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Volumn 187, Issue 17, 2005, Pages 6206-6212

Role of disulfide bridges in the activity and stability of a cold-active α-amylase

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; CYSTEINE; IODOACETAMIDE; IODOACETIC ACID; MERCAPTOETHANOL;

EID: 24344448645     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.17.6206-6212.2005     Document Type: Article
Times cited : (62)

References (39)
  • 1
    • 0031910806 scopus 로고    scopus 로고
    • Crystal structure of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
    • Aghajari, N., G. Feller, C. Gerday, and R. Haser. 1998. Crystal structure of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 7:564-572.
    • (1998) Protein Sci. , vol.7 , pp. 564-572
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 2
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level
    • Aghajari, N., G. Feller, C. Gerday, and R. Haser. 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
  • 4
    • 0033582933 scopus 로고    scopus 로고
    • Bridge over troubled waters: Sensing stress by disulfide-bond formation
    • Aslund, F., and J. Beckwith. 1999. Bridge over troubled waters: sensing stress by disulfide-bond formation. Cell 96:751-753.
    • (1999) Cell , vol.96 , pp. 751-753
    • Aslund, F.1    Beckwith, J.2
  • 6
    • 17444415538 scopus 로고    scopus 로고
    • Cold-adapted enzymes
    • A. Pandey, C. Webb, C. R. Soccol, and C. Larroche (ed.). AsiaTech Publishers, New Delhi, India
    • Cavicchioli, R., and K. S. Siddiqui. 2004. Cold-adapted enzymes, p. 615-638. In A. Pandey, C. Webb, C. R. Soccol, and C. Larroche (ed.), Enzyme technology. AsiaTech Publishers, New Delhi, India.
    • (2004) Enzyme Technology , pp. 615-638
    • Cavicchioli, R.1    Siddiqui, K.S.2
  • 8
    • 1642458395 scopus 로고    scopus 로고
    • Horizontal gene transfer from Eukarya to bacteria and domain shuffling: The α-amylase model
    • Da Lage, J. L., G. Feller, and S. Janecek. 2004. Horizontal gene transfer from Eukarya to bacteria and domain shuffling: the α-amylase model. Cell. Mol. Life Sci. 61:97-109.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 97-109
    • Da Lage, J.L.1    Feller, G.2    Janecek, S.3
  • 9
    • 0035854688 scopus 로고    scopus 로고
    • Structural determinants of cold adaptation and stability in a large protein
    • D'Amico, S., C. Gerday, and G. Feller. 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
  • 10
    • 0037195912 scopus 로고    scopus 로고
    • Dual effects of an extra disulfide-bond on the activity and stability of a cold-adapted α-amylase
    • D'Amico, S., C. Gerday, and G. Feller. 2002. Dual effects of an extra disulfide-bond on the activity and stability of a cold-adapted α-amylase. J. Biol. Chem. 277:46110-46115.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46110-46115
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 11
    • 0041384407 scopus 로고    scopus 로고
    • Temperature adaptation of proteins: Engineering mesophilic-like activity and stability in a cold-adapted α-amylase
    • D'Amico, S., C. Gerday, and G. Feller. 2003. Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted α-amylase. J. Mol. Biol. 332:981-988.
    • (2003) J. Mol. Biol. , vol.332 , pp. 981-988
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 12
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationship in extremophilic enzymes
    • D'Amico, S., J. C. Marx, C. Gerday, and G. Feller. 2003. Activity-stability relationship 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
  • 13
    • 0034713903 scopus 로고    scopus 로고
    • Structural similarities and evolutionary relationships in chloride-dependent α-amylases
    • D'Amico, S., C. Gerday, and G. Feller. 2000. Structural similarities and evolutionary relationships in chloride-dependent α-amylases. Gene 253:95-105.
    • (2000) Gene , vol.253 , pp. 95-105
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 14
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • Doig, A. J., and D. H. Williams. 1991. Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J. Mol. Biol. 217:389-398.
    • (1991) J. Mol. Biol. , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 15
    • 0000346442 scopus 로고
    • The application of the theory of absolute reaction rates to proteins
    • Eyring, H., and A. E. Stearn. 1939. The application of the theory of absolute reaction rates to proteins. Chem. Rev. 24:253-270.
    • (1939) Chem. Rev. , vol.24 , pp. 253-270
    • Eyring, H.1    Stearn, A.E.2
  • 16
    • 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
  • 17
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller, G., and C. Gerday. 2003. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1:200-208.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 18
  • 19
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from Antarctic bacterium Alteromonas haloplanctis
    • Feller, G., D. d'Amico, and C. Gerday. 1999. Thermodynamic stability of a cold-active α-amylase from Antarctic bacterium Alteromonas haloplanctis. Biochemistry 38:4613-4619.
    • (1999) Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    D'Amico, D.2    Gerday, C.3
  • 20
    • 0028289989 scopus 로고
    • Stability and structural analysis of an α-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23
    • Feller, G., F. Payan, F. Theys, M. Qian, R. Haser, and C. Gerday. 1994. Stability and structural analysis of an α-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23. Eur. J. Biochem. 222:441-447.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 441-447
    • Feller, G.1    Payan, F.2    Theys, F.3    Qian, M.4    Haser, R.5    Gerday, C.6
  • 23
    • 0000925011 scopus 로고
    • Analysis of protein conformation by gel electrophoresis
    • T. E. Creighton (ed.). IRL Press, Oxford, United Kingdom
    • Goldenberg, D. P. 1989. Analysis of protein conformation by gel electrophoresis, p. 225-250. In T. E. Creighton (ed.), Protein structure: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1989) Protein Structure: A Practical Approach , pp. 225-250
    • Goldenberg, D.P.1
  • 24
    • 0021416620 scopus 로고
    • Gel electrophoresis in studies of protein conformation and folding
    • Goldenberg, D. P., and T. E. Creighton. 1984. Gel electrophoresis in studies of protein conformation and folding. Anal. Biochem. 138:1-18.
    • (1984) Anal. Biochem. , vol.138 , pp. 1-18
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 25
    • 0000215805 scopus 로고
    • Counting integral number of residues by chemical modification
    • T. E. Creighton (ed.). IRL Press, Oxford, United Kingdom
    • Hollecker, M. 1989. Counting integral number of residues by chemical modification, p. 145-153. In T. E. Creighton (ed.), Protein structure: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1989) Protein Structure: A Practical Approach , pp. 145-153
    • Hollecker, M.1
  • 26
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob, U., W. Muse, M. Eser, and J. C. Bardwell. 1999. Chaperone activity with a redox switch. Cell 96:341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 27
    • 0037197677 scopus 로고    scopus 로고
    • Maximal stabilities of reversible two-state proteins
    • Kumar, S., J.-G. Tsai, and R. Nussinov. 2002. Maximal stabilities of reversible two-state proteins. Biochemistry 41:5359-5374.
    • (2002) Biochemistry , vol.41 , pp. 5359-5374
    • Kumar, S.1    Tsai, J.-G.2    Nussinov, R.3
  • 28
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for the determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for the determination of reducing sugar. Anal. Chem. 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 29
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide-bonds
    • Pace, C. N., G. R. Grimsley, J. A. Thomson, and B. J. Bernett. 1988. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide-bonds. J. Biol. Chem. 263:11820-11825.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thomson, J.A.3    Bernett, B.J.4
  • 30
    • 0018588511 scopus 로고
    • Stability of proteins
    • Privalov, P. L. 1979. Stability of proteins. Adv. Protein Chem. 33:167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 31
    • 0027296794 scopus 로고
    • Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution
    • Qian, M., R. Haser, and F. Payan. 1993. Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution. J. Mol. Biol. 231:785-799.
    • (1993) J. Mol. Biol. , vol.231 , pp. 785-799
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 32
    • 0002964990 scopus 로고
    • Estimating molecular weights of polypeptides by SDS gel electrophoresis
    • T. E. Creighton (ed.). IRL Press, Oxford, United Kingdom
    • See, Y. P., and G. Jackowski. 1989. Estimating molecular weights of polypeptides by SDS gel electrophoresis, p. 1-21. In T. E. Creighton (ed.), Protein structure: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1989) Protein Structure: A Practical Approach , pp. 1-21
    • See, Y.P.1    Jackowski, G.2
  • 33
    • 0034307643 scopus 로고    scopus 로고
    • Carboxyl group modification significantly altered the kinetic properties of purified carboxymethylcellulase from Aspergillus niger
    • Siddiqui, K. S., A. A. Najmus-Saquib, M. H. Rashid, and M. I. Rajoka. 2000. Carboxyl group modification significantly altered the kinetic properties of purified carboxymethylcellulase from Aspergillus niger. Enzyme Microb. Technol. 27:467-474.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 467-474
    • Siddiqui, K.S.1    Najmus-Saquib, A.A.2    Rashid, M.H.3    Rajoka, M.I.4
  • 34
    • 0036545550 scopus 로고    scopus 로고
    • Thermodynamic activation properties of elongation factor 2 (EF-2) proteins from psychrotolerant and thermophilic archaea
    • Siddiqui, K. S., R. Cavicchioli, and T. Thomas. 2002. Thermodynamic activation properties of elongation factor 2 (EF-2) proteins from psychrotolerant and thermophilic archaea. Extremophiles 6:143-150.
    • (2002) Extremophiles , vol.6 , pp. 143-150
    • Siddiqui, K.S.1    Cavicchioli, R.2    Thomas, T.3
  • 35
    • 24344486447 scopus 로고    scopus 로고
    • The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted α-amylase
    • 34a. Siddiqui, K. S., G. Feller, S. D'Amico, C. Gerday, L. Giaquinto, and R. Cavicchioli. 2005. The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted α-amylase. J. Bacteriol. 187:6197-6205.
    • (2005) J. Bacteriol. , vol.187 , pp. 6197-6205
    • Siddiqui, K.S.1    Feller, G.2    D'Amico, S.3    Gerday, C.4    Giaquinto, L.5    Cavicchioli, R.6
  • 37
    • 0025777290 scopus 로고
    • Structural and functional roles of cysteine residues of Bacillus polymyxa β-amylase
    • Uozumi, N., T. Matsuda, N. Tsukagoshi, and S. Udaka. 1991. Structural and functional roles of cysteine residues of Bacillus polymyxa β-amylase. Biochemistry 30:4594-4599.
    • (1991) Biochemistry , vol.30 , pp. 4594-4599
    • Uozumi, N.1    Matsuda, T.2    Tsukagoshi, N.3    Udaka, S.4
  • 38
    • 0029562948 scopus 로고
    • Mechanism of protein stabilization by disulfide-bridges: Calorimetric unfolding studies of disulfide-deficient mutants of the α-amylase inhibitor tendamistat
    • Vogl, T., R. Brengelmann, H.-J. Hinz, M. Scharf, M. Lotzbeyer, and J. W. Engels. 1995. Mechanism of protein stabilization by disulfide-bridges: calorimetric unfolding studies of disulfide-deficient mutants of the α-amylase inhibitor tendamistat. J. Mol. Biol. 254:481-496.
    • (1995) J. Mol. Biol. , vol.254 , pp. 481-496
    • Vogl, T.1    Brengelmann, R.2    Hinz, H.-J.3    Scharf, M.4    Lotzbeyer, M.5    Engels, J.W.6
  • 39
    • 0001227472 scopus 로고
    • Harnessing disulfide-bonds using protein engineering
    • Wetzel, R. 1987. Harnessing disulfide-bonds using protein engineering. Trends Biochem. Sci. 12:478-482.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 478-482
    • Wetzel, R.1


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