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Volumn 1764, Issue 2, 2006, Pages 190-198

Reversible inactivation of alkaline phosphatase from Atlantic cod (Gadus morhua) in urea

Author keywords

Cold adaptation; Dimer; Folding; Metalloenzyme; Psychrophilic; Stability

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALKALINE PHOSPHATASE; DIMER; METAL; TRYPTOPHAN; UREA; ZINC;

EID: 33644519055     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.12.015     Document Type: Article
Times cited : (13)

References (51)
  • 2
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • G. Feller, and C. Gerday 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
  • 3
    • 0025716254 scopus 로고
    • Protein structure and function at low temperatures
    • R. Jaenicke Protein structure and function at low temperatures Philos. Trans. R. Soc. Lond., B 326 1990 535 553
    • (1990) Philos. Trans. R. Soc. Lond., B , vol.326 , pp. 535-553
    • Jaenicke, R.1
  • 5
    • 0041384407 scopus 로고    scopus 로고
    • Temperature adaptation of proteins: Engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase
    • S. D'Amico, C. Gerday, and G. Feller Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase J. Mol. Biol. 332 2003 981 988
    • (2003) J. Mol. Biol. , vol.332 , pp. 981-988
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 7
    • 1542376774 scopus 로고    scopus 로고
    • Evolutionary convergence in adaptation of proteins to temperature: A4-Lactate dehydrogenases of Pacific damselfishes (Chromis spp.)
    • G.C. Johns, and G.N. Somero Evolutionary convergence in adaptation of proteins to temperature: A4-Lactate dehydrogenases of Pacific damselfishes (Chromis spp.) Mol. Biol. Evol. 21 2003 314 320
    • (2003) Mol. Biol. Evol. , vol.21 , pp. 314-320
    • Johns, G.C.1    Somero, G.N.2
  • 8
    • 0035816221 scopus 로고    scopus 로고
    • Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium
    • T. Lonhienne, J. Zoidakis, C.E. Vorgias, G. Feller, C. Gerday, and V. Bouriotis Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium J. Mol. Biol. 310 2001 291 297
    • (2001) J. Mol. Biol. , vol.310 , pp. 291-297
    • Lonhienne, T.1    Zoidakis, J.2    Vorgias, C.E.3    Feller, G.4    Gerday, C.5    Bouriotis, V.6
  • 9
    • 23844458318 scopus 로고    scopus 로고
    • Increased flexibility as a strategy for cold-adaptation: A comparative MD study of cold- and warm-active Uracil DNA glycosylase
    • M. Olufsen, A.O. Smalås, E. Moe, and B.O. Brandsdal Increased flexibility as a strategy for cold-adaptation: a comparative MD study of cold- and warm-active Uracil DNA glycosylase J. Biol. Chem. 280 2005 18042 18048
    • (2005) J. Biol. Chem. , vol.280 , pp. 18042-18048
    • Olufsen, M.1    Smalås, A.O.2    Moe, E.3    Brandsdal, B.O.4
  • 10
    • 0028606077 scopus 로고
    • Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
    • K.E. Neet, and D.E. Timm Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation Protein Sci. 3 1995 2167 2174
    • (1995) Protein Sci. , vol.3 , pp. 2167-2174
    • Neet, K.E.1    Timm, D.E.2
  • 12
    • 0031608378 scopus 로고    scopus 로고
    • Molecular adaptations in psychrophilic bacteria: Potential for biotechnological applications
    • N.J. Russell 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
  • 13
    • 0037931325 scopus 로고    scopus 로고
    • Characterization of a monomeric Escherichia coli alkaline phosphatase formed upon a single amino acid substitution
    • R.R. Boulanger Jr., and E.R. Kantrowitz Characterization of a monomeric Escherichia coli alkaline phosphatase formed upon a single amino acid substitution J. Biol. Chem. 278 2003 23497 23501
    • (2003) J. Biol. Chem. , vol.278 , pp. 23497-23501
    • Boulanger Jr., R.R.1    Kantrowitz, E.R.2
  • 14
    • 3342950031 scopus 로고    scopus 로고
    • Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis
    • V. Bucevic-Popovic, M. Pavela-Vrancic, and R. Dieckmann Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis Biochimie 6 2004 403 409
    • (2004) Biochimie , vol.6 , pp. 403-409
    • Bucevic-Popovic, V.1    Pavela-Vrancic, M.2    Dieckmann, R.3
  • 15
    • 0033762097 scopus 로고    scopus 로고
    • Dissociation and unfolding of cold-active alkaline phosphatase from Atlantic cod in the presence of guanidinium chloride
    • B. Ásgeirsson, J.B. Hauksson, and G.H. Gunnarsson Dissociation and unfolding of cold-active alkaline phosphatase from Atlantic cod in the presence of guanidinium chloride Eur. J. Biochem. 267 2000 6403 6412
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6403-6412
    • Ásgeirsson, B.1    Hauksson, J.B.2    Gunnarsson, G.H.3
  • 16
    • 0035960562 scopus 로고    scopus 로고
    • Dimeric procaspase-3 unfolds via a four-state equilibrium process
    • K. Bose, and A.C. Clark Dimeric procaspase-3 unfolds via a four-state equilibrium process Biochemistry 40 2001 14236 14242
    • (2001) Biochemistry , vol.40 , pp. 14236-14242
    • Bose, K.1    Clark, A.C.2
  • 17
    • 0035198044 scopus 로고    scopus 로고
    • Multiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturation
    • H.C. Hung, and G.G. Chang Multiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturation Biophys. J. 81 2001 3456 3471
    • (2001) Biophys. J. , vol.81 , pp. 3456-3471
    • Hung, H.C.1    Chang, G.G.2
  • 18
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures
    • E.E. Kim, and H.W. Wyckoff Reaction mechanism of alkaline phosphatase based on crystal structures J. Mol. Biol. 218 1991 449 469
    • (1991) J. Mol. Biol. , vol.218 , pp. 449-469
    • Kim, E.E.1    Wyckoff, H.W.2
  • 20
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution. Implication for a substrate specificity
    • M.H. Le Du, T. Stigbrand, M.J. Taussig, A. Ménez, and E.A. Stura Crystal structure of alkaline phosphatase from human placenta at 1.8 Å resolution. Implication for a substrate specificity J. Biol. Chem. 276 2001 9158 9165
    • (2001) J. Biol. Chem. , vol.276 , pp. 9158-9165
    • Le Du, M.H.1    Stigbrand, T.2    Taussig, M.J.3    Ménez, A.4    Stura, E.A.5
  • 21
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism for the alkaline phosphatase reaction involving three metal ions
    • B. Stec, K.M. Holtz, and E.R. Kantrowitz A revised mechanism for the alkaline phosphatase reaction involving three metal ions J. Mol. Biol. 299 2000 1323 1331
    • (2000) J. Mol. Biol. , vol.299 , pp. 1323-1331
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 22
    • 0028278168 scopus 로고
    • Why are mammalian alkaline phosphatases much more active than bacterial alkaline phosphatases?
    • J.E. Murphy, and E.R. Kantrowitz Why are mammalian alkaline phosphatases much more active than bacterial alkaline phosphatases? Mol. Microbiol. 12 1994 351 357
    • (1994) Mol. Microbiol. , vol.12 , pp. 351-357
    • Murphy, J.E.1    Kantrowitz, E.R.2
  • 23
    • 0025836206 scopus 로고
    • Alkaline phosphatase from the hepatopancreas of shrimp (Pandalus borealis): A dimeric enzyme with catalytically active subunits
    • R.L. Olsen, K. Øverbø, and B. Myrnes Alkaline phosphatase from the hepatopancreas of shrimp (Pandalus borealis): a dimeric enzyme with catalytically active subunits Comp. Biochem. Physiol. 99B 1991 755 761
    • (1991) Comp. Biochem. Physiol. , vol.99 , pp. 755-761
    • Olsen, R.L.1    Øverbø, K.2    Myrnes, B.3
  • 24
    • 0028873872 scopus 로고
    • Alkaline phosphatase from Atlantic cod (Gadus morhua). Kinetic and structural properties which indicate adaptation to low temperatures
    • B. Ásgeirsson, R. Hartemink, and J.F. Chlebowski Alkaline phosphatase from Atlantic cod (Gadus morhua). Kinetic and structural properties which indicate adaptation to low temperatures Comp. Biochem. Physiol. 110B 1995 315 329
    • (1995) Comp. Biochem. Physiol. , vol.110 , pp. 315-329
    • Ásgeirsson, B.1    Hartemink, R.2    Chlebowski, J.F.3
  • 27
    • 0036547751 scopus 로고    scopus 로고
    • Cloning of cold-active alkaline phosphatase gene of a psychrophile, Shewanella sp., and expression of the recombinant enzyme
    • T. Murakawa, H. Yamagata, H. Tsuruta, and Y. Aizono Cloning of cold-active alkaline phosphatase gene of a psychrophile, Shewanella sp., and expression of the recombinant enzyme Biosci. Biotechnol. Biochem. 66 2002 754 761
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 754-761
    • Murakawa, T.1    Yamagata, H.2    Tsuruta, H.3    Aizono, Y.4
  • 29
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • O.D. Monera, C.M. Kay, and R.S. Hodges Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions Protein Sci. 3 1994 1984 1991
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 30
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton IRL Press at Oxford Univ. Press Oxford
    • C.N. Pace, B.A. Shirley, and J.A. Thomson Measuring the conformational stability of a protein T.E. Creighton Protein Structure: A Practical Approach 1997 IRL Press at Oxford Univ. Press Oxford 299 321
    • (1997) Protein Structure: A Practical Approach , pp. 299-321
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 31
    • 0010174061 scopus 로고    scopus 로고
    • Fluorescence principles and measurement
    • D.A. Harris C.L. Bashford Oxford Univ. Press Oxford
    • A.G. Szabo Fluorescence principles and measurement D.A. Harris C.L. Bashford Spectrophotometry and Spectrofluorometry 2000 Oxford Univ. Press Oxford 62 66
    • (2000) Spectrophotometry and Spectrofluorometry , pp. 62-66
    • Szabo, A.G.1
  • 32
    • 19544365690 scopus 로고    scopus 로고
    • Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies
    • J.A. Sigman, T.H. Patwa, A.V. Tablante, C.D. Joseph, M.J. Glucksman, and A.J. Wolfson Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies Biochem. J. 388 2005 255 261
    • (2005) Biochem. J. , vol.388 , pp. 255-261
    • Sigman, J.A.1    Patwa, T.H.2    Tablante, A.V.3    Joseph, C.D.4    Glucksman, M.J.5    Wolfson, A.J.6
  • 33
    • 0042697207 scopus 로고    scopus 로고
    • Amino acid sequence of the cold-active alkaline phosphatase from Atlantic cod (Gadus morhua)
    • B. Ásgeirsson, B. Noesgaard Nielsen, and P. Højrup Amino acid sequence of the cold-active alkaline phosphatase from Atlantic cod (Gadus morhua) Comp. Biochem. Physiol. 136B 2003 45 60
    • (2003) Comp. Biochem. Physiol. , vol.136 , pp. 45-60
    • Ásgeirsson, B.1    Noesgaard Nielsen, B.2    Højrup, P.3
  • 34
    • 0344519692 scopus 로고    scopus 로고
    • Equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate
    • P. Wojciak, A. Mazurkiewicz, A. Bakalova, and R. Kuciel Equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate Int. J. Biol. Macromol. 32 2003 43 54
    • (2003) Int. J. Biol. Macromol. , vol.32 , pp. 43-54
    • Wojciak, P.1    Mazurkiewicz, A.2    Bakalova, A.3    Kuciel, R.4
  • 35
    • 0027279418 scopus 로고
    • Fluorometric analysis of native, urea-denatured and refolded human prostatic acid phosphatase
    • W.S. Ostrowski, R. Kuciel, F. Tanaka, and K. Yagi Fluorometric analysis of native, urea-denatured and refolded human prostatic acid phosphatase Biochim. Biophys. Acta 1164 1993 319 326
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 319-326
    • Ostrowski, W.S.1    Kuciel, R.2    Tanaka, F.3    Yagi, K.4
  • 36
    • 0029977146 scopus 로고    scopus 로고
    • Reversible unfolding of Escherichia coli alkaline phosphatase-Active site can be reconstituted by a number of pathways
    • S.N. Sarkar, and N. Ghosh Reversible unfolding of Escherichia coli alkaline phosphatase-Active site can be reconstituted by a number of pathways Arch. Biochem. Biophys. 330 1996 174 180
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 174-180
    • Sarkar, S.N.1    Ghosh, N.2
  • 39
    • 0023460908 scopus 로고
    • Early conformational changes and activity modulation induced by guanidinium chloride on intestinal alkaline phosphatase
    • G.A.D. Miggiano, A. Morsente, M.G. Pischiutta, G.E. Martoran, and A. Castelli Early conformational changes and activity modulation induced by guanidinium chloride on intestinal alkaline phosphatase Biochem. J. 248 1987 551 556
    • (1987) Biochem. J. , vol.248 , pp. 551-556
    • Miggiano, G.A.D.1    Morsente, A.2    Pischiutta, M.G.3    Martoran, G.E.4    Castelli, A.5
  • 40
    • 0025845421 scopus 로고
    • Anomalous stimulation of Escherichia coli alkaline phosphatase activity in guanidinium chloride-modulation of the rate-limiting step and negative cooperativity
    • N.M. Rao, and R. Nagaraj Anomalous stimulation of Escherichia coli alkaline phosphatase activity in guanidinium chloride-modulation of the rate-limiting step and negative cooperativity J. Biol. Chem. 266 1991 5018 5024
    • (1991) J. Biol. Chem. , vol.266 , pp. 5018-5024
    • Rao, N.M.1    Nagaraj, R.2
  • 41
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • S. Jones, and J.M. Thornton Analysis of protein-protein interaction sites using surface patches J. Mol. Biol. 272 1997 121 132
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 42
    • 0032522670 scopus 로고    scopus 로고
    • Morphology of protein-protein interfaces
    • T.A. Larsen, A.J. Olson, and D.S. Goodsell Morphology of protein-protein interfaces Structure 6 1998 421 427
    • (1998) Structure , vol.6 , pp. 421-427
    • Larsen, T.A.1    Olson, A.J.2    Goodsell, D.S.3
  • 43
    • 0033597205 scopus 로고    scopus 로고
    • Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum
    • S.Y. Kim, K.Y. Hwang, S.H. Kim, H.C. Sung, Y.S. Han, and Y. Cho Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum J. Biol. Chem. 274 1999 11761 11767
    • (1999) J. Biol. Chem. , vol.274 , pp. 11761-11767
    • Kim, S.Y.1    Hwang, K.Y.2    Kim, S.H.3    Sung, H.C.4    Han, Y.S.5    Cho, Y.6
  • 44
    • 0028103991 scopus 로고
    • The unfolding of trp aporepressor as a function of pH: Evidence for an unfolding intermediate
    • M.R. Eftink, K.J. Helton, A. Beavers, and G.D. Ramsay The unfolding of trp aporepressor as a function of pH: evidence for an unfolding intermediate Biochemistry 33 1994 10220 10228
    • (1994) Biochemistry , vol.33 , pp. 10220-10228
    • Eftink, M.R.1    Helton, K.J.2    Beavers, A.3    Ramsay, G.D.4
  • 45
    • 0027162425 scopus 로고
    • Energetics of intersubunit and intrasubunit interactions of Escherichia coli adenosine cyclic 3′,5′-phosphate receptor protein
    • X. Cheng, M.L. Gonzalez, and J.C. Lee Energetics of intersubunit and intrasubunit interactions of Escherichia coli adenosine cyclic 3′,5′-phosphate receptor protein Biochemistry 32 1993 8130 8139
    • (1993) Biochemistry , vol.32 , pp. 8130-8139
    • Cheng, X.1    Gonzalez, M.L.2    Lee, J.C.3
  • 46
    • 0037081777 scopus 로고    scopus 로고
    • Equilibrium unfolding studies of the rat liver methionine adenosyltransferase III, a dimeric enzyme with intersubunit active sites
    • M. Gasset, C. Alfonso, J.L. Neira, G. Rivas, and M.A. Pajares Equilibrium unfolding studies of the rat liver methionine adenosyltransferase III, a dimeric enzyme with intersubunit active sites Biochem. J. 361 2002 307 315
    • (2002) Biochem. J. , vol.361 , pp. 307-315
    • Gasset, M.1    Alfonso, C.2    Neira, J.L.3    Rivas, G.4    Pajares, M.A.5
  • 47
    • 0028820703 scopus 로고
    • Denaturant m-values and heat capacity changes: Relations to changes in accessible surface areas of protein folding
    • J.K. Myers, C.N. Pace, and J.M. Scholtz Denaturant m-values and heat capacity changes: relations to changes in accessible surface areas of protein folding Protein Sci. 4 1995 2138 2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 48
    • 33644526540 scopus 로고    scopus 로고
    • Thermodynamic characterization of yeast triosephosphate isomerase refolding. Insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme
    • H. Najera, M. Costas, and D.A. Fernandez-Velasco Thermodynamic characterization of yeast triosephosphate isomerase refolding. Insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme Biochem. J. 10 2002
    • (2002) Biochem. J. , vol.10
    • Najera, H.1    Costas, M.2    Fernandez-Velasco, D.A.3
  • 49
    • 0032953191 scopus 로고    scopus 로고
    • Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stability
    • D.C. Martin, S.C. Pastra-Landis, and E.R. Kantrowitz Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stability Protein Sci. 8 1999 1152 1159
    • (1999) Protein Sci. , vol.8 , pp. 1152-1159
    • Martin, D.C.1    Pastra-Landis, S.C.2    Kantrowitz, E.R.3
  • 51
    • 0032189529 scopus 로고    scopus 로고
    • Biphasic denaturation of human placental alkaline phosphatase in guanidinium chloride
    • H.C. Hung, and G.G. Chang Biphasic denaturation of human placental alkaline phosphatase in guanidinium chloride Proteins 33 1998 49 61
    • (1998) Proteins , vol.33 , pp. 49-61
    • Hung, H.C.1    Chang, G.G.2


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