메뉴 건너뛰기




Volumn 1784, Issue 11, 2008, Pages 1865-1872

Cold adaptation of enzymes: Structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile Colwellia psychrerythraea and of human leukotriene A4 hydrolase

Author keywords

Aminopeptidase; Cold active enzyme; Colwellia psychrerythraea; Leukotriene A4 hydrolase; Psychrophile

Indexed keywords

AMINOPEPTIDASE; GUANIDINE; LEUKOTRIENE A4 HYDROLASE; PROLINE;

EID: 54149091012     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.06.002     Document Type: Article
Times cited : (42)

References (45)
  • 2
    • 0031061411 scopus 로고    scopus 로고
    • Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit for life to 113 degrees C
    • Blochl E., Rachel R., Burggraf S., Hafenbradl D., Jannasch H.W., and Stetter K.O. Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit for life to 113 degrees C. Extremophiles 1 (1997) 14-21
    • (1997) Extremophiles , vol.1 , pp. 14-21
    • Blochl, E.1    Rachel, R.2    Burggraf, S.3    Hafenbradl, D.4    Jannasch, H.W.5    Stetter, K.O.6
  • 3
    • 0042021865 scopus 로고    scopus 로고
    • Extending the upper temperature limit for life
    • Kashefi K., and Lovley D.R. Extending the upper temperature limit for life. Science 301 (2003) 934
    • (2003) Science , vol.301 , pp. 934
    • Kashefi, K.1    Lovley, D.R.2
  • 5
    • 1942535726 scopus 로고    scopus 로고
    • Transcriptional regulation in Archaea
    • Ouhammouch M. Transcriptional regulation in Archaea. Curr. Opin. Genet. Dev. 14 (2004) 133-138
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 133-138
    • Ouhammouch, M.1
  • 6
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
    • Motohashi K., Watanabe Y., Yohda M., and Yoshida M. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 7184-7189
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 7
    • 0023905575 scopus 로고
    • The mechanism of cryoprotection of proteins by solutes
    • Carpenter J.F., and Crowe J.H. The mechanism of cryoprotection of proteins by solutes. Cryobiology 25 (1988) 244-255
    • (1988) Cryobiology , vol.25 , pp. 244-255
    • Carpenter, J.F.1    Crowe, J.H.2
  • 8
    • 0031608378 scopus 로고    scopus 로고
    • Molecular adaptations in psychrophilic bacteria: potential for biotechnological applications
    • Russell N.J. Molecular adaptations in psychrophilic bacteria: potential for biotechnological applications. Adv. Biochem. Eng. Biotechnol. 61 (1998) 1-21
    • (1998) Adv. Biochem. Eng. Biotechnol. , vol.61 , pp. 1-21
    • Russell, N.J.1
  • 9
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P., Kardos J., Svingor, and Petsko G.A. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 7406-74011
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7406-74011
    • Zavodszky, P.1    Kardos, J.2    Svingor3    Petsko, G.A.4
  • 10
    • 0034973280 scopus 로고    scopus 로고
    • Protein function at thermal extremes: balancing stability and flexibility
    • Fields P.A. Protein function at thermal extremes: balancing stability and flexibility. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 129 (2001) 417-431
    • (2001) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 11
    • 0026720247 scopus 로고
    • Crystalline ribonuclease A loses function below the dynamical transition at 220 K
    • Rasmussen B.F., Stock A.M., Ringe D., and Petsko G.A. Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature 357 (1992) 423-424
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 12
    • 0037688133 scopus 로고    scopus 로고
    • Molecular adaptations to cold in psychrophilic enzymes
    • Feller G. Molecular adaptations to cold in psychrophilic enzymes. Cell. Mol. Life Sci. 60 (2003) 648-662
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 648-662
    • Feller, G.1
  • 13
    • 69449102173 scopus 로고    scopus 로고
    • Biotechnological aspects of cold-adapted enzymes
    • Margesin R., Schinner F., Marx J.C., and Gerday C. (Eds), Springer Verlag, Heidelberg
    • Huston A.L. Biotechnological aspects of cold-adapted enzymes. In: Margesin R., Schinner F., Marx J.C., and Gerday C. (Eds). Psychrophiles: from Biodiversity to Biotechnology (2007), Springer Verlag, Heidelberg 347-363
    • (2007) Psychrophiles: from Biodiversity to Biotechnology , pp. 347-363
    • Huston, A.L.1
  • 14
    • 2942560270 scopus 로고    scopus 로고
    • Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H
    • Huston A.L., Methe B., and Deming J.W. Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H. Appl. Environ. Microbiol. 70 (2004) 3321-3328
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3321-3328
    • Huston, A.L.1    Methe, B.2    Deming, J.W.3
  • 15
    • 10944253095 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis
    • Haeggstrom J.Z. Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis. J. Biol. Chem. 279 (2004) 50639-50642
    • (2004) J. Biol. Chem. , vol.279 , pp. 50639-50642
    • Haeggstrom, J.Z.1
  • 16
    • 0035146853 scopus 로고    scopus 로고
    • Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation
    • Thunnissen M.M., Nordlund P., and Haeggstrom J.Z. Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat. Struct. Biol. 8 (2001) 131-135
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 131-135
    • Thunnissen, M.M.1    Nordlund, P.2    Haeggstrom, J.Z.3
  • 17
    • 0034548849 scopus 로고    scopus 로고
    • Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice
    • Huston A.L., Krieger-Brockett B.B., and Deming J.W. Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice. Environ. Microbiol. 2 (2000) 383-388
    • (2000) Environ. Microbiol. , vol.2 , pp. 383-388
    • Huston, A.L.1    Krieger-Brockett, B.B.2    Deming, J.W.3
  • 18
    • 3342936478 scopus 로고    scopus 로고
    • A comprehensive analysis of 40 blind protein structure predictions
    • Samudrala R., and Levitt M. A comprehensive analysis of 40 blind protein structure predictions. BMC Struct. Biol. 2 (2002) 3-18
    • (2002) BMC Struct. Biol. , vol.2 , pp. 3-18
    • Samudrala, R.1    Levitt, M.2
  • 19
    • 0029103125 scopus 로고
    • Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase
    • Blomster M., Wetterholm A., Mueller M.J., and Haeggstrom J.Z. Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase. Eur. J. Biochem. 231 (1995) 528-534
    • (1995) Eur. J. Biochem. , vol.231 , pp. 528-534
    • Blomster, M.1    Wetterholm, A.2    Mueller, M.J.3    Haeggstrom, J.Z.4
  • 21
    • 0037059334 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms
    • Rudberg P.C., Tholander F., Thunnissen M.M., and Haeggstrom J.Z. Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J. Biol. Chem. 277 (2002) 1398-1404
    • (2002) J. Biol. Chem. , vol.277 , pp. 1398-1404
    • Rudberg, P.C.1    Tholander, F.2    Thunnissen, M.M.3    Haeggstrom, J.Z.4
  • 22
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 23
    • 33646151145 scopus 로고    scopus 로고
    • A nondetergent sulfobetaine prevents protein aggregation in microcalorimetric studies
    • Collins T., D'Amico S., Georlette D., Marx J.C., Huston A.L., and Feller G. A nondetergent sulfobetaine prevents protein aggregation in microcalorimetric studies. Anal. Biochem. 352 (2006) 299-301
    • (2006) Anal. Biochem. , vol.352 , pp. 299-301
    • Collins, T.1    D'Amico, S.2    Georlette, D.3    Marx, J.C.4    Huston, A.L.5    Feller, G.6
  • 24
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • Sanchez-Ruiz J.M., Lopez-Lacomba J.L., Cortijo M., and Mateo P.L. Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry 27 (1988) 1648-1652
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 25
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne T., Gerday C., and Feller G. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta 1543 (2000) 1-10
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 26
    • 0027378450 scopus 로고
    • Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants
    • Royer C.A., Mann C.J., and Matthews C.R. Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Sci. 2 (1993) 1844-1852
    • (1993) Protein Sci. , vol.2 , pp. 1844-1852
    • Royer, C.A.1    Mann, C.J.2    Matthews, C.R.3
  • 27
    • 0021111837 scopus 로고
    • Oxygen quenching and fluorescence depolarization of tyrosine residues in proteins
    • Lakowicz J.R., and Maliwal B.P. Oxygen quenching and fluorescence depolarization of tyrosine residues in proteins. J. Biol. Chem. 258 (1983) 4794-4801
    • (1983) J. Biol. Chem. , vol.258 , pp. 4794-4801
    • Lakowicz, J.R.1    Maliwal, B.P.2
  • 28
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 29
    • 24944585182 scopus 로고    scopus 로고
    • Characterization of arginine as a solvent additive: a halophilic enzyme as a model protein
    • Ishibashi M., Tsumoto K., Ejima D., Arakawa T., and Tokunaga M. Characterization of arginine as a solvent additive: a halophilic enzyme as a model protein. Protein Pept. Lett. 12 (2005) 649-653
    • (2005) Protein Pept. Lett. , vol.12 , pp. 649-653
    • Ishibashi, M.1    Tsumoto, K.2    Ejima, D.3    Arakawa, T.4    Tokunaga, M.5
  • 30
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: hot topics in cold adaptation
    • Feller G., and Gerday C. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1 (2003) 200-208
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 31
    • 0034099760 scopus 로고    scopus 로고
    • Structure, function, and regulation of leukotriene A4 hydrolase
    • Haeggstrom J.Z. Structure, function, and regulation of leukotriene A4 hydrolase. Am. J. Respir. Crit. Care Med. 161 (2000) S25-S31
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161
    • Haeggstrom, J.Z.1
  • 32
    • 25844496980 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae
    • Tholander F., Kull F., Ohlson E., Shafqat J., Thunnissen M.M., and Haeggstrom J.Z. Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 33477-33486
    • (2005) J. Biol. Chem. , vol.280 , pp. 33477-33486
    • Tholander, F.1    Kull, F.2    Ohlson, E.3    Shafqat, J.4    Thunnissen, M.M.5    Haeggstrom, J.Z.6
  • 33
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes
    • Fields P.A., and Somero G.N. Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 11476-11481
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 34
    • 0036384211 scopus 로고    scopus 로고
    • Structural bases of stability-function tradeoffs in enzymes
    • Beadle B.M., and Shoichet B.K. Structural bases of stability-function tradeoffs in enzymes. J. Mol. Biol. 321 (2002) 285-296
    • (2002) J. Mol. Biol. , vol.321 , pp. 285-296
    • Beadle, B.M.1    Shoichet, B.K.2
  • 35
    • 0037466287 scopus 로고    scopus 로고
    • Activity, stability and flexibility in glycosidases adapted to extreme thermal environments
    • Collins T., Meuwis M.A., Gerday C., and Feller G. Activity, stability and flexibility in glycosidases adapted to extreme thermal environments. J. Mol. Biol. 328 (2003) 419-428
    • (2003) J. Mol. Biol. , vol.328 , pp. 419-428
    • Collins, T.1    Meuwis, M.A.2    Gerday, C.3    Feller, G.4
  • 36
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico S., Marx J.C., Gerday C., and Feller G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 278 (2003) 7891-7896
    • (2003) J. Biol. Chem. , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 37
    • 0141596172 scopus 로고    scopus 로고
    • Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases
    • Georlette D., Damien B., Blaise V., Depiereux E., Uversky V.N., Gerday C., and Feller G. Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases. J. Biol. Chem. 278 (2003) 37015-37023
    • (2003) J. Biol. Chem. , vol.278 , pp. 37015-37023
    • Georlette, D.1    Damien, B.2    Blaise, V.3    Depiereux, E.4    Uversky, V.N.5    Gerday, C.6    Feller, G.7
  • 38
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Privalov P.L. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35 (1982) 1-104
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 39
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews B.W., Nicholson H., and Becktel W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 6663-6667
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 40
    • 0035092041 scopus 로고    scopus 로고
    • Molecular confinement influences protein structure and enhances thermal protein stability
    • Eggers D.K., and Valentine J.S. Molecular confinement influences protein structure and enhances thermal protein stability. Protein Sci. 10 (2001) 250-261
    • (2001) Protein Sci. , vol.10 , pp. 250-261
    • Eggers, D.K.1    Valentine, J.S.2
  • 41
    • 1242338901 scopus 로고    scopus 로고
    • Loops, linkages, rings, catenanes, cages, and crowders: entropy-based strategies for stabilizing proteins
    • Zhou H.X. Loops, linkages, rings, catenanes, cages, and crowders: entropy-based strategies for stabilizing proteins. Acc. Chem. Res. 37 (2004) 123-130
    • (2004) Acc. Chem. Res. , vol.37 , pp. 123-130
    • Zhou, H.X.1
  • 42
    • 0026648514 scopus 로고
    • Stability and reconstitution of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    • Rehaber V., and Jaenicke R. Stability and reconstitution of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima. J. Biol. Chem. 267 (1992) 10999-11006
    • (1992) J. Biol. Chem. , vol.267 , pp. 10999-11006
    • Rehaber, V.1    Jaenicke, R.2
  • 43
    • 0029086917 scopus 로고
    • Activation of chicken liver dihydrofolate reductase in concentrated urea solutions
    • Fan Y.X., Ju M., Zhou J.M., and Tsou C.L. Activation of chicken liver dihydrofolate reductase in concentrated urea solutions. Biochim. Biophys. Acta 1252 (1995) 151-157
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 151-157
    • Fan, Y.X.1    Ju, M.2    Zhou, J.M.3    Tsou, C.L.4
  • 44
    • 0034237245 scopus 로고    scopus 로고
    • Effect of thermal and chemical denaturants on Thermoanaerobacter ethanolicus secondary-alcohol dehydrogenase stability and activity
    • Burdette D.S., Tchernajencko V.V., and Zeikus J.G. Effect of thermal and chemical denaturants on Thermoanaerobacter ethanolicus secondary-alcohol dehydrogenase stability and activity. Enzyme Microb. Technol. 27 (2000) 11-18
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 11-18
    • Burdette, D.S.1    Tchernajencko, V.V.2    Zeikus, J.G.3
  • 45
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero G.N. Proteins and temperature. Annu. Rev. Physiol. 57 (1995) 43-68
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.