메뉴 건너뛰기




Volumn 6, Issue , 2000, Pages 1-57

Cold adapted enzymes

Author keywords

Catalytic activity; Catalytic efficiency; Cold active; Cold adaptation; Enzyme; Molecular flexibility; Psychrophilic; Structural features; Thermal stability

Indexed keywords

ARGININE; ENZYME; ENZYME INHIBITOR; GLYCINE; ION; ISOENZYME; METHIONINE; PROLINE;

EID: 0034568704     PISSN: 13872656     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1387-2656(00)06018-X     Document Type: Article
Times cited : (198)

References (193)
  • 1
    • 84867840437 scopus 로고
    • General biology and nomenclature of psychrophilic bacteria
    • N.B. Gibbons, Editor. University of Toronto Press: Toronto
    • Stoke, J.L., General biology and nomenclature of psychrophilic bacteria., in Recent progress in Microbiology, N.B. Gibbons, Editor. 1963, University of Toronto Press: Toronto, p. 18-92.
    • (1963) Recent Progress in Microbiology , pp. 18-92
    • Stoke, J.L.1
  • 2
    • 0016516090 scopus 로고
    • Psychrophilic bacteria
    • Morita, R.Y., Psychrophilic bacteria. Bacteriology Reviews, 1975. 39: p. 144-167.
    • (1975) Bacteriology Reviews , vol.39 , pp. 144-167
    • Morita, R.Y.1
  • 3
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Molecular basis of cold adaptation
    • Feller, G. & Gerday, C., Psychrophilic enzymes: molecular basis of cold adaptation. CMLS Cell, and Mol. Life Sci., 1997. 53: p. 830-841.
    • (1997) CMLS Cell, and Mol. Life Sci. , vol.53 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 4
    • 0030513148 scopus 로고    scopus 로고
    • Psychrophilic microorganisms and their cold-active enzymes
    • Brenchley, J.E., Psychrophilic microorganisms and their cold-active enzymes. J. of Industrial Microbiology, 1996. 17: p. 432-437.
    • (1996) J. of Industrial Microbiology , vol.17 , pp. 432-437
    • Brenchley, J.E.1
  • 6
    • 0031941134 scopus 로고    scopus 로고
    • Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties
    • Alvarez, M., Zeelen, J.P., Mainfroid, V., Rentier-Delrue, F., Martial, J.A., Wyns, L., Wierenga, R.K., & Maes, D., Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties. J Biol Chem, 1998. 273(4): p. 2199-206.
    • (1998) J Biol Chem , vol.273 , Issue.4 , pp. 2199-2206
    • Alvarez, M.1    Zeelen, J.P.2    Mainfroid, V.3    Rentier-Delrue, F.4    Martial, J.A.5    Wyns, L.6    Wierenga, R.K.7    Maes, D.8
  • 7
    • 0029114702 scopus 로고
    • Molecular cloning and characterization of anionic and cationic variants of trypsin from Atlantic salmon
    • Male, R., Lorens, J.B., Smal s, A.O., Torrissen, K.R., Molecular cloning and characterization of anionic and cationic variants of trypsin from Atlantic salmon. Eur. J. Biochem., 1995. 232: p. 677-685.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 677-685
    • Male, R.1    Lorens, J.B.2    Smal S, A.O.3    Torrissen, K.R.4
  • 8
    • 0029851195 scopus 로고    scopus 로고
    • Temperature and pH sensitivity of trypsins from atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin
    • Outzen, H., Berglund, G.I., Smal s, A.O., & Willassen, N.P., Temperature and pH sensitivity of trypsins from atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin. Comp. Biochem. Biophys., 1996. 115B: p. 33-45.
    • (1996) Comp. Biochem. Biophys. , vol.115 B , pp. 33-45
    • Outzen, H.1    Berglund, G.I.2    Smal S, A.O.3    Willassen, N.P.4
  • 9
    • 85013534503 scopus 로고
    • Temperature: The ectothermy option
    • M. Hochachka, Editor. Elsevier Science Publisher B.V.
    • Hochachka, P.W., Temperature: the ectothermy option, in Biochemistry and molecular biology of fishes, M. Hochachka, Editor. 1991, Elsevier Science Publisher B.V. p. 313-322.
    • (1991) Biochemistry and Molecular Biology of Fishes , pp. 313-322
    • Hochachka, P.W.1
  • 10
    • 0015578550 scopus 로고
    • Temperature adaptation of enzymes: Roles of the free energy, enthalpy, and the entropy of activation
    • Low, P.S., Bada, J.L. & Somero, G.N., Temperature adaptation of enzymes: Roles of the free energy, enthalpy, and the entropy of activation. Proc. Nat. Acad. Sci. USA, 1973. 70: p. 430-432.
    • (1973) Proc. Nat. Acad. Sci. USA , vol.70 , pp. 430-432
    • Low, P.S.1    Bada, J.L.2    Somero, G.N.3
  • 11
    • 0021707123 scopus 로고
    • Purification and characterization of trypsin from the Greenland cod (Gadus ogac.). 1. Kinetic and thermodynamic characteristics
    • Simpson, B.K. & Haard, N.F, Purification and characterization of trypsin from the Greenland cod (Gadus ogac.). 1. Kinetic and thermodynamic characteristics. Can. J. Biochem. Cell Biol., 1984. 62: p. 894-900.
    • (1984) Can. J. Biochem. Cell Biol. , vol.62 , pp. 894-900
    • Simpson, B.K.1    Haard, N.F.2
  • 12
    • 0028292010 scopus 로고
    • Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41
    • Davail, S., Feller, G., Narinx, E. & Gerday, C., Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41. J. Biol. Chem., 1994. 259: p. 17448-17453.
    • (1994) J. Biol. Chem. , vol.259 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 13
    • 0032985526 scopus 로고    scopus 로고
    • A cold-active glucanase from Ruminal Bacterium Fibrobacter succinogenes S85
    • Iyo, A.H., & Forsberg C.W., A cold-active glucanase from Ruminal Bacterium Fibrobacter succinogenes S85. Appl. and Environ. Microbiol., 1999. 65: p. 995-998.
    • (1999) Appl. and Environ. Microbiol. , vol.65 , pp. 995-998
    • Iyo, A.H.1    Forsberg, C.W.2
  • 14
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: Realized increases in conformational flexibility in lactate dehydrogenase A4 ortologs of Antarctic notothenioid fishes
    • Fields, P.A. & Somero, G.N., Hot spots in cold adaptation: Realized increases in conformational flexibility in lactate dehydrogenase A4 ortologs of Antarctic notothenioid fishes. Proc. Nat. Acad. Sci. USA, 1998. 95: p. 11476-11481.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 15
    • 0001946718 scopus 로고
    • Temperature adaptation
    • Princeton University Press, New Jersey, Chapter 11
    • Hochachka, P.W. & Somero, G.N., Temperature adaptation. In Biochemical Adaptations, Princeton University Press, New Jersey, Chapter 11. 1984.
    • (1984) Biochemical Adaptations
    • Hochachka, P.W.1    Somero, G.N.2
  • 16
    • 0001386812 scopus 로고
    • Purification and characterization of trypsin from pyloric caeca of rainbow trout (Oncorhynchus mykiss)
    • Kristjansson, M.M., Purification and characterization of trypsin from pyloric caeca of rainbow trout (Oncorhynchus mykiss). J. Agric. Food Chem., 1991. 39: p. 1738-1742.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1738-1742
    • Kristjansson, M.M.1
  • 17
    • 0032102873 scopus 로고    scopus 로고
    • Purification and characterization of pancreatic elastase from North Atlantic salmon (Salmo salar)
    • Berglund, G.I., Smal s, A.O., Outzen, H. & Willassen, N.P., Purification and characterization of pancreatic elastase from North Atlantic salmon (Salmo salar). Molec. Marine Bio. and Biotech., 1998. 7: p. 105-114.
    • (1998) Molec. Marine Bio. and Biotech. , vol.7 , pp. 105-114
    • Berglund, G.I.1    Smal S, A.O.2    Outzen, H.3    Willassen, N.P.4
  • 18
    • 0027194992 scopus 로고
    • Properties of elastase from Atlantic cod, a cold-adapted proteinase
    • Asgeirsson, B., & Bjarnason, J.B, Properties of elastase from Atlantic cod, a cold-adapted proteinase. Biochem. Biophys. Acta., 1993. 1164: p. 91-100.
    • (1993) Biochem. Biophys. Acta. , vol.1164 , pp. 91-100
    • Asgeirsson, B.1    Bjarnason, J.B.2
  • 19
    • 0026567107 scopus 로고
    • Purification and characterization of two chymotrypsin-like proteases from the pyloric caeca of rainbow trout (Oncorhynchus mykiss)
    • Kristjansson, M.M. & Nielsen, H., Purification and characterization of two chymotrypsin-like proteases from the pyloric caeca of rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol., 1992. 101B: p. 247-253.
    • (1992) Comp. Biochem. Physiol. , vol.101 B , pp. 247-253
    • Kristjansson, M.M.1    Nielsen, H.2
  • 20
    • 0025761645 scopus 로고
    • Structural and kinetic properties of chymotrypsin from atlantic cod (Gadus morhua). Comparison with bovine chymotrypsin
    • Asgeirsson, B. & Bjarnason, J.B., Structural and kinetic properties of chymotrypsin from atlantic cod (Gadus morhua). Comparison with bovine chymotrypsin. Comp. Biochem. Physiol., 1991. 99B: p. 327-335.
    • (1991) Comp. Biochem. Physiol. , vol.99 B , pp. 327-335
    • Asgeirsson, B.1    Bjarnason, J.B.2
  • 21
    • 0031415284 scopus 로고    scopus 로고
    • Subtilisin from psychrophilic antarctic bacteria: Characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold
    • Narinx, E., Baise, E. & Gerday, C., Subtilisin from psychrophilic antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng., 1997. 10: p. 1271-1279.
    • (1997) Protein Eng. , vol.10 , pp. 1271-1279
    • Narinx, E.1    Baise, E.2    Gerday, C.3
  • 22
    • 0028289989 scopus 로고
    • Stability and structural analyses of ±-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
    • Feller, G., Payan, F., Theys, F., Qian, M. & Gerday, C., Stability and structural analyses of ±-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Eur. J. Biochem., 1994. 222: p. 441-447.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 441-447
    • Feller, G.1    Payan, F.2    Theys, F.3    Qian, M.4    Gerday, C.5
  • 23
    • 0028873872 scopus 로고
    • Alkaline phosphatase from Atlantic cod (Gadus morhua). Kinetic and structural properties which indicate adaptation to low temperatures
    • Asgeirsson, B., Hartemink, R., & Chlebowski, J.F. Alkaline phosphatase from Atlantic cod (Gadus morhua). Kinetic and structural properties which indicate adaptation to low temperatures. Comp. Biochem. Physiol., 1995. 110B: p. 315-329.
    • (1995) Comp. Biochem. Physiol. , vol.110 B , pp. 315-329
    • Asgeirsson, B.1    Hartemink, R.2    Chlebowski, J.F.3
  • 24
    • 0031052268 scopus 로고    scopus 로고
    • Enzymes from cold-adapted microorganisms. The class C″-lactamase from the antarctic psychrophile Psychrobacter immobilis A5
    • Feller, G., Zekhnini, Z., Lamotte-Brausseur, J., & Gerday, C. Enzymes from cold-adapted microorganisms. The class C″-lactamase from the antarctic psychrophile Psychrobacter immobilis A5. Eur. J. Biochem., 1997. 244: p. 186-191.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 186-191
    • Feller, G.1    Zekhnini, Z.2    Lamotte-Brausseur, J.3    Gerday, C.4
  • 25
    • 0032103265 scopus 로고    scopus 로고
    • Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123
    • Tsigos, I., Velonia, K., Smonou, I. & Bouriotis, V., Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123. Eur. J. Biochem., 1998. 254: p. 356-362.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 356-362
    • Tsigos, I.1    Velonia, K.2    Smonou, I.3    Bouriotis, V.4
  • 26
    • 0033597205 scopus 로고    scopus 로고
    • Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillum arcticum
    • Kim, S.-Y., Hwang, KY., Kim, S-H., Sung, H-C., Han, YS., & Cho, Y., Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillum arcticum. J. of Biol. Chem, 1999. 274: p. 11761-11767.
    • (1999) J. of 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.6
  • 28
    • 0022651240 scopus 로고
    • Activation of pancreatic zymogens. Normal activation, premature intrapancreatic activation, protective mechanisms against innappropiate activation
    • Rinderknecht, H., Activation of Pancreatic Zymogens. Normal Activation, Premature Intrapancreatic Activation, Protective Mechanisms against Innappropiate Activation. Digestive Disease and Sciences, 1986. 31: p. 314-321.
    • (1986) Digestive Disease and Sciences , vol.31 , pp. 314-321
    • Rinderknecht, H.1
  • 29
    • 0000618105 scopus 로고
    • Trypsin from the antarctic fish (Paranotothenia magellanica forster) as compared with trout (Salmo gairdneri) trypsin
    • Genicot, S., Feller, G. & Gerday, C., Trypsin from the antarctic fish (Paranotothenia magellanica forster) as compared with trout (Salmo gairdneri) trypsin. Comp. Biochem. Physiol., 1988. 90B: p. 601-609.
    • (1988) Comp. Biochem. Physiol. , vol.90 B , pp. 601-609
    • Genicot, S.1    Feller, G.2    Gerday, C.3
  • 30
    • 0024638262 scopus 로고
    • Purification and characterization of trypsin from the poikilotherm Gadus morhua
    • Asgeirsson, B., Fox, J.W., & Bjarnason, J. B., Purification and characterization of trypsin from the poikilotherm Gadus morhua. Eur. J. Biochem., 1989. 180: p. 85-94.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 85-94
    • Asgeirsson, B.1    Fox, J.W.2    Bjarnason, J.B.3
  • 32
    • 0030865449 scopus 로고    scopus 로고
    • Characterization of a DNA polymerase from uncultivated psychrophilic Archaeon Cenarchaeum symbiosum
    • Schleper, C., Swanson, R.V., Mathur, E.J., & DeLong, E.F., Characterization of a DNA polymerase from uncultivated psychrophilic Archaeon Cenarchaeum symbiosum. J. of Bacteriology, 1997. 179: p. 7802-7811.
    • (1997) J. of Bacteriology , vol.179 , pp. 7802-7811
    • Schleper, C.1    Swanson, R.V.2    Mathur, E.J.3    Delong, E.F.4
  • 33
    • 0033574176 scopus 로고    scopus 로고
    • Characterization of psychrophilic alanine racemose from Bacillus psychrosaccharolyticuc
    • Okubo, Y., Yokoigawa, K., Esaki, N., Soda, K., & Kawai, H., Characterization of psychrophilic alanine racemose from Bacillus psychrosaccharolyticuc. Biochem. and Biophys. Res. Comm., 1999. 256: p. 333-340.
    • (1999) Biochem. and Biophys. Res. Comm. , vol.256 , pp. 333-340
    • Okubo, Y.1    Yokoigawa, K.2    Esaki, N.3    Soda, K.4    Kawai, H.5
  • 34
    • 0031406893 scopus 로고    scopus 로고
    • Enzymes in Antarctic Fish: Glucose-6-phospate dehydrogenase and glutamate dehydrogenase
    • Ciardiello, M.A., Camardella, L., Carrotore, V. & de Frisco, G., Enzymes in Antarctic Fish: Glucose-6-phospate dehydrogenase and glutamate dehydrogenase. Comp. Biochem. Physiol., 1997. 118A: p. 1031-1036.
    • (1997) Comp. Biochem. Physiol. , vol.118 A , pp. 1031-1036
    • Ciardiello, M.A.1    Camardella, L.2    Carrotore, V.3    De Frisco, G.4
  • 35
    • 0033612211 scopus 로고    scopus 로고
    • Interscaffolding additivity: Binding of Pl variants of bovine pancreatic trypsin inhibitor to four serine proteinases
    • Krowarsch, D., Dadlez, M., Buczek, O., Krokoszynska, I., Smal s, A.O. & Otlewski, J., Interscaffolding additivity: Binding of Pl variants of bovine pancreatic trypsin inhibitor to four serine proteinases. J. Mol. Biol., 1999. 289: p. 175-186.
    • (1999) J. Mol. Biol. , vol.289 , pp. 175-186
    • Krowarsch, D.1    Dadlez, M.2    Buczek, O.3    Krokoszynska, I.4    Smal S, A.O.5    Otlewski, J.6
  • 36
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of cold-active synthase from an Antarctic bacterium
    • Russel, R., Gerike, U, Danson, MJ, Hough, DW. & Taylor GL, Structural adaptations of cold-active synthase from an Antarctic bacterium. Structure, 1998. 6: p. 351-361.
    • (1998) Structure , vol.6 , pp. 351-361
    • Russel, R.1    Gerike, U.2    Danson, M.J.3    Hough, D.W.4    Taylor, G.L.5
  • 37
    • 0029085197 scopus 로고
    • A thermolabile triosephosphate isomerase from the psychrophile Vibrio sp. strain ANT-300
    • Adler, E. & Knowles, J., A thermolabile triosephosphate isomerase from the psychrophile Vibrio sp. strain ANT-300. Arch Biochem Biophys, 1995. 321(1): p. 137-9.
    • (1995) Arch Biochem Biophys , vol.321 , Issue.1 , pp. 137-139
    • Adler, E.1    Knowles, J.2
  • 38
    • 0024352698 scopus 로고
    • Purification and Characterization of Chymotrypsin, Trypsin and Elastase like Proteinases from Cod (Gadus morhua l.)
    • Raae, A.J. & Walther, B.T., Purification and Characterization of Chymotrypsin, Trypsin and Elastase like Proteinases from Cod (Gadus morhua l.). Comp. Biochem. Pysiol., 1989. 93B: p. 317-324.
    • (1989) Comp. Biochem. Pysiol. , vol.93 B , pp. 317-324
    • Raae, A.J.1    Walther, B.T.2
  • 39
    • 0024991717 scopus 로고
    • Effect of low and high temperatures on chymotrypsin from Atlantic cod (Gadus morhua L.); Comparison with bovine α-Chymotrypsin
    • Raae, A.J., Effect of low and high temperatures on chymotrypsin from Atlantic cod (Gadus morhua L.); Comparison with bovine α-Chymotrypsin. Comp. Biochem. Physiol., 1990. 97B: p. 145-149.
    • (1990) Comp. Biochem. Physiol. , vol.97 B , pp. 145-149
    • Raae, A.J.1
  • 40
    • 0031888333 scopus 로고    scopus 로고
    • Structure and proposed amino-acid sequence of a pepsin from Atlantic cod (Gadus morhua)
    • Karlsen, S., Hough, E. & Olsen, R., Structure and proposed amino-acid sequence of a pepsin from Atlantic cod (Gadus morhua). Acta Cryst., 1998. D54: p. 32-46.
    • (1998) Acta Cryst. , vol.D54 , pp. 32-46
    • Karlsen, S.1    Hough, E.2    Olsen, R.3
  • 41
    • 0029187318 scopus 로고
    • Structure of native pancreatic elastase from North Atlantic salmon at 1.61 Å resolution
    • Berglund, G.I., Willassen, N.P., Horvik, A. & Smal s, A.O. Structure of native pancreatic elastase from North Atlantic salmon at 1.61 Å resolution. Acta Cryst, 1995. D51: p. 925-937.
    • (1995) Acta Cryst , vol.D51 , pp. 925-937
    • Berglund, G.I.1    Willassen, N.P.2    Horvik, A.3    Smal S, A.O.4
  • 42
    • 0000528385 scopus 로고
    • Structure Determination and Refinement of Benzamidine-Inhibited Trypsin from the North Atlantic Salmon (Salmo salar) at 1.82 Å Resolution
    • Smal s, A.O. & Hordvik, A., Structure Determination and Refinement of Benzamidine-Inhibited Trypsin from the North Atlantic Salmon (Salmo salar) at 1.82 Å Resolution. Acta Cryst., 1993. D49: p. 318-330.
    • (1993) Acta Cryst. , vol.D49 , pp. 318-330
    • Smal S, A.O.1    Hordvik, A.2
  • 43
    • 0031910806 scopus 로고    scopus 로고
    • Crystal structures of the psychrophilic ±-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
    • Aghajari, N., Feller, G., Gerday, C., &. Haser, R., Crystal structures of the psychrophilic ±-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci, 1998. 7(3): p. 564-72.
    • (1998) Protein Sci , vol.7 , Issue.3 , pp. 564-572
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 44
    • 0030696497 scopus 로고    scopus 로고
    • Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa
    • Villeret, V., Chessa, J.P., Gerday, C. &. Van Beeumen, J., Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa. Protein Sci, 1997. 6(11): p. 2462-4.
    • (1997) Protein Sci , vol.6 , Issue.11 , pp. 2462-2464
    • Villeret, V.1    Chessa, J.P.2    Gerday, C.3    Van Beeumen, J.4
  • 45
    • 0028033122 scopus 로고
    • Cold adaption of enzymes: Structural comparison between salmon and bovine trypsins
    • Smal s, A.O., Heimstad, E.S., Hordvik, A., Willassen, N.P. & Male, R., Cold adaption of enzymes: structural comparison between salmon and bovine trypsins. Proteins, 1994. 20(2): p. 149-66.
    • (1994) Proteins , vol.20 , Issue.2 , pp. 149-166
    • Smal S, A.O.1    Heimstad, E.S.2    Hordvik, A.3    Willassen, N.P.4    Male, R.5
  • 46
    • 0032167924 scopus 로고    scopus 로고
    • Structure of a Non-psychrophilic Trypsin from a Cold-Adpted Fish Species
    • Schrøder, H.-K., Willassen, N.P. & Smal s, A.O., Structure of a Non-psychrophilic Trypsin from a Cold-Adpted Fish Species. Acta Cryst, 1998. D54: p. 780-798.
    • (1998) Acta Cryst , vol.D54 , pp. 780-798
    • Schrøder, H.-K.1    Willassen, N.P.2    Smal S, A.O.3
  • 48
    • 0029042854 scopus 로고
    • Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution
    • Heimstad, E.S., Hansen, L.K. & Smal s, A.O., Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution. Protein Eng, 1995. 8(4): p. 379-88.
    • (1995) Protein Eng , vol.8 , Issue.4 , pp. 379-388
    • Heimstad, E.S.1    Hansen, L.K.2    Smal S, A.O.3
  • 49
    • 0031698348 scopus 로고    scopus 로고
    • The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor
    • Submitted
    • Helland, R., Leiros, I., Willassen, N.P., Berglund, G.I. & Smal s, A.O., The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Submitted to Eur J Mol., 1999. 256, p. 317-324.
    • (1999) Eur J Mol. , vol.256 , pp. 317-324
    • Helland, R.1    Leiros, I.2    Willassen, N.P.3    Berglund, G.I.4    Smal S, A.O.5
  • 50
    • 0032923399 scopus 로고    scopus 로고
    • High resolution crystal structures of three new trypsin-squash inhibitor complexes: A detailed comparison with other trypsins and their complexes
    • Helland, R., Berglund, G.I., Otlewski, J., Apostoluk, W., Andersen, O.A., Willassen, N.P. & Smal s, A.O., High resolution crystal structures of three new trypsin-squash inhibitor complexes: a detailed comparison with other trypsins and their complexes. Acta Cryst., 1999. D55: p. 138-148.
    • (1999) Acta Cryst. , vol.D55 , pp. 138-148
    • Helland, R.1    Berglund, G.I.2    Otlewski, J.3    Apostoluk, W.4    Andersen, O.A.5    Willassen, N.P.6    Smal S, A.O.7
  • 53
    • 0005492283 scopus 로고    scopus 로고
    • Structural comparison of psychrophilic and mesophilic trypsins: Elucidating the molecular basis of cold-adaptation
    • Leiros, H.-K.S., Willassen, N.P. & Smal s, A.O., Structural comparison of psychrophilic and mesophilic trypsins: elucidating the molecular basis of cold-adaptation. Eniop. J. Biochem., 2000. 267: p. 1039-1049.
    • (2000) Eniop. J. Biochem. , vol.267 , pp. 1039-1049
    • Leiros, H.-K.S.1    Willassen, N.P.2    Smal S, A.O.3
  • 54
    • 0030924747 scopus 로고    scopus 로고
    • Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta
    • Aittaleb, M., Hubner, R., Lamotte-Brasseur, J. & Gerday, C., Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta. Protein Eng, 1997. 10(5): p. 475-7.
    • (1997) Protein Eng , vol.10 , Issue.5 , pp. 475-477
    • Aittaleb, M.1    Hubner, R.2    Lamotte-Brasseur, J.3    Gerday, C.4
  • 55
    • 0029138559 scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of native elastase from North Atlantic salmon (Salmo salar)
    • Berglund, G., Smal s, A.O. Hansen, L.K. & Willassen, N.P., Crystallization and preliminary X-ray crystallographic studies of native elastase from North Atlantic salmon (Salmo salar). Acta Cryst, 1995. D51: p. 393-394.
    • (1995) Acta Cryst , vol.D51 , pp. 393-394
    • Berglund, G.1    Smal S, A.O.2    Hansen, L.K.3    Willassen, N.P.4
  • 56
    • 0030789078 scopus 로고    scopus 로고
    • Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R
    • Gerike, U., Danson, M.J., Russell, N.J. & Hough, D.W., Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R. Eur J Biochem, 1997. 248(1): p. 49-57.
    • (1997) Eur J Biochem , vol.248 , Issue.1 , pp. 49-57
    • Gerike, U.1    Danson, M.J.2    Russell, N.J.3    Hough, D.W.4
  • 57
    • 0027397742 scopus 로고
    • Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences
    • Rentier-Delrue, F., Mande, S.C., Moyens, S., Terpstra, P., Mainfroid, V., Goraj, K., Lion, M., Hol, W.G. & Martial, J.A., Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences. J Mol Biol, 1993. 229(1): p. 85-93.
    • (1993) J Mol Biol , vol.229 , Issue.1 , pp. 85-93
    • Rentier-Delrue, F.1    Mande, S.C.2    Moyens, S.3    Terpstra, P.4    Mainfroid, V.5    Goraj, K.6    Lion, M.7    Hol, W.G.8    Martial, J.A.9
  • 58
    • 0342981073 scopus 로고    scopus 로고
    • Molecular adaptation to cold of an Antarctic bacterial lipase
    • Arpigny, J.L., Lamotte, J. & Gerday, C., Molecular adaptation to cold of an Antarctic bacterial lipase. J. Mol. Cat., 1997. B3: p. 29-35.
    • (1997) J. Mol. Cat. , vol.B3 , pp. 29-35
    • Arpigny, J.L.1    Lamotte, J.2    Gerday, C.3
  • 59
    • 0344549848 scopus 로고    scopus 로고
    • Residue determinants and sequence analysis of cold-adapted trypsins
    • Leiros, H.-K.S., Willassen, N.P. & Smal s, A.O., Residue determinants and sequence analysis of cold-adapted trypsins. Extremophilies, 1999. 3: p. 205-219.
    • (1999) Extremophilies , vol.3 , pp. 205-219
    • Leiros, H.-K.S.1    Willassen, N.P.2    Smal S, A.O.3
  • 61
    • 0015783856 scopus 로고
    • Determination of Amino Acid Sequence of Porcine Trypsin by Sequenator
    • Hermodson, M.A., Ericsson, L.H., Neurath, H. & Walsh, K.A., Determination of Amino Acid Sequence of Porcine Trypsin by Sequenator. Biochemistry, 1973. 12: p. 3146-3153.
    • (1973) Biochemistry , vol.12 , pp. 3146-3153
    • Hermodson, M.A.1    Ericsson, L.H.2    Neurath, H.3    Walsh, K.A.4
  • 62
    • 0014013139 scopus 로고
    • Covalent structure of bovine trypsinogen. The position of remaining amides
    • Mikes, O., Holeysovsky, V., Tomasek, V. & Sorm, F., Covalent structure of bovine trypsinogen. The position of remaining amides. Biochem. Biophys. Res. Commun., 1966. 24: p. 346-352.
    • (1966) Biochem. Biophys. Res. Commun. , vol.24 , pp. 346-352
    • Mikes, O.1    Holeysovsky, V.2    Tomasek, V.3    Sorm, F.4
  • 63
    • 0020484805 scopus 로고
    • Primary structure of two distinct rat pancreatic preproelas tases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences
    • MacDonald, R.J., Swift, G.H., Quinto, C., Swain, W., Pictet, R.L., Nikovits, W. & Rutter, W.J., Primary structure of two distinct rat pancreatic preproelas tases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences. Biochemistry, 1982. 21(6): p. 1453-63.
    • (1982) Biochemistry , vol.21 , Issue.6 , pp. 1453-1463
    • MacDonald, R.J.1    Swift, G.H.2    Quinto, C.3    Swain, W.4    Pictet, R.L.5    Nikovits, W.6    Rutter, W.J.7
  • 64
    • 0023199150 scopus 로고
    • Isolation and Characterization of a cDNA Encoding Rat Cationic Trypsinogen
    • Fletcher, T.S., Alhadeff, M., Craik, C. S. & Largman, C., Isolation and Characterization of a cDNA Encoding Rat Cationic Trypsinogen. Biochemistry, 1987. 26: p. 3081-3086.
    • (1987) Biochemistry , vol.26 , pp. 3081-3086
    • Fletcher, T.S.1    Alhadeff, M.2    Craik, C.S.3    Largman, C.4
  • 65
    • 0026580541 scopus 로고
    • Identification of cDNAs encoding two novel rat pancreatic serine proteases
    • Kang, J., Wiegand, U. & Muller-Hill, B., Identification of cDNAs encoding two novel rat pancreatic serine proteases. Gene, 1992. 110(2): p. 181-7.
    • (1992) Gene , vol.110 , Issue.2 , pp. 181-187
    • Kang, J.1    Wiegand, U.2    Muller-Hill, B.3
  • 66
    • 0021817726 scopus 로고
    • Differential regulation of trypsinogen mRNA translation: Full-lenght mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas
    • Pinsky, S.D., LaForge, K.S. & Scheele, G., Differential regulation of trypsinogen mRNA translation: Full-lenght mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas. Mol. Cell. Biol., 1985. 5: p. 2669-2676.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2669-2676
    • Pinsky, S.D.1    Laforge, K.S.2    Scheele, G.3
  • 67
    • 0022545173 scopus 로고
    • Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens
    • Emi, M., Nakamura, Y., Ogawa, M., Yamamoto, T., Nishide, T. & Matsubara, K., Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens. Gene, 1986. 41: p. 305-310.
    • (1986) Gene , vol.41 , pp. 305-310
    • Emi, M.1    Nakamura, Y.2    Ogawa, M.3    Yamamoto, T.4    Nishide, T.5    Matsubara, K.6
  • 68
    • 0025288981 scopus 로고
    • Nucleotide sequence of the human pancreatic trypsinogen III cDNA
    • Tani, T., Kawashima, I., Mita, K. & Takiguchi, Y., Nucleotide sequence of the human pancreatic trypsinogen III cDNA. Nucleic Acids Res., 1990. 18: p. 1631.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1631
    • Tani, T.1    Kawashima, I.2    Mita, K.3    Takiguchi, Y.4
  • 69
    • 0025009050 scopus 로고
    • Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity within the trypsin family
    • Le Huerou, I., Wicker, C., Guilloteau, P., Toullec, R. & Puigserver, A., Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity within the trypsin family. Eur. J. Biochem., 1990. 193: p. 767-773.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 767-773
    • Le Huerou, I.1    Wicker, C.2    Guilloteau, P.3    Toullec, R.4    Puigserver, A.5
  • 70
    • 0023047215 scopus 로고
    • Sequence organisation and transcriptional regulation of the mouse elastase II and trypsin genes
    • Stevenson, B.J., Hagenbuchle, O. & Wellauer, P.K., Sequence organisation and transcriptional regulation of the mouse elastase II and trypsin genes. Nucleic Acids Res, 1986. 14(21): p. 8307-30.
    • (1986) Nucleic Acids Res , vol.14 , Issue.21 , pp. 8307-8330
    • Stevenson, B.J.1    Hagenbuchle, O.2    Wellauer, P.K.3
  • 71
    • 33544462674 scopus 로고
    • Isolation and characterization of the chicken trypsinogen gene family
    • Wang, K., Gan, L., Lee, I. & Hood, L., Isolation and characterization of the chicken trypsinogen gene family. Protein Eng., 1995. 10: p. 665-672.
    • (1995) Protein Eng. , vol.10 , pp. 665-672
    • Wang, K.1    Gan, L.2    Lee, I.3    Hood, L.4
  • 72
    • 0025195638 scopus 로고
    • Developmenal and thyroid hormone-dependent regulation of pancreatic genes in Xenopus laevis
    • Shi, Y.B. & Brown, D.D., Developmenal and thyroid hormone-dependent regulation of pancreatic genes in Xenopus laevis. Genes Dev., 1990. 4: p. 1107-1113.
    • (1990) Genes Dev. , vol.4 , pp. 1107-1113
    • Shi, Y.B.1    Brown, D.D.2
  • 74
    • 0031453045 scopus 로고    scopus 로고
    • The molecular evolution of vertebrate trypsinogenes
    • Roach, J.C., Wang, K., Gan, L. & Hood, L., The molecular evolution of vertebrate trypsinogenes. J. Mol. Evol., 1997. 45: p. 640-652.
    • (1997) J. Mol. Evol. , vol.45 , pp. 640-652
    • Roach, J.C.1    Wang, K.2    Gan, L.3    Hood, L.4
  • 77
    • 0027368995 scopus 로고
    • A tight cluster of five unrelated human genes on chromosome 16q22.1
    • Larsen, F., Solheim, J., Kristensen, T., Kolsto, A.B. and Prydz, H., A tight cluster of five unrelated human genes on chromosome 16q22.1. Hum Mol Genet, 1993. 2(10): p. 1589-95.
    • (1993) Hum Mol Genet , vol.2 , Issue.10 , pp. 1589-1595
    • Larsen, F.1    Solheim, J.2    Kristensen, T.3    Kolsto, A.B.4    Prydz, H.5
  • 78
    • 0013958696 scopus 로고
    • Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen a
    • Brown, J.R. & Hartley, B.S., Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A. Biochem J, 1966. 101(1): p. 214-28.
    • (1966) Biochem J , vol.101 , Issue.1 , pp. 214-228
    • Brown, J.R.1    Hartley, B.S.2
  • 79
    • 0014431863 scopus 로고
    • Structure of chymotrypsinogen B compared with chymotrypsinogen a and trypsinogen
    • Smillie, L.B., Furka, A., Nagabhushan, N., Stevenson, K.J. & Parkes, C.O., Structure of chymotrypsinogen B compared with chymotrypsinogen A and trypsinogen. Nature, 1968. 218(139): p. 343-6.
    • (1968) Nature , vol.218 , Issue.139 , pp. 343-346
    • Smillie, L.B.1    Furka, A.2    Nagabhushan, N.3    Stevenson, K.J.4    Parkes, C.O.5
  • 80
    • 0021013478 scopus 로고
    • Identification of cDNA clones encoding secretory isoenzyme forms: Sequence determination of canine pancreatic prechymotrypsinogen 2 mRNA
    • Pinsky, S.D., LaForge, K.S., Luc, V. & Scheele, G., Identification of cDNA clones encoding secretory isoenzyme forms: sequence determination of canine pancreatic prechymotrypsinogen 2 mRNA. Proc Natl Acad Sci USA, 1983. 80(24): p. 7486-90.
    • (1983) Proc Natl Acad Sci USA , vol.80 , Issue.24 , pp. 7486-7490
    • Pinsky, S.D.1    Laforge, K.S.2    Luc, V.3    Scheele, G.4
  • 83
    • 0023105553 scopus 로고
    • Characterization of pancreatic elastase II cDNAs: Two elastase II mRNAs are expressed in human pancreas
    • Kawashima, I., Tani, T., Shimoda, K. & Takiguchi, Y., Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas. Dna, 1987. 6(2): p. 163-72.
    • (1987) Dna , vol.6 , Issue.2 , pp. 163-172
    • Kawashima, I.1    Tani, T.2    Shimoda, K.3    Takiguchi, Y.4
  • 85
    • 0023855495 scopus 로고
    • Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic gene cloning
    • Tani, T., Ohsumi, J., Mita, K., & Takiguchi, Y., Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic gene cloning. J Biol Chem, 1988. 263(3): p. 1231-9.
    • (1988) J Biol Chem , vol.263 , Issue.3 , pp. 1231-1239
    • Tani, T.1    Ohsumi, J.2    Mita, K.3    Takiguchi, Y.4
  • 86
    • 0022728916 scopus 로고
    • Isolation and expression in Escherichia coll of a cDNA clone encoding porcine pancreatic elastase
    • Shirasu, Y., Yoshida, H., Mikayama, T., Matsuki, S., Tanaka, J., & Ikenaga, H., Isolation and expression in Escherichia coll of a cDNA clone encoding porcine pancreatic elastase. J Biochem (Tokyo), 1986. 99(6): p. 1707-12.
    • (1986) J Biochem (Tokyo) , vol.99 , Issue.6 , pp. 1707-1712
    • Shirasu, Y.1    Yoshida, H.2    Mikayama, T.3    Matsuki, S.4    Tanaka, J.5    Ikenaga, H.6
  • 88
    • 0025948934 scopus 로고
    • Development-dependent expression of isozymogens of monkey pepsinogens and structural differences between them
    • Kageyama, T., Tanabe, K. & Koiwai, O., Development-dependent expression of isozymogens of monkey pepsinogens and structural differences between them. Eur J Biochem, 1991. 202(1): p. 205-15.
    • (1991) Eur J Biochem , vol.202 , Issue.1 , pp. 205-215
    • Kageyama, T.1    Tanabe, K.2    Koiwai, O.3
  • 91
    • 0023914848 scopus 로고
    • Nucleotide sequence and expression in Escherichia coli ofcDNA of swine pepsinogen: Involvement of the amino-terminal portion of the activation peptide segment in restoration of the functional protein
    • Tsukagoshi, N., Ando, Y., Tomita, Y., Uchida, R., Takemura, T., Sasaki, T., Yamagata, H., Udaka, S., Ichihara, Y., Takahashi, K., Nucleotide sequence and expression in Escherichia coli ofcDNA of swine pepsinogen: involvement of the amino-terminal portion of the activation peptide segment in restoration of the functional protein. Gene, 1988. 65(2): p. 285-92.
    • (1988) Gene , vol.65 , Issue.2 , pp. 285-292
    • Tsukagoshi, N.1    Ando, Y.2    Tomita, Y.3    Uchida, R.4    Takemura, T.5    Sasaki, T.6    Yamagata, H.7    Udaka, S.8    Ichihara, Y.9    Takahashi, K.10
  • 92
    • 0025064552 scopus 로고
    • Structure and development of rabbit pepsinogens. Stage-specific zymogens, nucleotide sequences of cDNAs, molecular evolution, and gene expression during development
    • Kageyama, T., Tanabe, K. & Koiwai, O., Structure and development of rabbit pepsinogens. Stage-specific zymogens, nucleotide sequences of cDNAs, molecular evolution, and gene expression during development. J Biol Chem, 1990. 265(28): p. 17031-8.
    • (1990) J Biol Chem , vol.265 , Issue.28 , pp. 17031-17038
    • Kageyama, T.1    Tanabe, K.2    Koiwai, O.3
  • 93
    • 0029682084 scopus 로고    scopus 로고
    • Purification and characterization of turtle pepsinogen and pepsin
    • Hirasawa, A., Athauda, S.B. & Takahashi, K., Purification and characterization of turtle pepsinogen and pepsin. J Biochem (Tokyo), 1996. 120(2): p. 407-14.
    • (1996) J Biochem (Tokyo) , vol.120 , Issue.2 , pp. 407-414
    • Hirasawa, A.1    Athauda, S.B.2    Takahashi, K.3
  • 94
    • 0021106960 scopus 로고
    • Covalent structure of chicken pepsinogen
    • Baudys, M. & Kostka, V., Covalent structure of chicken pepsinogen. Eur J Biochem, 1983. 136(1): p. 89-99.
    • (1983) Eur J Biochem , vol.136 , Issue.1 , pp. 89-99
    • Baudys, M.1    Kostka, V.2
  • 95
    • 0023954680 scopus 로고
    • Molecular cloning and the nucleotide sequence of cDNA for embryonic chicken pepsinogen: Phylogenetic relationship with prochymosin
    • Hayashi, K., Agata, K., Mochii, M., Yasugi, S., Eguchi, G. & Mizuno, T., Molecular cloning and the nucleotide sequence of cDNA for embryonic chicken pepsinogen: phylogenetic relationship with prochymosin. J Biochem (Tokyo), 1988. 103(2): p. 290-6.
    • (1988) J Biochem (Tokyo) , vol.103 , Issue.2 , pp. 290-296
    • Hayashi, K.1    Agata, K.2    Mochii, M.3    Yasugi, S.4    Eguchi, G.5    Mizuno, T.6
  • 96
    • 0025788156 scopus 로고
    • Purification, characterization, and amino acid sequences of pepsinogens and pepsins from the esophageal mucosa of bullfrog (Rana catesbeiana) [published erratum appears in J Biol Chem 1992 Sep 25;267(27):19752]
    • Yakabe, E., Tanji, M., Ichinose, M., Goto, S., Miki, K., Kurokawa, K., Ito, H., Kageyama, T. & Takahashi, K., Purification, characterization, and amino acid sequences of pepsinogens and pepsins from the esophageal mucosa of bullfrog (Rana catesbeiana) [published erratum appears in J Biol Chem 1992 Sep 25;267(27):19752]. J Biol Chem, 1991. 266(33): p. 22436-43.
    • (1991) J Biol Chem , vol.266 , Issue.33 , pp. 22436-22443
    • Yakabe, E.1    Tanji, M.2    Ichinose, M.3    Goto, S.4    Miki, K.5    Kurokawa, K.6    Ito, H.7    Kageyama, T.8    Takahashi, K.9
  • 97
    • 0029742212 scopus 로고    scopus 로고
    • The primary structure of the major pepsinogen from the gastric mucosa of tuna stomach
    • Tanji, M., Yakabe, E., Kageyama, T., & Takahashi, K., The primary structure of the major pepsinogen from the gastric mucosa of tuna stomach. J Biochem (Tokyo), 1996. 120(3): p. 647-56.
    • (1996) J Biochem (Tokyo) , vol.120 , Issue.3 , pp. 647-656
    • Tanji, M.1    Yakabe, E.2    Kageyama, T.3    Takahashi, K.4
  • 99
    • 0027434569 scopus 로고
    • Use of an ordered cosmid library to deduce the genomic organization of Mycobacterium leprae
    • Eiglmeier, K., Honore, N., Woods, S.A., Caudron, B. & Cole, S.T., Use of an ordered cosmid library to deduce the genomic organization of Mycobacterium leprae. Mol Microbiol, 1993. 7(2): p. 197-206.
    • (1993) Mol Microbiol , vol.7 , Issue.2 , pp. 197-206
    • Eiglmeier, K.1    Honore, N.2    Woods, S.A.3    Caudron, B.4    Cole, S.T.5
  • 100
    • 0025773491 scopus 로고
    • Citrate synthase from Mycobacterium smegmatis. Cloning, sequence determination and expression in Escherichia coli
    • David, M., Lubinsky-Mink, S., Ben-Zvi, A., Suissa, M., Ulitzur, S. & Kuhn, J., Citrate synthase from Mycobacterium smegmatis. Cloning, sequence determination and expression in Escherichia coli. Biochem J, 1991. 278(Pt 1): p. 225-34.
    • (1991) Biochem J , vol.278 , Issue.PART 1 , pp. 225-234
    • David, M.1    Lubinsky-Mink, S.2    Ben-Zvi, A.3    Suissa, M.4    Ulitzur, S.5    Kuhn, J.6
  • 101
    • 0029780426 scopus 로고    scopus 로고
    • The gene for gamma-glutamylcysteine synthetase from Thiobacillus ferrooxidans has low homology to its Escherichia coli equivalent and is linked to the gene for citrate synthase
    • Powles, R., Deane, S. & Rawlings, D., The gene for gamma-glutamylcysteine synthetase from Thiobacillus ferrooxidans has low homology to its Escherichia coli equivalent and is linked to the gene for citrate synthase. Microbiology, 1996. 142: p. 2543-2548.
    • (1996) Microbiology , vol.142 , pp. 2543-2548
    • Powles, R.1    Deane, S.2    Rawlings, D.3
  • 102
    • 0027994424 scopus 로고
    • Identification of two distinct Bacillus subtilis citrate synthase genes
    • Jin, S. & Sonenshein, A.L., Identification of two distinct Bacillus subtilis citrate synthase genes. J Bacteriol, 1994. 176(15): p. 4669-79.
    • (1994) J Bacteriol , vol.176 , Issue.15 , pp. 4669-4679
    • Jin, S.1    Sonenshein, A.L.2
  • 103
    • 0031019456 scopus 로고    scopus 로고
    • Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans
    • Cvitkovitch, D.G., Gutierrez, J.A. & Bleiweis, A.S., Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans. J Bacteriol, 1997. 179(3): p. 650-5.
    • (1997) J Bacteriol , vol.179 , Issue.3 , pp. 650-655
    • Cvitkovitch, D.G.1    Gutierrez, J.A.2    Bleiweis, A.S.3
  • 104
    • 0025636490 scopus 로고
    • Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilium. Cloning and sequencing of the gene
    • Sutherland, K.J., Henneke, C.M., Towner, P., Hough, D.W. & Danson, M.J., Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilium. Cloning and sequencing of the gene. Eur J Biochem, 1990. 194(3): p. 839-44.
    • (1990) Eur J Biochem , vol.194 , Issue.3 , pp. 839-844
    • Sutherland, K.J.1    Henneke, C.M.2    Towner, P.3    Hough, D.W.4    Danson, M.J.5
  • 105
    • 0029116222 scopus 로고
    • Citrate synthase from the hyperthermophilic Archaean, Pyrococcus furiosus
    • Muir, J.M., Russell, R.J., Hough, D.W. & Danson, M.J., Citrate synthase from the hyperthermophilic Archaean, Pyrococcus furiosus. Protein Eng, 1995. 8(6): p. 583-92.
    • (1995) Protein Eng , vol.8 , Issue.6 , pp. 583-592
    • Muir, J.M.1    Russell, R.J.2    Hough, D.W.3    Danson, M.J.4
  • 107
    • 0027508357 scopus 로고
    • Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1
    • Ishii, A., Suzuki, M., Sahara, T., Takada, Y., Sasaki, S., & Fukunaga, N., Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1. J Bacteriol, 1993. 175(21): p. 6873-80.
    • (1993) J Bacteriol , vol.175 , Issue.21 , pp. 6873-6880
    • Ishii, A.1    Suzuki, M.2    Sahara, T.3    Takada, Y.4    Sasaki, S.5    Fukunaga, N.6
  • 108
    • 0029967931 scopus 로고    scopus 로고
    • Isocitrate dehydrogenase from Thermus aquaticus YTI: Purification of the enzyme and cloning, sequencing, and expression of the gene
    • Miyazaki, K., Isocitrate dehydrogenase from Thermus aquaticus YTI: purification of the enzyme and cloning, sequencing, and expression of the gene. Appl Environ Microbiol, 1996. 62(12): p. 4627-31.
    • (1996) Appl Environ Microbiol , vol.62 , Issue.12 , pp. 4627-4631
    • Miyazaki, K.1
  • 111
    • 0031032608 scopus 로고    scopus 로고
    • Cloning, sequencing and overexpression of the gene encoding malate dehydrogenase from the deep-sea bacterium Photobacterium species strain SS9
    • Welch, T.J. & Bartlett, D.H., Cloning, sequencing and overexpression of the gene encoding malate dehydrogenase from the deep-sea bacterium Photobacterium species strain SS9. Biochim Biophys Acta, 1997. 1350(1): p. 41-6.
    • (1997) Biochim Biophys Acta , vol.1350 , Issue.1 , pp. 41-46
    • Welch, T.J.1    Bartlett, D.H.2
  • 112
    • 0030013608 scopus 로고    scopus 로고
    • Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene
    • Ohkuma, M., Ohtoko, K., Takada, N., Hamamoto, T., Usami, R., Kudo, T., & Horikoshi, K., Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene. FEMS Microbiol Lett, 1996. 137(2-3): p. 247-52.
    • (1996) FEMS Microbiol Lett , vol.137 , Issue.2-3 , pp. 247-252
    • Ohkuma, M.1    Ohtoko, K.2    Takada, N.3    Hamamoto, T.4    Usami, R.5    Kudo, T.6    Horikoshi, K.7
  • 113
    • 0023664596 scopus 로고
    • Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase
    • McAlister-Henn, L., Blaber, M., Bradshaw, R.A., & Nisco, S.J., Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase. Nucleic Acids Res, 1987. 15(12): p. 4993.
    • (1987) Nucleic Acids Res , vol.15 , Issue.12 , pp. 4993
    • McAlister-Henn, L.1    Blaber, M.2    Bradshaw, R.A.3    Nisco, S.J.4
  • 114
    • 0027506680 scopus 로고
    • Complete sequence of the Salmonella typhimurium gene encoding malate dehydrogenase
    • Lu, C.D. & Abdelal, A.T., Complete sequence of the Salmonella typhimurium gene encoding malate dehydrogenase. Gene, 1993. 123(1): p. 143-4.
    • (1993) Gene , vol.123 , Issue.1 , pp. 143-144
    • Lu, C.D.1    Abdelal, A.T.2
  • 116
    • 0026576411 scopus 로고
    • Nucleotide and derived amino acid sequence of the subtilisin from the antarctic psychrotroph Bacillus TA39
    • Narinx, E., Davail, S., Feller, G. & Gerday, C., Nucleotide and derived amino acid sequence of the subtilisin from the antarctic psychrotroph Bacillus TA39. Biochim Biophys Acta, 1992. 1131(1): p. 111-3.
    • (1992) Biochim Biophys Acta , vol.1131 , Issue.1 , pp. 111-113
    • Narinx, E.1    Davail, S.2    Feller, G.3    Gerday, C.4
  • 117
    • 0026757906 scopus 로고
    • Sequence of the subtilisin-encoding gene from an antarctic psychrotroph Bacillus TA41
    • Davail, S., Feller, G., Narinx, E. & Gerday, C., Sequence of the subtilisin-encoding gene from an antarctic psychrotroph Bacillus TA41. Gene, 1992. 119(1): p. 143-4.
    • (1992) Gene , vol.119 , Issue.1 , pp. 143-144
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 118
    • 0026950259 scopus 로고
    • Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto)
    • Nakamura, T., Yamagata, Y., & Ichishima, E., Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto). Biosci Biotechnol Biochem, 1992. 56(11): p. 1869-71.
    • (1992) Biosci Biotechnol Biochem , vol.56 , Issue.11 , pp. 1869-1871
    • Nakamura, T.1    Yamagata, Y.2    Ichishima, E.3
  • 119
    • 0026501813 scopus 로고
    • Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 Å resolution
    • Betzel, C., Klupsch, S., Papendorf, G., Hastrup, S., Branner, S. &. Wilson, K.S., Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 Å resolution. J Mol Biol, 1992. 223(2): p. 427-45.
    • (1992) J Mol Biol , vol.223 , Issue.2 , pp. 427-445
    • Betzel, C.1    Klupsch, S.2    Papendorf, G.3    Hastrup, S.4    Branner, S.5    Wilson, K.S.6
  • 120
    • 0021127425 scopus 로고
    • Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein
    • Vasantha, N., Thompson, L.D., Rhodes, C., Banner, C., Nagle, J. & Filpula, D., Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein. J Bacteriol, 1984. 159(3): p. 811-9.
    • (1984) J Bacteriol , vol.159 , Issue.3 , pp. 811-819
    • Vasantha, N.1    Thompson, L.D.2    Rhodes, C.3    Banner, C.4    Nagle, J.5    Filpula, D.6
  • 121
    • 0022429781 scopus 로고
    • Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis
    • Jacobs, M., Eliasson, M., Uhlen, M. & Flock, J.I., Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis. Nucleic Acids Res, 1985. 13(24): p. 8913-26.
    • (1985) Nucleic Acids Res , vol.13 , Issue.24 , pp. 8913-8926
    • Jacobs, M.1    Eliasson, M.2    Uhlen, M.3    Flock, J.I.4
  • 123
    • 0030988030 scopus 로고    scopus 로고
    • Gene from tropical Bacillus sphaericus encoding a protease closely related to subtilisins from Antarctic bacilli
    • Wati, M.R., Thanabalu, T. & Porter, A.G., Gene from tropical Bacillus sphaericus encoding a protease closely related to subtilisins from Antarctic bacilli. Biochim Biophys Acta, 1997. 1352(1): p. 56-62.
    • (1997) Biochim Biophys Acta , vol.1352 , Issue.1 , pp. 56-62
    • Wati, M.R.1    Thanabalu, T.2    Porter, A.G.3
  • 124
    • 0026692001 scopus 로고
    • Molecular cloning of a subtilisin J gene from Bacillus stearothermophilus and its expression in Bacillus subtilis
    • Jang, J.S., Kang, D.O., Chun, M.J. & Byun, S.M., Molecular cloning of a subtilisin J gene from Bacillus stearothermophilus and its expression in Bacillus subtilis. Biochem Biophys Res Commun, 1992. 184(1): p. 277-82.
    • (1992) Biochem Biophys Res Commun , vol.184 , Issue.1 , pp. 277-282
    • Jang, J.S.1    Kang, D.O.2    Chun, M.J.3    Byun, S.M.4
  • 125
    • 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., Van Beeumen, J. & Gerday, C., Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23. J Biol Chem, 1992. 267(8): p. 5217-21.
    • (1992) J Biol Chem , vol.267 , Issue.8 , pp. 5217-5221
    • Feller, G.1    Lonhienne, T.2    Deroanne, C.3    Libioulle, C.4    Van Beeumen, J.5    Gerday, C.6
  • 126
    • 0026062181 scopus 로고
    • Cloning, characterization and expression of an α-amylase gene from Streptomyces griseus IMRU3570
    • Vigal, T., Gil, J.A., Daza, A., Garcia-Gonzalez, M.D. & Martin, J.F., Cloning, characterization and expression of an α-amylase gene from Streptomyces griseus IMRU3570. Mol Gen Genet, 1991. 225(2): p. 278-88.
    • (1991) Mol Gen Genet , vol.225 , Issue.2 , pp. 278-288
    • Vigal, T.1    Gil, J.A.2    Daza, A.3    Garcia-Gonzalez, M.D.4    Martin, J.F.5
  • 127
    • 0024270115 scopus 로고
    • Cloning, characterisation and regulation of an α-amylase gene from Streptomyces venezuelae
    • Virolle, M.J., Long, C.M., Chang, S. & Bibb, M.J., Cloning, characterisation and regulation of an α-amylase gene from Streptomyces venezuelae. Gene, 1988. 74(2): p. 321-34.
    • (1988) Gene , vol.74 , Issue.2 , pp. 321-334
    • Virolle, M.J.1    Long, C.M.2    Chang, S.3    Bibb, M.J.4
  • 128
    • 0023549334 scopus 로고
    • Enzyme-coding genes as molecular clocks: The molecular evolution of animal α-amylases
    • Hickey, D.A., Benkel, B.F., Boer, P.H., Genest, Y., Abukashawa, S. & Ben-David, G., Enzyme-coding genes as molecular clocks: the molecular evolution of animal α-amylases. J Mol Evol, 1987. 26(3): p. 252-6.
    • (1987) J Mol Evol , vol.26 , Issue.3 , pp. 252-256
    • Hickey, D.A.1    Benkel, B.F.2    Boer, P.H.3    Genest, Y.4    Abukashawa, S.5    Ben-David, G.6
  • 129
    • 0027315031 scopus 로고
    • Sequence of the Streptomyces thermoviolaceus CUB74 alpha-amylase- encoding gene and its transcription analysis in Streptomyces lividans
    • Bahri, S.M. & Ward, J.M., Sequence of the Streptomyces thermoviolaceus CUB74 alpha-amylase- encoding gene and its transcription analysis in Streptomyces lividans. Gene, 1993. 127(1): p. 133-7.
    • (1993) Gene , vol.127 , Issue.1 , pp. 133-137
    • Bahri, S.M.1    Ward, J.M.2
  • 130
    • 0023040136 scopus 로고
    • Sequence of the Citrobacter freundii OS60 chromosomal ampC β-lactamase gene
    • Lindberg, F. & Normark, S., Sequence of the Citrobacter freundii OS60 chromosomal ampC β-lactamase gene. Eur J Biochem, 1986. 156(3): p. 441-5.
    • (1986) Eur J Biochem , vol.156 , Issue.3 , pp. 441-445
    • Lindberg, F.1    Normark, S.2
  • 131
    • 0000908299 scopus 로고
    • AmpC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type
    • Jaurin, B. & Grundstrom, T., ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type. Proc Natl Acad Sci U S A, 1981. 78(8): p. 4897-901.
    • (1981) Proc Natl Acad Sci U S a , vol.78 , Issue.8 , pp. 4897-4901
    • Jaurin, B.1    Grundstrom, T.2
  • 132
    • 0024287069 scopus 로고
    • Sequence and comparative analysis of three Enterobacter cloacae ampC β-lactamase genes and their products
    • Galleni, M., Lindberg, F., Normark, S., Cole, S., Honore, N., Joris, B. & Frere, J.M., Sequence and comparative analysis of three Enterobacter cloacae ampC β-lactamase genes and their products. Biochem J, 1988. 250(3): p. 753-60.
    • (1988) Biochem J , vol.250 , Issue.3 , pp. 753-760
    • Galleni, M.1    Lindberg, F.2    Normark, S.3    Cole, S.4    Honore, N.5    Joris, B.6    Frere, J.M.7
  • 133
    • 0026625014 scopus 로고
    • Nucleotide sequence of the ampC-ampR region from the chromosome of Yersinia enterocolitica
    • Seoane, A., Francia, M. V., & Garcia Lobo, J.M., Nucleotide sequence of the ampC-ampR region from the chromosome of Yersinia enterocolitica. Antimicrob Agents Chemother, 1992. 36(5): p. 1049-52.
    • (1992) Antimicrob Agents Chemother , vol.36 , Issue.5 , pp. 1049-1052
    • Seoane, A.1    Francia, M.V.2    Garcia Lobo, J.M.3
  • 134
    • 0031105430 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding the AmpC β-lactamase of Morganella morganii
    • Barnaud, G., Arlet, G., Danglot, C. & Philippen, A., Cloning and sequencing of the gene encoding the AmpC β-lactamase of Morganella morganii. FEMS Microbiol Lett, 1997. 148(1): p. 15-20.
    • (1997) FEMS Microbiol Lett , vol.148 , Issue.1 , pp. 15-20
    • Barnaud, G.1    Arlet, G.2    Danglot, C.3    Philippen, A.4
  • 135
    • 0027933363 scopus 로고
    • Cloning and expression of a cloxacillin-hydrolyzing enzyme and a cephalosporinase from Aeromonas sobria AER 14M in Escherichia coli: Requirement for an E. coli chromosomal mutation for efficient expression of the class D enzyme
    • Rasmussen, B. A., Keeney, D., Yang, Y. & Bush, K., Cloning and expression of a cloxacillin-hydrolyzing enzyme and a cephalosporinase from Aeromonas sobria AER 14M in Escherichia coli: requirement for an E. coli chromosomal mutation for efficient expression of the class D enzyme. Antimicrob Agents Chemother, 1994. 38(9): p. 2078-85.
    • (1994) Antimicrob Agents Chemother , vol.38 , Issue.9 , pp. 2078-2085
    • Rasmussen, B.A.1    Keeney, D.2    Yang, Y.3    Bush, K.4
  • 136
    • 0027966926 scopus 로고
    • Gene sequence and biochemical characterization of FOX-1 from Klebsiella pneumoniae, a new AmpC-type plasmid-mediated beta-lactamase with two molecular variants
    • Gonzalez Leiza, M., Perez-Diaz, J.C., Ayala, J., Casellas, J.M., Martinez-Beltran, J., Bush, K. & Baquero, F., Gene sequence and biochemical characterization of FOX-1 from Klebsiella pneumoniae, a new AmpC-type plasmid-mediated beta-lactamase with two molecular variants. Antimicrob Agents Chemother, 1994. 38(9): p. 2150-7.
    • (1994) Antimicrob Agents Chemother , vol.38 , Issue.9 , pp. 2150-2157
    • Gonzalez Leiza, M.1    Perez-Diaz, J.C.2    Ayala, J.3    Casellas, J.M.4    Martinez-Beltran, J.5    Bush, K.6    Baquero, F.7
  • 137
    • 0025600978 scopus 로고
    • Cloning, sequencing and analysis of the structural gene and regulatory region of the Pseudomonas aeruginosa chromosomal ampC beta-lactamase
    • Lodge, J.M., Minchin, S.D., Piddock, L.J., & Busby, J.W., Cloning, sequencing and analysis of the structural gene and regulatory region of the Pseudomonas aeruginosa chromosomal ampC beta-lactamase. Biochem J, 1990. 272(3): p. 627-31.
    • (1990) Biochem J , vol.272 , Issue.3 , pp. 627-631
    • Lodge, J.M.1    Minchin, S.D.2    Piddock, L.J.3    Busby, J.W.4
  • 138
    • 0025468886 scopus 로고
    • Nucleotide sequence of the Serratia marcescens SR50 chromosomal ampC beta-lactamase gene
    • Nomura, K. & Yoshida, T., Nucleotide sequence of the Serratia marcescens SR50 chromosomal ampC beta-lactamase gene. FEMS Microbiol Lett, 1990. 58(3): p. 295-9.
    • (1990) FEMS Microbiol Lett , vol.58 , Issue.3 , pp. 295-299
    • Nomura, K.1    Yoshida, T.2
  • 140
    • 10544255079 scopus 로고    scopus 로고
    • Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae
    • Himmelreich, R., Hubert, H., Plagens, H., Pirkl, E., Li, B.C., & Hermann, R., Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucleic Acids Res, 1996. 24(22): p. 4420-49.
    • (1996) Nucleic Acids Res , vol.24 , Issue.22 , pp. 4420-4449
    • Himmelreich, R.1    Hubert, H.2    Plagens, H.3    Pirkl, E.4    Li, B.C.5    Hermann, R.6
  • 141
    • 0021212892 scopus 로고
    • Nucleotide sequence of the triose phosphate isomerase gene of Escherichia coli
    • Pichersky, E., Gottlieb, L.D., & Hess, J.F., Nucleotide sequence of the triose phosphate isomerase gene of Escherichia coli. Mol Gen Genet, 1984. 195(1-2): p. 314-20.
    • (1984) Mol Gen Genet , vol.195 , Issue.1-2 , pp. 314-320
    • Pichersky, E.1    Gottlieb, L.D.2    Hess, J.F.3
  • 142
    • 0024512267 scopus 로고
    • Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase-coding gene of Corynebacterium glutamicum ATCC13032
    • O'Regan, M., Thierbach, G., Bachmann, B., Villeval, D., Lepage, P., Viret, J.F., & Lemoine, Y., Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase- coding gene of Corynebacterium glutamicum ATCC13032. Gene, 1989. 77(2): p. 237-51.
    • (1989) Gene , vol.77 , Issue.2 , pp. 237-251
    • O'Regan, M.1    Thierbach, G.2    Bachmann, B.3    Villeval, D.4    Lepage, P.5    Viret, J.F.6    Lemoine, Y.7
  • 143
    • 0030798863 scopus 로고    scopus 로고
    • Xanthobacter flavus employs a single triosephosphate isomerase for heterotrophic and autotrophic metabolism
    • Meijer, W.G., de Boer, P., & van Keulen, G., Xanthobacter flavus employs a single triosephosphate isomerase for heterotrophic and autotrophic metabolism. Microbiology, 1997. 143(Pt 6): p. 1925-31.
    • (1997) Microbiology , vol.143 , Issue.PART 6 , pp. 1925-1931
    • Meijer, W.G.1    De Boer, P.2    Van Keulen, G.3
  • 144
    • 0028336824 scopus 로고
    • Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis
    • Leyva-Vazquez, M.A. & Setlow, P., Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. J Bacteriol, 1994.176(13): p. 3903-10.
    • (1994) J Bacteriol , vol.176 , Issue.13 , pp. 3903-3910
    • Leyva-Vazquez, M.A.1    Setlow, P.2
  • 145
    • 0028838946 scopus 로고
    • The Lactococcus lactis triosephosphate isomerase gene, tpi, is monocistronic
    • Cancilla, M.R., Davidson, B.E., Hillier, A.J., Nguyen, N.Y. & Thompson, J., The Lactococcus lactis triosephosphate isomerase gene, tpi, is monocistronic. Microbiology, 1995. 141(Pt 1): p. 229-38.
    • (1995) Microbiology , vol.141 , Issue.PART 1 , pp. 229-238
    • Cancilla, M.R.1    Davidson, B.E.2    Hillier, A.J.3    Nguyen, N.Y.4    Thompson, J.5
  • 146
    • 0030050740 scopus 로고    scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii
    • Anda, P., Gebbia, J.A., Backenson, B.P., Coleman, J.L. and Benach, J.L., A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii. Infect Immun, 1996. 64(1): p. 262-8.
    • (1996) Infect Immun , vol.64 , Issue.1 , pp. 262-268
    • Anda, P.1    Gebbia, J.A.2    Backenson, B.P.3    Coleman, J.L.4    Benach, J.L.5
  • 147
    • 0026469921 scopus 로고
    • Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap operon) from mesophilic Bacillus megaterium: Comparison with corresponding sequences from thermophilic Bacillus stearothermophilus
    • Schlapfer, B.S. & Zuber, H., Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus. Gene, 1992. 122(1): p. 53-62.
    • (1992) Gene , vol.122 , Issue.1 , pp. 53-62
    • Schlapfer, B.S.1    Zuber, H.2
  • 148
    • 0027434228 scopus 로고
    • Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus
    • Rentier-Delrue, R, Moyens, S., Lion, M. & Martial, J.A., Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus. Gene, 1993. 134(1): p. 137-8.
    • (1993) Gene , vol.134 , Issue.1 , pp. 137-138
    • Rentier-Delrue, R.1    Moyens, S.2    Lion, M.3    Martial, J.A.4
  • 149
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A.R., Matouschek, A. & Serrano, L., The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol., 1992. 224: p. 771-82.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 150
    • 2442481562 scopus 로고
    • Stability of the folded conformation
    • Creighton, T.E., Stability of the folded conformation. Curr. Op. Struct. Bio., 1991. 1: p. 5-16.
    • (1991) Curr. Op. Struct. Bio. , vol.1 , pp. 5-16
    • Creighton, T.E.1
  • 153
    • 0028846686 scopus 로고
    • Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isome rases with known three-dimensional structures points to the importance of hydrophobic interactions
    • Delboni, L.F., Mande, S.C., Rentier-Delrue, R, Mainfroid, V., Turley, S., Vellieux, F.M., Martial, J.A., & Hol, W.G., Crystal structure of
    • (1995) Protein Sci , vol.4 , Issue.12 , pp. 2594-2604
    • Delboni, L.F.1    Mande, S.C.2    Rentier-Delrue, R.3    Mainfroid, V.4    Turley, S.5    Vellieux, F.M.6    Martial, J.A.7    Hol, W.G.8
  • 154
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T., & Oshima, T., Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur J Biochem, 1994. 220(1): p. 275-81.
    • (1994) Eur J Biochem , vol.220 , Issue.1 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 155
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interactions
    • Privalov, P.I. & Gill, S. J., Stability of protein structure and hydrophobic interactions. Adv. Prot. Chem., 1988. 39: p. 191-234.
    • (1988) Adv. Prot. Chem. , vol.39 , pp. 191-234
    • Privalov, P.I.1    Gill, S.J.2
  • 156
    • 0029176320 scopus 로고
    • How make my blood boil
    • Goldman, A., How make my blood boil. Structure, 1995. 3: p. 1277-1279.
    • (1995) Structure , vol.3 , pp. 1277-1279
    • Goldman, A.1
  • 157
  • 158
    • 0026566303 scopus 로고
    • The role of packing interactions in stabilizing folded proteins
    • Sneddon, S.F. & Tobias, D.J., The role of packing interactions in stabilizing folded proteins. Biochemistry, 1992. 31(10): p. 2842-6.
    • (1992) Biochemistry , vol.31 , Issue.10 , pp. 2842-2846
    • Sneddon, S.F.1    Tobias, D.J.2
  • 159
    • 0030970741 scopus 로고    scopus 로고
    • Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus
    • Haney, P., Konisky, J., Koretke, K.K., Luthey-Schulten, Z. & Wolynes, P.G., Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus. Proteins, 1997. 28: p. 117-130.
    • (1997) Proteins , vol.28 , pp. 117-130
    • Haney, P.1    Konisky, J.2    Koretke, K.K.3    Luthey-Schulten, Z.4    Wolynes, P.G.5
  • 160
    • 0024384836 scopus 로고
    • Hydrophobic cluster analysis of the primary sequences of alpha-amylases
    • Raimbaud, E., Buleon, A., Perez, S. & Henrissat, B., Hydrophobic cluster analysis of the primary sequences of alpha-amylases. Int J Biol Macromol, 1989. 11(4): p. 217-25.
    • (1989) Int J Biol Macromol , vol.11 , Issue.4 , pp. 217-225
    • Raimbaud, E.1    Buleon, A.2    Perez, S.3    Henrissat, B.4
  • 162
    • 0031279830 scopus 로고    scopus 로고
    • Molecular adaptations of enzymes from psychrophilic organisms
    • Feller, G., Arpigny, J.L., Narix, E. & Gerday, C., Molecular adaptations of enzymes from psychrophilic organisms. Comp. Biochem. Physiol., 1997. A118: p. 495-499.
    • (1997) Comp. Biochem. Physiol. , vol.A118 , pp. 495-499
    • Feller, G.1    Arpigny, J.L.2    Narix, E.3    Gerday, C.4
  • 163
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G., Woell, S., & Argos, P., Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol., 1997. 269: p. 631-643.
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 164
    • 0029115963 scopus 로고
    • The optimization of protein-solvent interactions: Thermostability and role of hydrophobic and electrostatic interactions
    • Spassov, V.Z., Karshikoff, A.D., & Ladenstein, R., The optimization of protein-solvent interactions: Thermostability and role of hydrophobic and electrostatic interactions. Protein Science, 1995. 4: p. 1516-1527.
    • (1995) Protein Science , vol.4 , pp. 1516-1527
    • Spassov, V.Z.1    Karshikoff, A.D.2    Ladenstein, R.3
  • 165
    • 0027476253 scopus 로고
    • Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile
    • Arpigny, J.L., Feller, G. & Gerday, C., Cloning, sequence and structural features of a lipase from the antarctic facultative psychrophile. Biochim. Biophys. Acta, 1993. 1171: p. 331-333.
    • (1993) Biochim. Biophys. Acta , vol.1171 , pp. 331-333
    • Arpigny, J.L.1    Feller, G.2    Gerday, C.3
  • 166
    • 0028277521 scopus 로고
    • Spatial Optimization of electrostatic Interactions between the ionized groups in globular proteins
    • Spassov, V.Z. & Atanasov, B.P., Spatial Optimization of electrostatic Interactions between the ionized groups in globular proteins. Proteins: Structure, Function & Genetics, 1994. 19: p. 222-229.
    • (1994) Proteins: Structure, Function & Genetics , vol.19 , pp. 222-229
    • Spassov, V.Z.1    Atanasov, B.P.2
  • 167
    • 0027246520 scopus 로고
    • Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 Å resolution
    • Ishikawa, K., Okumura, M., Katayanagi, K., Kimura, S., Kanaya, S. & Morikawa, K., Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 Å resolution. J. Mol. Biol., 1993. 230: p. 529-542.
    • (1993) J. Mol. Biol. , vol.230 , pp. 529-542
    • Ishikawa, K.1    Okumura, M.2    Katayanagi, K.3    Kimura, S.4    Kanaya, S.5    Morikawa, K.6
  • 168
    • 0027474760 scopus 로고
    • The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent
    • Davies, G.J., Gamblin, S.J., Littlechild, J.A., & Watson, H.C., The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent. Proteins, 1993. 3: p. 283-289.
    • (1993) Proteins , vol.3 , pp. 283-289
    • Davies, G.J.1    Gamblin, S.J.2    Littlechild, J.A.3    Watson, H.C.4
  • 169
    • 0023036230 scopus 로고    scopus 로고
    • The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability
    • Mitchinson, C. & Baldwin, R.L., The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability. Proteins, 1: p. 23-33.
    • Proteins , vol.1 , pp. 23-33
    • Mitchinson, C.1    Baldwin, R.L.2
  • 170
    • 0029020484 scopus 로고
    • N- and C-capping preferences for all 20 amino acids in α-helical peptides
    • Doig, A.J. & Baldwin, R.L., N- and C-capping preferences for all 20 amino acids in α-helical peptides. Protein Science, 1995. 4: p. 1325-1336.
    • (1995) Protein Science , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 171
    • 0002780655 scopus 로고
    • Secondary structure formation and stability
    • Ptitsyn, O.B., Secondary structure formation and stability. Curr. Op. Struct. Biol., 1992. 2: p. 13-20.
    • (1992) Curr. Op. Struct. Biol. , vol.2 , pp. 13-20
    • Ptitsyn, O.B.1
  • 172
    • 0027998757 scopus 로고
    • Context is a major determinant of β-sheet propensity
    • Minor, D.L. & Kim, P.S., Context is a major determinant of β-sheet propensity. Nature, 1994. 371: p. 264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor, D.L.1    Kim, P.S.2
  • 173
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor, D.L. & Kim, P.S., Measurement of the β-sheet-forming propensities of amino acids. Nature, 1994. 367: p. 660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor, D.L.1    Kim, P.S.2
  • 174
    • 0028988836 scopus 로고
    • Side-chain determinants of β-sheet stability
    • Otzen, D.E., & Fersht, A.R., Side-chain determinants of β-sheet stability. Biochemistry, 1995. 34: p. 5718-5724.
    • (1995) Biochemistry , vol.34 , pp. 5718-5724
    • Otzen, D.E.1    Fersht, A.R.2
  • 175
    • 0030781507 scopus 로고    scopus 로고
    • Insights into thermal resistance of proteins from the intrinsic stability of their alpha-helices
    • Petukhov, M., Kil, Y., Kuramitsu, S., & Lanzov, V., Insights into thermal resistance of proteins from the intrinsic stability of their alpha-helices. Proteins, 1997. 29(3): p. 309-20.
    • (1997) Proteins , vol.29 , Issue.3 , pp. 309-320
    • Petukhov, M.1    Kil, Y.2    Kuramitsu, S.3    Lanzov, V.4
  • 176
    • 0028887397 scopus 로고
    • Structure of anionic salmon trypsin in a second crystal form
    • Berglund, G., Smal s, A., Hordvik, A. & Willassen, N.P., Structure of anionic salmon trypsin in a second crystal form. Acta Cryst, 1995. D51: p. 725-730.
    • (1995) Acta Cryst , vol.D51 , pp. 725-730
    • Berglund, G.1    Smal S, A.2    Hordvik, A.3    Willassen, N.P.4
  • 177
    • 0027462173 scopus 로고
    • Principles of protein stability derived from protein engineering experiments
    • Fersht, A.R. & Serrano, L., Principles of protein stability derived from protein engineering experiments. Curr. Op. Struct. Biol., 1993. 3: p. 75-83.
    • (1993) Curr. Op. Struct. Biol. , vol.3 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 179
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and Applications
    • Sharp, K.A. & Honig, B., Electrostatic interactions in macromolecules: Theory and Applications. Annu. Rev. Biophys. Biophys. Chem., 1990. 19: p. 301-332.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 180
    • 0015901579 scopus 로고
    • The Complex formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. Crystal structure determination and sterechemistry of the Contact Region
    • R hlmann, A., Kukla, D., Schwager, P., Bartels, K., & Huber, R., The Complex formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. Crystal structure determination and sterechemistry of the Contact Region. J. Mol. Biol., 1973. 77: p. 417-436.
    • (1973) J. Mol. Biol. , vol.77 , pp. 417-436
    • R Hlmann, A.1    Kukla, D.2    Schwager, P.3    Bartels, K.4    Huber, R.5
  • 181
    • 0034257240 scopus 로고    scopus 로고
    • Electrostatics of mesophilic and psychrophilic trypsin isoenzymes. Qualitative evaluation of differences at the substrate binding site
    • manuscript in preparation
    • Gorfe, A., A., Brandsdal, B.O., Leiros, H-K., Helland, R.I. & Smal s, A.O., Electrostatics of mesophilic and psychrophilic trypsin isoenzymes. Qualitative evaluation of differences at the substrate binding site. Proteins, 2000, manuscript in preparation.
    • (2000) Proteins
    • Gorfe, A.1    Brandsdal, B.O.2    Leiros, H.-K.3    Helland, R.I.4    Smal S, A.O.5
  • 184
    • 0026319199 scopus 로고
    • Protein folding and association: Insight from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., & Honig, B., Protein folding and association: insight from the interfacial and thermodynamic properties of hydrocarbons. Proteins, Structure, Functions and Genetics, 1991. 11: p. 281-296.
    • (1991) Proteins, Structure, Functions and Genetics , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 185
    • 0025255604 scopus 로고
    • Conformational free energy of armadillo metmyoglobin
    • Kelly, L. & Holladay, L.A., Conformational free energy of armadillo metmyoglobin. Int J Pept Protein Res, 1990. 35(3): p. 235-40.
    • (1990) Int J Pept Protein Res , vol.35 , Issue.3 , pp. 235-240
    • Kelly, L.1    Holladay, L.A.2
  • 186
    • 0025234587 scopus 로고
    • PH-induced denaturation of Proteins: A single salt-bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson, D.E., Becktel, W.J., & Dahlquist, F.W., pH-induced denaturation of Proteins: A single salt-bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry, 1990. 29: p. 2403-2408.
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 187
    • 0028235775 scopus 로고
    • Molecular mechanism of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin
    • Barrick, D., Hughson, F.M. & Baldwin, R.L., Molecular mechanism of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. J. Mol. Biol., 1994. 237: p. 588-601.
    • (1994) J. Mol. Biol. , vol.237 , pp. 588-601
    • Barrick, D.1    Hughson, F.M.2    Baldwin, R.L.3
  • 188
    • 0025044680 scopus 로고
    • Contribution of histidine residues to the conformational stability of ribunuclease T1 and mutant Glu-58 -> Ala
    • McNutt, M., Mullins, L.S., Raushel, F.M. & Pace, C.N., Contribution of histidine residues to the conformational stability of ribunuclease T1 and mutant Glu-58 -> Ala. Biochemistry, 1990. 29: p. 7572-7576.
    • (1990) Biochemistry , vol.29 , pp. 7572-7576
    • McNutt, M.1    Mullins, L.S.2    Raushel, F.M.3    Pace, C.N.4
  • 189
    • 0023726958 scopus 로고
    • Stabilization of protein structure by interaction of α-helix dipole with charged side chain
    • Sali, D., Bycroft, M. & Fersht, A.R., Stabilization of protein structure by interaction of α-helix dipole with charged side chain. Nature, 1988. 335: p. 740-743.
    • (1988) Nature , vol.335 , pp. 740-743
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 190
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to stability
    • Vihnen, M., Relationship of protein flexibility to stability. Protein Engineering, 1987. 1: p. 477-480.
    • (1987) Protein Engineering , vol.1 , pp. 477-480
    • Vihnen, M.1
  • 192
    • 0027441807 scopus 로고
    • Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability
    • Serrano, L., Day, A.G. & Fersht, A.R., Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J. Mol. Biol., 1993. 233: p. 305-312.
    • (1993) J. Mol. Biol. , vol.233 , pp. 305-312
    • Serrano, L.1    Day, A.G.2    Fersht, A.R.3
  • 193
    • 0030961917 scopus 로고    scopus 로고
    • Serine proteinases from cold-adapted organisms
    • Damodaran, Editor. Plenum Press: New York
    • Kristjansson, M.M., sgeirsson, B. & Bjarnason, J.B., Serine proteinases from cold-adapted organisms, in Food Proteins and Lipids, Damodaran, Editor. 1997, Plenum Press: New York. p. 27-46.
    • (1997) Food Proteins and Lipids , pp. 27-46
    • Kristjansson, M.M.1    Sgeirsson, B.2    Bjarnason, J.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.