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Volumn 267, Issue 12, 2000, Pages 3502-3512

A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures

Author keywords

NAD+ dependent DNA ligase; Overexpression; Psychrophile; Structural comparison; Thermophile

Indexed keywords

POLYDEOXYRIBONUCLEOTIDE SYNTHASE; SEA WATER;

EID: 0033946342     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01377.x     Document Type: Article
Times cited : (60)

References (66)
  • 1
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Molecular basis of cold adaptation
    • 1. Feller, G. & Gerday, C. (1997) Psychrophilic enzymes: molecular basis of cold adaptation. Cell. Mol Life Sci. 53, 830-841.
    • (1997) Cell. Mol Life Sci. , vol.53 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 4
    • 0001946718 scopus 로고
    • Temperature adaptation
    • Hochacka, P.W. & Somero, G.N., eds. Princeton University Press, Princeton, NJ
    • 4. Hochachka, P.W. & Somero, G.N. (1984) Temperature adaptation. In Biochemical Adaptations (Hochacka, P.W. & Somero, G.N., eds), pp. 355-449. Princeton University Press, Princeton, NJ.
    • (1984) Biochemical Adaptations , pp. 355-449
    • Hochachka, P.W.1    Somero, G.N.2
  • 5
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level
    • 5. 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
  • 6
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium
    • 6. Russell, R.J., Gerike, U., Danson, M.J., Hough, D.W. & Taylor, G.L. (1998) Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 6, 351-361.
    • (1998) Structure , vol.6 , pp. 351-361
    • Russell, R.J.1    Gerike, U.2    Danson, M.J.3    Hough, D.W.4    Taylor, G.L.5
  • 8
    • 0033597205 scopus 로고    scopus 로고
    • Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum
    • 8. Kim, S.Y., Hwang, K.Y., Kim, S.H., Sung, H.C., Han, Y.S. & Cho, Y.J. (1999) Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J. Biol. Chem. 274, 11761-11767.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11761-11767
    • Kim, S.Y.1    Hwang, K.Y.2    Kim, S.H.3    Sung, H.C.4    Han, Y.S.5    Cho, Y.J.6
  • 9
    • 0016273515 scopus 로고
    • DNA ligase: Structure, mechanism, and function
    • 9. Lehman, I.R. (1974) DNA ligase: structure, mechanism, and function. Science 186, 790-797.
    • (1974) Science , vol.186 , pp. 790-797
    • Lehman, I.R.1
  • 11
    • 0031260117 scopus 로고    scopus 로고
    • Mammalian DNA ligases
    • 11. Tomkinson, A.E. & Levin, D.S. (1997) Mammalian DNA ligases. Bioessays 19, 893-901.
    • (1997) Bioessays , vol.19 , pp. 893-901
    • Tomkinson, A.E.1    Levin, D.S.2
  • 12
    • 0014078321 scopus 로고
    • Enzymatic breakage and joining of deoxyribonucleic acid. I. Repair of single-strand breaks in DNA by an enzyme system from Escherichia coli infected with T4 bacteriophage
    • 12. Weiss, B. & Richardson, C.C. (1967) Enzymatic breakage and joining of deoxyribonucleic acid. I. Repair of single-strand breaks in DNA by an enzyme system from Escherichia coli infected with T4 bacteriophage. Proc. Natl Acad. Sci. USA 57, 1021-1028.
    • (1967) Proc. Natl Acad. Sci. USA , vol.57 , pp. 1021-1028
    • Weiss, B.1    Richardson, C.C.2
  • 13
    • 0022422374 scopus 로고
    • The nucleotide sequence of the DNA ligase gene (CDC9) from Saccharomyces cerevisiae: A gene which is cell-cycle regulated and induced in response to DNA damage
    • 13. Barker, D.G., White, J.H. & Johnston, L.H. (1985) The nucleotide sequence of the DNA ligase gene (CDC9) from Saccharomyces cerevisiae: a gene which is cell-cycle regulated and induced in response to DNA damage. Nucleic Acids Res. 13, 8323-8337.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8323-8337
    • Barker, D.G.1    White, J.H.2    Johnston, L.H.3
  • 14
    • 0026011091 scopus 로고
    • Location of the active site for enzyme-adenylate formation in DNA ligases
    • 14. Tomkinson, A.E., Totty, N.F., Ginsburg, M. & Lindahl, T. (1991) Location of the active site for enzyme-adenylate formation in DNA ligases. Proc. Natl Acad. Sci. USA 88, 400-404.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 400-404
    • Tomkinson, A.E.1    Totty, N.F.2    Ginsburg, M.3    Lindahl, T.4
  • 15
    • 0026661136 scopus 로고
    • Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases
    • 15. Kletzin, A. (1992) Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases. Nucleic Acids Res. 20, 5389-5396.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5389-5396
    • Kletzin, A.1
  • 16
    • 0014093442 scopus 로고
    • Enzymatic joining of DNA strands: A novel reaction of diphosphopyridine nucleotide
    • 16. Zimmerman, S.B., Little, J.W., Oshinsky, C.K. & Gellert, M. (1967) Enzymatic joining of DNA strands: a novel reaction of diphosphopyridine nucleotide. Proc. Natl Acad. Sci. USA 57, 1841-1848.
    • (1967) Proc. Natl Acad. Sci. USA , vol.57 , pp. 1841-1848
    • Zimmerman, S.B.1    Little, J.W.2    Oshinsky, C.K.3    Gellert, M.4
  • 17
    • 0026917009 scopus 로고
    • Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis
    • 17. Shark, K.B. & Conway, T. (1992) Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis. FEMS Microbiol. Lett. 75, 19-26.
    • (1992) FEMS Microbiol. Lett. , vol.75 , pp. 19-26
    • Shark, K.B.1    Conway, T.2
  • 19
    • 0021229570 scopus 로고
    • Thermophilic DNA ligase. Purification and properties of the enzyme from Thermus thermophilus HB8
    • 19. Takahashi, M., Yamaguchi, E. & Uchida, T. (1984) Thermophilic DNA ligase. Purification and properties of the enzyme from Thermus thermophilus HB8. J. Biol. Chem. 259, 10041-10047.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10041-10047
    • Takahashi, M.1    Yamaguchi, E.2    Uchida, T.3
  • 20
    • 0029096564 scopus 로고
    • Cloning and sequence analysis of the DNA ligase-encoding gene of Rhodothermus marinus, and overproduction, purification and characterization of two thermophilic DNA ligases
    • 20. Thorbjarnardóttir, S.H., Jónsson, Z.O., Andresson, O.S., Kristjánsson, J.K., Eggertsson, G. & Pálsdóttir, A. (1995) Cloning and sequence analysis of the DNA ligase-encoding gene of Rhodothermus marinus, and overproduction, purification and characterization of two thermophilic DNA ligases. Gene 161, 1-6.
    • (1995) Gene , vol.161 , pp. 1-6
    • Thorbjarnardóttir, S.H.1    Jónsson, Z.O.2    Andresson, O.S.3    Kristjánsson, J.K.4    Eggertsson, G.5    Pálsdóttir, A.6
  • 21
    • 0032584830 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence, and expression of the DNA ligase-encoding gene from Thermus filiformis
    • 21. Kim, H.K. & Kwon, ST. (1998) Cloning, nucleotide sequence, and expression of the DNA ligase-encoding gene from Thermus filiformis. Mol. Cells 8, 438-443.
    • (1998) Mol. Cells , vol.8 , pp. 438-443
    • Kim, H.K.1    Kwon, S.T.2
  • 22
    • 0030738222 scopus 로고    scopus 로고
    • Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae
    • 22. Cheng, C. & Shuman, S. (1997) Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae. Nucleic Acids Res. 25, 1369-1374.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1369-1374
    • Cheng, C.1    Shuman, S.2
  • 23
    • 0031736121 scopus 로고    scopus 로고
    • Evidence for massive gene exchange between archaeal and bacterial hyperthermophiles
    • 23. Aravind, L., Tatusov, R.L., Wolf, Y.I., Walker, D.R. & Koonin, E.V. (1998) Evidence for massive gene exchange between archaeal and bacterial hyperthermophiles. Trends Genet. 14, 442-444.
    • (1998) Trends Genet. , vol.14 , pp. 442-444
    • Aravind, L.1    Tatusov, R.L.2    Wolf, Y.I.3    Walker, D.R.4    Koonin, E.V.5
  • 25
    • 0027137057 scopus 로고
    • Cloning of the large subunit of activator 1 (replication factor C) reveals homology with bacterial DNA ligases
    • 25. Burbelo, P.D., Utani, A., Pan, Z.Q. & Yamada, Y. (1993) Cloning of the large subunit of activator 1 (replication factor C) reveals homology with bacterial DNA ligases. Proc. Natl Acad. Sci. USA 90, 11543-11547.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11543-11547
    • Burbelo, P.D.1    Utani, A.2    Pan, Z.Q.3    Yamada, Y.4
  • 26
    • 0015844621 scopus 로고
    • Deoxyribonucleic acid ligase. Isolation and physical characterization of the homogeneous enzyme from Escherichia coli
    • 26. Modrich, P., Anraku, Y. & Lehman, I.R. (1973) Deoxyribonucleic acid ligase. Isolation and physical characterization of the homogeneous enzyme from Escherichia coli. J. Biol. Chem. 248, 7495-7501.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7495-7501
    • Modrich, P.1    Anraku, Y.2    Lehman, I.R.3
  • 27
    • 0017847292 scopus 로고
    • A simple, three-step procedure for the large scale purification of DNA ligase from a hybrid lambda lysogen constructed in vitro
    • 27. Panasenko, S.M., Alazard, R.J. & Lehman, I.R. (1978) A simple, three-step procedure for the large scale purification of DNA ligase from a hybrid lambda lysogen constructed in vitro. J. Biol. Chem. 253, 4590-4592.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4590-4592
    • Panasenko, S.M.1    Alazard, R.J.2    Lehman, I.R.3
  • 28
    • 0022557540 scopus 로고
    • Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli
    • 28. Ishino, Y., Shinagawa, H., Makino, K., Tsunasawu, S., Sakiyama, F. & Nakata, A. (1986) Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli. Mol. Gen. Genet. 204, 1-7.
    • (1986) Mol. Gen. Genet. , vol.204 , pp. 1-7
    • Ishino, Y.1    Shinagawa, H.2    Makino, K.3    Tsunasawu, S.4    Sakiyama, F.5    Nakata, A.6
  • 29
    • 3042689834 scopus 로고
    • Macromolecular crowding allows blunt-end ligation by DNA ligases from rat liver or Escherichia coli
    • 29. Zimmerman, S.B. & Pheiffer, B.H. (1983) Macromolecular crowding allows blunt-end ligation by DNA ligases from rat liver or Escherichia coli. Proc. Natl Acad. Sci. USA 80, 5852-5856.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 5852-5856
    • Zimmerman, S.B.1    Pheiffer, B.H.2
  • 31
    • 0030574263 scopus 로고    scopus 로고
    • Co-operativity of hexamer ligation
    • 31. Kaczorowski, T. & Szybalski, W. (1996) Co-operativity of hexamer ligation. Gene 179, 189-193.
    • (1996) Gene , vol.179 , pp. 189-193
    • Kaczorowski, T.1    Szybalski, W.2
  • 32
    • 0022742336 scopus 로고
    • Thermophilic HB8 DNA ligase: Effects of polyethylene glycols and polyamines on blunt-end ligation of DNA
    • 32. Takahashi, M. & Uchida, T. (1986) Thermophilic HB8 DNA ligase: effects of polyethylene glycols and polyamines on blunt-end ligation of DNA. J. Biochem. (Tokyo) 100, 123-131.
    • (1986) J. Biochem. (Tokyo) , vol.100 , pp. 123-131
    • Takahashi, M.1    Uchida, T.2
  • 33
    • 0025889025 scopus 로고
    • Cloning, overexpression and nucleotide sequence of a thermostable DNA ligase-encoding gene
    • 33. Barany, F. & Gelfand, D.H. (1991) Cloning, overexpression and nucleotide sequence of a thermostable DNA ligase-encoding gene. Gene 109, 1-11.
    • (1991) Gene , vol.109 , pp. 1-11
    • Barany, F.1    Gelfand, D.H.2
  • 34
    • 0026349588 scopus 로고
    • Cloning, nucleotide sequence, and engineered expression of Thermus thermophilus DNA ligase, a homolog of Escherichia coli DNA ligase
    • 34. Lauer, G., Rudd, E.A., McKay, D.L., Ally, A., Ally, D. & Backman, K.C. (1991) Cloning, nucleotide sequence, and engineered expression of Thermus thermophilus DNA ligase, a homolog of Escherichia coli DNA ligase. J. Bacteriol. 173, 5047-5053.
    • (1991) J. Bacteriol. , vol.173 , pp. 5047-5053
    • Lauer, G.1    Rudd, E.A.2    McKay, D.L.3    Ally, A.4    Ally, D.5    Backman, K.C.6
  • 35
    • 0029744212 scopus 로고    scopus 로고
    • Identification of essential residues in Thermus thermophilus DNA ligase
    • 35. Luo, J. & Barany, F. (1996) Identification of essential residues in Thermus thermophilus DNA ligase. Nucleic Acids Res. 24, 3079-3085.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3079-3085
    • Luo, J.1    Barany, F.2
  • 36
    • 0029776838 scopus 로고    scopus 로고
    • Improving the fidelity of Thermus thermophilus DNA ligase
    • 36. Luo, J., Bergstrom, D.E. & Barany, F. (1996) Improving the fidelity of Thermus thermophilus DNA ligase. Nucleic Acids Res. 24, 3071-3078.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3071-3078
    • Luo, J.1    Bergstrom, D.E.2    Barany, F.3
  • 37
    • 0030738913 scopus 로고    scopus 로고
    • Effects of base mismatches on joining of short oligodeoxynucleotides by DNA ligases
    • 37. Pritchard, C.E. & Southern, E.M. (1997) Effects of base mismatches on joining of short oligodeoxynucleotides by DNA ligases. Nucleic Acids Res. 25, 3403-3407.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3403-3407
    • Pritchard, C.E.1    Southern, E.M.2
  • 38
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 38. Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 39
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • 39. Sali, A. & Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 40
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • 40. Sali, A. & Overington, J.P. (1994) Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci. 3, 1582-1596.
    • (1994) Protein Sci. , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 41
    • 0028871814 scopus 로고
    • Evaluation of comparative protein modeling by MODELLER
    • 41. Sali, A., Potterton, L., Yuan, F., van vlijmen, H. & Karplus, M. (1995) Evaluation of comparative protein modeling by MODELLER. Proteins 23, 318-326.
    • (1995) Proteins , vol.23 , pp. 318-326
    • Sali, A.1    Potterton, L.2    Yuan, F.3    Van Vlijmen, H.4    Karplus, M.5
  • 42
    • 0029361476 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • 42. Sali, A. (1995) Comparative protein modeling by satisfaction of spatial restraints. Mol. Med. Today. 1, 270-277.
    • (1995) Mol. Med. Today , vol.1 , pp. 270-277
    • Sali, A.1
  • 43
    • 0031307019 scopus 로고    scopus 로고
    • Evaluation of comparative protein structure modeling by MODELLER-3
    • 43. Sanchez, R. & Sali, A. (1997) Evaluation of comparative protein structure modeling by MODELLER-3. Proteins Suppl. 1, 50-58.
    • (1997) Proteins Suppl. , vol.1 , pp. 50-58
    • Sanchez, R.1    Sali, A.2
  • 44
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • 44. Brünger, A.T., Kuriyan, J. & Karplus, M. (1987) Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 45
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 45. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 47
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • 47. McDonald, I.K. & Thornton, J.M. (1994) Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 49
  • 50
    • 0032480772 scopus 로고    scopus 로고
    • DNA polymerase III of Gram-positive eubacteria is a zinc metalloprotein conserving an essential finger-like domain
    • 50. Barnes, M.H., Leo, C.J. & Brown, N.C. (1998) DNA polymerase III of Gram-positive eubacteria is a zinc metalloprotein conserving an essential finger-like domain. Biochemistry 37, 15254-15260.
    • (1998) Biochemistry , vol.37 , pp. 15254-15260
    • Barnes, M.H.1    Leo, C.J.2    Brown, N.C.3
  • 51
    • 0039710446 scopus 로고    scopus 로고
    • Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen
    • 51. Jónsson, Z.O., Hindges, R. & Hübscher, U. (1998) Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen. EMBO J. 17, 2412-2425.
    • (1998) EMBO J. , vol.17 , pp. 2412-2425
    • Jónsson, Z.O.1    Hindges, R.2    Hübscher, U.3
  • 52
    • 0033013881 scopus 로고    scopus 로고
    • Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus
    • 52. Brannigan, J.A., Ashford, S.R., Doherty, A.J., Timson, D.J. & Wigley, D.B. (1999) Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus. Biochim. Biophys. Acta 1432, 413-418.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 413-418
    • Brannigan, J.A.1    Ashford, S.R.2    Doherty, A.J.3    Timson, D.J.4    Wigley, D.B.5
  • 53
    • 0026316725 scopus 로고
    • Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006
    • 53. Watanabe, K., Chishiro, K., Kitamura, K. & Suzuki, Y. (1991) Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem. 266, 24287-24294.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24287-24294
    • Watanabe, K.1    Chishiro, K.2    Kitamura, K.3    Suzuki, Y.4
  • 54
    • 0028130117 scopus 로고
    • Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule
    • 54. Watanabe, K., Masuda, T., Ohashi, H., Mihara, H. & Suzuki, Y. (1994) Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule. Eur. J. Biochem. 226, 277-283.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihara, H.4    Suzuki, Y.5
  • 55
    • 0029890431 scopus 로고    scopus 로고
    • Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues
    • 55. Watanabe, K., Kitamura, K. & Suzuki, Y. (1996) Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues. Appl. Environ. Microbiol. 62, 2066-2073.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2066-2073
    • Watanabe, K.1    Kitamura, K.2    Suzuki, Y.3
  • 56
    • 0032087621 scopus 로고    scopus 로고
    • Clustered proline residues around the active-site cleft in thermostable oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228
    • 56. Kashiwabara, S., Matsuki, Y., Kishimoto, T. & Suzuki, Y. (1998) Clustered proline residues around the active-site cleft in thermostable oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228. Biosci. Biotechnol. Biochem. 62, 1093-1102.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1093-1102
    • Kashiwabara, S.1    Matsuki, Y.2    Kishimoto, T.3    Suzuki, Y.4
  • 59
    • 0031279830 scopus 로고    scopus 로고
    • Molecular adaptations of enzymes from psychrophilic organisms
    • 59. Feller, G., Arpigny, J.L., Narinx, E. & Gerday, C. (1997) Molecular adaptations of enzymes from psychrophilic organisms. Comp. Biochem. Physiol. 118, 495-499.
    • (1997) Comp. Biochem. Physiol. , vol.118 , pp. 495-499
    • Feller, G.1    Arpigny, J.L.2    Narinx, E.3    Gerday, C.4
  • 60
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • 60. Dill, K.A. (1990) Dominant forces in protein folding. Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 61
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • 61. Doig, A.J. & Williams, D.H. (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
  • 62
    • 0028033122 scopus 로고
    • Cold adaption of enzymes: Structural comparison between salmon and bovine trypsins
    • 62. Smalas, A.O., Heimstad, E.S., Hordvik, A., Willassen, N.P. & Male, R. (1994) Cold adaption of enzymes: structural comparison between salmon and bovine trypsins. Proteins 20, 149-166.
    • (1994) Proteins , vol.20 , pp. 149-166
    • Smalas, A.O.1    Heimstad, E.S.2    Hordvik, A.3    Willassen, N.P.4    Male, R.5
  • 63
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • 63. Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. & Higgins, D.G. (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 64
    • 0015333007 scopus 로고
    • Stability constant for the zinc-dithiothreitol complex
    • 64. Cornell, N.W. & Crivaro, K.E. (1972) Stability constant for the zinc-dithiothreitol complex. Anal. Biochem. 47, 203-208.
    • (1972) Anal. Biochem. , vol.47 , pp. 203-208
    • Cornell, N.W.1    Crivaro, K.E.2
  • 65
    • 0019325181 scopus 로고
    • Crystallographic refinement of rubredoxin at 1.2 Å degrees resolution
    • 65. Watenpaugh, K.D., Sieker, L.C. & Jensen, L.H. (1980) Crystallographic refinement of rubredoxin at 1.2 Å degrees resolution. J. Mol. Biol. 138, 615-633.
    • (1980) J. Mol. Biol. , vol.138 , pp. 615-633
    • Watenpaugh, K.D.1    Sieker, L.C.2    Jensen, L.H.3
  • 66
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis
    • 66. Feller, G., d'Amico, D. & Gerday, C. (1999) Thermodynamic stability of a cold-active α-amylase from the 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


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