메뉴 건너뛰기




Volumn 11, Issue 3, 2007, Pages 505-515

Intrinsic halotolerance of the psychrophilic α-amylase from Pseudoalteromonas haloplanktis

Author keywords

Acidic protein; Halophilic; Halotolerance; Pseudoalteromonas haloplanktis amylase; Psychrophilic; Stability

Indexed keywords

AMYLASE; HALOGEN;

EID: 34248392177     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-007-0062-5     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level
    • Aghajari N, Feller G, Gerday C, Haser R (1998) Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level. Structure 6:1503-1516
    • (1998) Structure , vol.6 , pp. 1503-1516
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 2
    • 0036113602 scopus 로고    scopus 로고
    • Structural basis of α-amylase activation by chloride
    • Aghajari N, Feller G, Gerday C, Haser R (2002) Structural basis of α-amylase activation by chloride. Protein Sci 11:1435-1441
    • (2002) Protein Sci , vol.11 , pp. 1435-1441
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 3
    • 0033955301 scopus 로고    scopus 로고
    • Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana
    • Coronado M, Vargas C, Hofemeister J, Ventosa A, Nieto JJ (2000) Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana. FEMS Microbiol Lett 183:67-71
    • (2000) FEMS Microbiol Lett , vol.183 , pp. 67-71
    • Coronado, M.1    Vargas, C.2    Hofemeister, J.3    Ventosa, A.4    Nieto, J.J.5
  • 4
    • 0035854688 scopus 로고    scopus 로고
    • Structural determinants of cold adaptation and stability in a large protein
    • D'Amico S, Gerday C, Feller G (2001) Structural determinants of cold adaptation and stability in a large protein. J Biol Chem 276:25791-25796
    • (2001) J Biol Chem , vol.276 , pp. 25791-25796
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 5
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico S, Marx J-C, Gerday C, Feller G (2003) Activity-stability relationships in extremophilic enzymes. J Biol Chem 278:7891-7896
    • (2003) J Biol Chem , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.-C.2    Gerday, C.3    Feller, G.4
  • 6
    • 0031195026 scopus 로고    scopus 로고
    • The structural basis of protein halophilicity
    • Danson MJ, Hough DW (1997) The structural basis of protein halophilicity. Comp Biochem Physiol 117A:307-312
    • (1997) Comp Biochem Physiol , vol.117 A , pp. 307-312
    • Danson, M.J.1    Hough, D.W.2
  • 7
    • 0028958071 scopus 로고
    • Structural features that stabilize halophilic malate dehydrogenase from an archae-bacterium
    • Dym O, Mevarech M, Sussman JL (1994) Structural features that stabilize halophilic malate dehydrogenase from an archae-bacterium. Science 267:1344-1346
    • (1994) Science , vol.267 , pp. 1344-1346
    • Dym, O.1    Mevarech, M.2    Sussman, J.L.3
  • 8
    • 0037688133 scopus 로고    scopus 로고
    • Molecular adaptations to cold in psychrophilic enzymes
    • Feller G (2003) Molecular adaptations to cold in psychrophilic enzymes. Cell Mol Life Sci 60:648-662
    • (2003) Cell Mol Life Sci , vol.60 , pp. 648-662
    • Feller, G.1
  • 9
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanktis
    • Feller G, D'Amico S, Gerday C (1999) Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanktis. Biochemistry 38:4613-4619
    • (1999) Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    D'Amico, S.2    Gerday, C.3
  • 10
    • 0026673888 scopus 로고
    • Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis A23
    • Feller G, Lonhienne T, Deroanne C, Libioulle C, Beeumen JV, Gerday C (1992) Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis A23. J Biol Chem 267:5217-5221
    • (1992) J Biol Chem , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhienne, T.2    Deroanne, C.3    Libioulle, C.4    Beeumen, J.V.5    Gerday, C.6
  • 13
    • 29244438994 scopus 로고    scopus 로고
    • Characterisation of a highly stable α-amylase from the halophilic archaeon Haloarcula hispanica
    • Hutcheon GW, Vasisht N, Bolhuis A (2005) Characterisation of a highly stable α-amylase from the halophilic archaeon Haloarcula hispanica. Extremophiles 6:487-495
    • (2005) Extremophiles , vol.6 , pp. 487-495
    • Hutcheon, G.W.1    Vasisht, N.2    Bolhuis, A.3
  • 14
    • 0037027525 scopus 로고    scopus 로고
    • Secondary and quaternary structural transition of the halophilic archaeon nucleotide diphosphate kinase under high- and low-salt conditions
    • Ishibashi M, Arakawa T, Philo JS, Sakashita K, Yonezawa Y, Tokunaga H, TokunagaM (2002) Secondary and quaternary structural transition of the halophilic archaeon nucleotide diphosphate kinase under high- and low-salt conditions. FEMS Microbiol Lett 216:235-241
    • (2002) FEMS Microbiol Lett , vol.216 , pp. 235-241
    • Ishibashi, M.1    Arakawa, T.2    Philo, J.S.3    Sakashita, K.4    Yonezawa, Y.5    Tokunaga, H.6    TokunagaM7
  • 15
    • 0027992184 scopus 로고
    • Cloning, expression, and nucleotide sequence of the α-amylase gene from the haloalkaliphilic archaeon Natronococcus sp strain Ah-36
    • Kobayashi T, Kanai H, Aono R, Horikoshi K, Kudo T (1994) Cloning, expression, and nucleotide sequence of the α-amylase gene from the haloalkaliphilic archaeon Natronococcus sp strain Ah-36. J Bacteriol 176:5131-5134
    • (1994) J Bacteriol , vol.176 , pp. 5131-5134
    • Kobayashi, T.1    Kanai, H.2    Aono, R.3    Horikoshi, K.4    Kudo, T.5
  • 17
    • 13144305048 scopus 로고    scopus 로고
    • Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
    • Machius M, Declerck N, Huber R, Wiegand G (1998) Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 6:281-292
    • (1998) Structure , vol.6 , pp. 281-292
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 18
    • 8744261915 scopus 로고    scopus 로고
    • Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii
    • Madern D, Camacho M, Rodriguez-Arnedo A, Bonete MJ, Zaccai G (2004) Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii. Extremophiles 8:377-384
    • (2004) Extremophiles , vol.8 , pp. 377-384
    • Madern, D.1    Camacho, M.2    Rodriguez-Arnedo, A.3    Bonete, M.J.4    Zaccai, G.5
  • 20
    • 2942674796 scopus 로고    scopus 로고
    • Molecular adaptation: The malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein
    • Madern D, Zaccai G (2004) Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein. Biochimie 86:295-303
    • (2004) Biochimie , vol.86 , pp. 295-303
    • Madern, D.1    Zaccai, G.2
  • 22
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • Mevarech M, Frolow F, Gloss LM (2000) Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86:155-164
    • (2000) Biophys Chem , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 24
    • 16544377687 scopus 로고    scopus 로고
    • Transport of compatible solutes in extremophiles
    • Pflüger K, Müller V (2004) Transport of compatible solutes in extremophiles. J Bioenerg Biomembr 36:17-24
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 17-24
    • Pflüger, K.1    Müller, V.2
  • 27
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectric effects, Hofmeister effects and osmotic effects of salts
    • Record MTJ, Zhang W, Anderson CF (1998) Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectric effects, Hofmeister effects and osmotic effects of salts. Adv Protein Chem 51:281-353
    • (1998) Adv Protein Chem , vol.51 , pp. 281-353
    • Record, M.T.J.1    Zhang, W.2    Anderson, C.F.3
  • 29
    • 33646205656 scopus 로고    scopus 로고
    • Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition
    • Sivakumar N, Li N, Tang JW, Patel BK, Swaminathan K (2006) Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition. FEBS Lett 580:2646-2652
    • (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
  • 30
    • 0028033122 scopus 로고
    • Cold adaptation of enzymes: Structural comparison between salmon and bovine trypsins
    • Smalås AO, Heimstad ES, Hordvik A, Willassen NP, Male R (1994) Cold adaptation of enzymes: structural comparison between salmon and bovine trypsins. Proteins 20:149-166
    • (1994) Proteins , vol.20 , pp. 149-166
    • Smalås, A.O.1    Heimstad, E.S.2    Hordvik, A.3    Willassen, N.P.4    Male, R.5
  • 31
    • 14544285260 scopus 로고    scopus 로고
    • Effect of glycosylation on the catalytic and conformational stability of homologous α-amylases
    • Srimathi S, Jayaraman G (2005) Effect of glycosylation on the catalytic and conformational stability of homologous α-amylases. Protein J 24:79-88
    • (2005) Protein J , vol.24 , pp. 79-88
    • Srimathi, S.1    Jayaraman, G.2
  • 32
    • 21044436414 scopus 로고    scopus 로고
    • Analysis of catalytic and structural stability of native and covalently modified enzymes
    • Svendsen A ed, Marcel Dekker, New York, pp
    • Sundaram PV, Srimathi S (2004) Analysis of catalytic and structural stability of native and covalently modified enzymes. In: Svendsen A (ed) Enzyme functionality: design, engineering and screening. Marcel Dekker, New York, pp 632-661
    • (2004) Enzyme functionality: Design, engineering and screening , pp. 632-661
    • Sundaram, P.V.1    Srimathi, S.2
  • 33
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff SN (1998) Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv Protein Chem 51:355-432
    • (1998) Adv Protein Chem , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 34
    • 14544281033 scopus 로고    scopus 로고
    • Enhanced catalytic and conformational stability of Atlantic cod trypsin upon neoglycosylation
    • Venkatesh R, Srimathi S, Yamuna A, Jayaraman G (2005) Enhanced catalytic and conformational stability of Atlantic cod trypsin upon neoglycosylation. Biochim Biophys Acta 1722:113-115
    • (2005) Biochim Biophys Acta , vol.1722 , pp. 113-115
    • Venkatesh, R.1    Srimathi, S.2    Yamuna, A.3    Jayaraman, G.4
  • 35
    • 0036408309 scopus 로고    scopus 로고
    • The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases
    • Wright DB, Banks DD, Lohman JR, Hilsenbeck JL, Gloss LM (2002) The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases. J Mol Biol 323:327-344
    • (2002) J Mol Biol , vol.323 , pp. 327-344
    • Wright, D.B.1    Banks, D.D.2    Lohman, J.R.3    Hilsenbeck, J.L.4    Gloss, L.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.