    Jayaraman, G.2    Feller, G.3    Danielsson, B.4    Narayanan, P.R.5
  • 31
    • 0027652134 scopus 로고
    • Molecular cloning and expression of proteinaceous α-amylase inhibitor gene from Streptomyces nitrosporeus in Escherichia coli
    • 1:CAS:528:DyaK2cXhs1Oi 10.1271/bbb.57.1243
    • J Sumitani T Kawaguchi N Hattori S Murao M Arai 1993 Molecular cloning and expression of proteinaceous α-amylase inhibitor gene from Streptomyces nitrosporeus in Escherichia coli Biosci Biotechnol Biochem 57 1243 1248 1:CAS:528:DyaK2cXhs1Oi 10.1271/bbb.57.1243
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 1243-1248
    • Sumitani, J.1    Kawaguchi, T.2    Hattori, N.3    Murao, S.4    Arai, M.5
  • 32
    • 0034283404 scopus 로고    scopus 로고
    • New type of starch-binding domain: The direct repeat motif in the C-terminal region of Bacillus sp. no 195 α-amylase contributes to starch binding and raw starch degrading
    • 1:CAS:528:DC%2BD2cXlt1Shu70%3D 10.1042/0264-6021:3500477
    • J Sumitani T Tottori T Kawaguchi M Arai 2000 New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no 195 α-amylase contributes to starch binding and raw starch degrading Biochem J 350 477 484 1:CAS:528:DC%2BD2cXlt1Shu70%3D 10.1042/0264-6021:3500477
    • (2000) Biochem J , vol.350 , pp. 477-484
    • Sumitani, J.1    Tottori, T.2    Kawaguchi, T.3    Arai, M.4
  • 33
    • 0034253246 scopus 로고    scopus 로고
    • Cloning and secretive expression of the gene encoding the proteinaceous α-amylase inhibitor Paim from Streptomyces corchorusii
    • 1:CAS:528:DC%2BD3cXntlyjtbc%3D
    • J Sumitani Y Tsujimoto T Kawaguchi M Arai 2000 Cloning and secretive expression of the gene encoding the proteinaceous α-amylase inhibitor Paim from Streptomyces corchorusii J Biosci Bioeng 90 214 216 1:CAS:528: DC%2BD3cXntlyjtbc%3D
    • (2000) J Biosci Bioeng , vol.90 , pp. 214-216
    • Sumitani, J.1    Tsujimoto, Y.2    Kawaguchi, T.3    Arai, M.4
  • 34
    • 0842303216 scopus 로고    scopus 로고
    • Highly efficient renaturation of beta-lactamase isolated from moderately halophilic bacteria
    • 1:CAS:528:DC%2BD2cXpsV2htg%3D%3D 10.1016/S0014-5793(03)01508-4
    • H Tokunaga M Ishibashi T Arakawa M Tokunaga 2004 Highly efficient renaturation of beta-lactamase isolated from moderately halophilic bacteria FEBS Lett 558 7 12 1:CAS:528:DC%2BD2cXpsV2htg%3D%3D 10.1016/S0014-5793(03)01508-4
    • (2004) FEBS Lett , vol.558 , pp. 7-12
    • Tokunaga, H.1    Ishibashi, M.2    Arakawa, T.3    Tokunaga, M.4
  • 35
    • 32044446927 scopus 로고    scopus 로고
    • Opposing effects of NaCl on reversibility and thermal stability of halophilic beta-lactamase from a moderate halophile, Chromohalobacter sp. 560
    • 1:CAS:528:DC%2BD28Xhtlehtrg%3D 10.1016/j.bpc.2005.10.006
    • H Tokunaga T Arakawa H Fukada M Tokunaga 2006 Opposing effects of NaCl on reversibility and thermal stability of halophilic beta-lactamase from a moderate halophile, Chromohalobacter sp. 560 Biophys Chem 119 316 320 1:CAS:528:DC%2BD28Xhtlehtrg%3D 10.1016/j.bpc.2005.10.006
    • (2006) Biophys Chem , vol.119 , pp. 316-320
    • Tokunaga, H.1    Arakawa, T.2    Fukada, H.3    Tokunaga, M.4
  • 36
    • 33646394637 scopus 로고    scopus 로고
    • Contribution of halophilic nucleoside diphosphate kinase sequence to the heat stability of chimeric molecule
    • 1:CAS:528:DC%2BD28XlsVGqsL8%3D 10.2174/092986606776819628
    • H Tokunaga Y Oda Y Yonezawa T Arakawa M Tokunaga 2006 Contribution of halophilic nucleoside diphosphate kinase sequence to the heat stability of chimeric molecule Protein Pept Lett 13 525 530 1:CAS:528:DC%2BD28XlsVGqsL8%3D 10.2174/092986606776819628
    • (2006) Protein Pept Lett , vol.13 , pp. 525-530
    • Tokunaga, H.1    Oda, Y.2    Yonezawa, Y.3    Arakawa, T.4    Tokunaga, M.5
  • 37
    • 50049123899 scopus 로고    scopus 로고
    • Engineering of halophilic enzymes: Two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases
    • 1:CAS:528:DC%2BD1cXhtV2rsbzN 10.1110/ps.035725.108
    • H Tokunaga T Arakawa M Tokunaga 2008 Engineering of halophilic enzymes: two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases Protein Sci 17 1603 1610 1:CAS:528:DC%2BD1cXhtV2rsbzN 10.1110/ps.035725.108
    • (2008) Protein Sci , vol.17 , pp. 1603-1610
    • Tokunaga, H.1    Arakawa, T.2    Tokunaga, M.3
  • 38
    • 40849123928 scopus 로고    scopus 로고
    • Residue 134 determines the dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacteria
    • 1:CAS:528:DC%2BD1cXjs1Khsb0%3D 10.1016/j.febslet.2008.02.054
    • H Tokunaga M Ishibashi F Arisaka S Arai R Kuroki T Arakawa M Tokunaga 2008 Residue 134 determines the dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacteria FEBS Lett 582 1049 1054 1:CAS:528:DC%2BD1cXjs1Khsb0%3D 10.1016/j.febslet.2008.02.054
    • (2008) FEBS Lett , vol.582 , pp. 1049-1054
    • Tokunaga, H.1    Ishibashi, M.2    Arisaka, F.3    Arai, S.4    Kuroki, R.5    Arakawa, T.6    Tokunaga, M.7
  • 39
    • 71249137609 scopus 로고    scopus 로고
    • Dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacterium Chromohalobacter salexigens DSM3043:Both residues 134 and 136 are critical for the tetramer assembly
    • 1:CAS:528:DC%2BD1MXhsFGgs73N 10.1016/j.enzmictec.2009.10.009
    • H Tokunaga K Izutsu S Arai Y Yonezawa R Kuroki T Arakawa M Tokunaga 2010 Dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacterium Chromohalobacter salexigens DSM3043:Both residues 134 and 136 are critical for the tetramer assembly Enzyme Microb Technol 46 129 135 1:CAS:528:DC%2BD1MXhsFGgs73N 10.1016/j.enzmictec.2009.10.009
    • (2010) Enzyme Microb Technol , vol.46 , pp. 129-135
    • Tokunaga, H.1    Izutsu, K.2    Arai, S.3    Yonezawa, Y.4    Kuroki, R.5    Arakawa, T.6    Tokunaga, M.7
  • 40
    • 77249093485 scopus 로고    scopus 로고
    • Halophilic β-lactamase as a new solubility- and folding-enhancing tag protein: Production of native human interleukin 1α and human neutrophil α-defensin
    • 1:CAS:528:DC%2BC3cXit1amtr0%3D 10.1007/s00253-009-2325-9
    • H Tokunaga S Saito K Sakai R Yamaguchi I Katsuyama T Arakawa K Onozaki T Arakawa M Tokunaga 2010 Halophilic β-lactamase as a new solubility- and folding-enhancing tag protein: production of native human interleukin 1α and human neutrophil α-defensin Appl Microbiol Biotechnol 86 649 658 1:CAS:528:DC%2BC3cXit1amtr0%3D 10.1007/s00253-009-2325-9
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 649-658
    • Tokunaga, H.1    Saito, S.2    Sakai, K.3    Yamaguchi, R.4    Katsuyama, I.5    Arakawa, T.6    Onozaki, K.7    Arakawa, T.8    Tokunaga, M.9
  • 41
    • 0031810562 scopus 로고    scopus 로고
    • Biology of moderately halophilic aerobic bacteria
    • 1:CAS:528:DyaK1cXkt1Oitb0%3D
    • A Ventosa JJ Nieto A Oren 1998 Biology of moderately halophilic aerobic bacteria Microbiol Mol Biol Rev 62 504 544 1:CAS:528:DyaK1cXkt1Oitb0%3D
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 504-544
    • Ventosa, A.1    Nieto, J.J.2    Oren, A.3
  • 42
    • 0025953577 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • 1:CAS:528:DyaK38Xjt1an
    • DL Wilkinson RG Harrison 1991 Predicting the solubility of recombinant proteins in Escherichia coli Bio Technol 9 443 448 1:CAS:528:DyaK38Xjt1an
    • (1991) Bio Technol , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 43
    • 0032540918 scopus 로고    scopus 로고
    • AmlC, Another amylolytic gene maps close to the amlB locus in Streptomyces lividans TK24
    • 1:CAS:528:DyaK1cXltlKlt7Y%3D 10.1016/S0378-1119(98)00265-0
    • XH Yin C Gerbaud FX Francou VMJ GuerineauM 1998 amlC, Another amylolytic gene maps close to the amlB locus in Streptomyces lividans TK24 Gene 215 171 180 1:CAS:528:DyaK1cXltlKlt7Y%3D 10.1016/S0378-1119(98)00265-0
    • (1998) Gene , vol.215 , pp. 171-180
    • Yin, X.H.1    Gerbaud, C.2    Francou, F.X.3    Guerineaum, V.M.J.4
  • 44
    • 33846652454 scopus 로고    scopus 로고
    • Dimeric structure of nucleoside diphosphate kinase from moderately halophilic bacterium: Contrast to the tetrameric Pseudomonas counterpart
    • 1:CAS:528:DC%2BD2sXitVeku7s%3D 10.1111/j.1574-6968.2007.00626.x
    • Y Yonezawa K Izutsu H Tokunaga H Maeda T Arakawa M Tokunaga 2007 Dimeric structure of nucleoside diphosphate kinase from moderately halophilic bacterium: contrast to the tetrameric Pseudomonas counterpart FEMS Microbiol Lett 268 52 58 1:CAS:528:DC%2BD2sXitVeku7s%3D 10.1111/j.1574-6968.2007.00626.x
    • (2007) FEMS Microbiol Lett , vol.268 , pp. 52-58
    • Yonezawa, Y.1    Izutsu, K.2    Tokunaga, H.3    Maeda, H.4    Arakawa, T.5    Tokunaga, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.