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Volumn 282, Issue 8, 2015, Pages 1445-1457

Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II

Author keywords

bioengineering; carbonic anhydrase; differential scanning calorimetry; protein crystallography; protein thermal stability

Indexed keywords

CARBONATE DEHYDRATASE II; PROLINE;

EID: 84927626008     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13232     Document Type: Article
Times cited : (33)

References (57)
  • 3
    • 0015239422 scopus 로고
    • The carbon dioxide hydration activity of carbonic anhydrase I. Stop-flow kinetic studies on the native human isoenzyme B and C
    • Khalifah RG, (1971) The carbon dioxide hydration activity of carbonic anhydrase I. Stop-flow kinetic studies on the native human isoenzyme B and C. J Biol Chem 246, 2561-2573.
    • (1971) J Biol Chem , vol.246 , pp. 2561-2573
    • Khalifah, R.G.1
  • 4
    • 33845278732 scopus 로고
    • The catalytic mechanism of carbonic anhydrase: Implications of a rate-limiting protolysis of water
    • Silverman DN, &, Lindskog S, (1988) The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water. Acc Chem Res 21, 30-36.
    • (1988) Acc Chem Res , vol.21 , pp. 30-36
    • Silverman, D.N.1    Lindskog, S.2
  • 5
    • 0024421430 scopus 로고
    • Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant
    • Tu CK, Silverman DN, Forsman C, Jonsson BH, &, Lindskog S, (1989) Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant. Biochemistry 28, 7913-7918.
    • (1989) Biochemistry , vol.28 , pp. 7913-7918
    • Tu, C.K.1    Silverman, D.N.2    Forsman, C.3    Jonsson, B.H.4    Lindskog, S.5
  • 6
    • 0016722749 scopus 로고
    • Catalytic mechanism of carbonic anhydrase - Hydrogen-isotope effects on kinetic-parameters of human C isoenzyme
    • Steiner H, Jonsson BH, &, Lindskog S, (1975) Catalytic mechanism of carbonic anhydrase-hydrogen-isotope effects on kinetic-parameters of human C isoenzyme. Eur J Biochem 59, 253-259.
    • (1975) Eur J Biochem , vol.59 , pp. 253-259
    • Steiner, H.1    Jonsson, B.H.2    Lindskog, S.3
  • 7
    • 34548724094 scopus 로고    scopus 로고
    • Solvent-mediated proton transfer in catalysis by carbonic anhydrase
    • Silverman DN, &, McKenna R, (2007) Solvent-mediated proton transfer in catalysis by carbonic anhydrase. Acc Chem Res 40, 669-675.
    • (2007) Acc Chem Res , vol.40 , pp. 669-675
    • Silverman, D.N.1    McKenna, R.2
  • 9
    • 84885465812 scopus 로고    scopus 로고
    • Carbonic anhydrase: An efficient enzyme with possible global implications
    • Boone CD, Gill S, Habibzadegan A, &, McKenna R, (2013) Carbonic anhydrase: an efficient enzyme with possible global implications. Int J Chem Eng 2013, 1-6.
    • (2013) Int J Chem Eng , vol.2013 , pp. 1-6
    • Boone, C.D.1    Gill, S.2    Habibzadegan, A.3    McKenna, R.4
  • 10
    • 84881306371 scopus 로고    scopus 로고
    • Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond
    • Boone CD, Habibzadegan A, Tu C, Silverman DN, &, McKenna R, (2013) Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond. Acta Crystallogr D 69, 1414-1422.
    • (2013) Acta Crystallogr D , vol.69 , pp. 1414-1422
    • Boone, C.D.1    Habibzadegan, A.2    Tu, C.3    Silverman, D.N.4    McKenna, R.5
  • 15
    • 0027474760 scopus 로고
    • The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent
    • Davies GJ, Gamblin SJ, Littlechild JA, &, Watson HC, (1993) The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent. Proteins 15, 283-289.
    • (1993) Proteins , vol.15 , pp. 283-289
    • Davies, G.J.1    Gamblin, S.J.2    Littlechild, J.A.3    Watson, H.C.4
  • 16
    • 0029018981 scopus 로고
    • XylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana
    • Vieille C, Hess JM, Kelly RM, &, Zeikus JG, (1995) xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana. Appl Environ Microbiol 61, 1867-1875.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1867-1875
    • Vieille, C.1    Hess, J.M.2    Kelly, R.M.3    Zeikus, J.G.4
  • 17
    • 0032526414 scopus 로고    scopus 로고
    • Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: The crystal structure at 2.1 Å resolution reveals strategies for intrinsic protein stabilization
    • Auerbach G, Ostendorp R, Prade L, Korndörfer I, Dams T, Huber R, &, Jaenicke R, (1998) Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: the crystal structure at 2.1 Å resolution reveals strategies for intrinsic protein stabilization. Structure 6, 769-781.
    • (1998) Structure , vol.6 , pp. 769-781
    • Auerbach, G.1    Ostendorp, R.2    Prade, L.3    Korndörfer, I.4    Dams, T.5    Huber, R.6    Jaenicke, R.7
  • 18
    • 0032982023 scopus 로고    scopus 로고
    • Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: Insights into its activity and thermostability
    • Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, &, Kim SH, (1999) Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability. FEBS Lett 445, 375-383.
    • (1999) FEBS Lett , vol.445 , pp. 375-383
    • Chi, Y.I.1    Martinez-Cruz, L.A.2    Jancarik, J.3    Swanson, R.V.4    Robertson, D.E.5    Kim, S.H.6
  • 20
    • 0033588218 scopus 로고    scopus 로고
    • Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
    • Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, &, Littlechild JA, (1999) Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. J Mol Biol 291, 651-660.
    • (1999) J Mol Biol , vol.291 , pp. 651-660
    • Isupov, M.N.1    Fleming, T.M.2    Dalby, A.R.3    Crowhurst, G.S.4    Bourne, P.C.5    Littlechild, J.A.6
  • 21
    • 0032709104 scopus 로고    scopus 로고
    • The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparitive thermostability structural analysis of ten different TIM structures
    • Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, et al,. (1999) The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparitive thermostability structural analysis of ten different TIM structures. Proteins 37, 441-453.
    • (1999) Proteins , vol.37 , pp. 441-453
    • Maes, D.1    Zeelen, J.P.2    Thanki, N.3    Beaucamp, N.4    Alvarez, M.5    Thi, M.H.6    Backmann, J.7    Martial, J.A.8    Wyns, L.9    Jaenicke, R.10    Al, E.11
  • 22
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolutoin
    • Russell RJ, Ferguson JM, Hough DW, Danson MJ, &, Taylor GL, (1997) The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolutoin. Biochemistry 36, 9983-9994.
    • (1997) Biochemistry , vol.36 , pp. 9983-9994
    • Russell, R.J.1    Ferguson, J.M.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 24
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov PL, &, Khechinashvili NN, (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J Mol Biol 86, 665-684.
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 25
    • 0025182227 scopus 로고
    • Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond
    • Kuwajima K, Ikeguchi M, Sugawara M, Hiraoka Y, &, Sugai S, (1990) Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond. Biochemistry 29, 8240-8249.
    • (1990) Biochemistry , vol.29 , pp. 8240-8249
    • Kuwajima, K.1    Ikeguchi, M.2    Sugawara, M.3    Hiraoka, Y.4    Sugai, S.5
  • 26
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, &, Honig B, (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 27
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews BW, Nicholson H, &, Becktel WJ, (1987) Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc Natl Acad Sci USA 84, 6663-6667.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 28
    • 74549207309 scopus 로고    scopus 로고
    • Assessing computational methods for predicting protein stability upon mutation: Good on average but not in the details
    • Potapov V, Cohen M, &, Schreiber G, (2009) Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details. Protein Eng Des Sel 22, 553-560.
    • (2009) Protein Eng des Sel , vol.22 , pp. 553-560
    • Potapov, V.1    Cohen, M.2    Schreiber, G.3
  • 29
    • 0033958727 scopus 로고    scopus 로고
    • Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive subfamily from the archaeon Archaeoglobus fulgidus
    • Manco G, Giosuè E, D'Auria S, Herman P, Carrea G, &, Rossi M, (2000) Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive subfamily from the archaeon Archaeoglobus fulgidus. Arch Biochem Biophys 373, 182-192.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 182-192
    • Manco, G.1    Giosuè, E.2    D'Auria, S.3    Herman, P.4    Carrea, G.5    Rossi, M.6
  • 30
    • 0030249182 scopus 로고    scopus 로고
    • Adenylate kinase from Sulfolobus acidocaldarius: Expression in Escherichia coli and characterization by Fourier transform infrared spectroscopy
    • Bonisch H, Backmann J, Kath T, Naumann D, &, Schafer G, (1996) Adenylate kinase from Sulfolobus acidocaldarius: expression in Escherichia coli and characterization by Fourier transform infrared spectroscopy. Arch Biochem Biophys 333, 75-84.
    • (1996) Arch Biochem Biophys , vol.333 , pp. 75-84
    • Bonisch, H.1    Backmann, J.2    Kath, T.3    Naumann, D.4    Schafer, G.5
  • 31
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, &, Bohm G, (1998) The stability of proteins in extreme environments. Curr Opin Struct Biol 8, 738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 32
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Závodszky P, Kardos J, Svingor A, &, Petsko GA, (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc Natl Acad Sci USA 95, 406-411.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 406-411
    • Závodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 33
    • 0034712678 scopus 로고    scopus 로고
    • Tryptophan phophorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases
    • Gershenson A, Schauerte JA, Giver L, &, Arnold FH, (2000) Tryptophan phophorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases. Biochemistry 39, 4658-4665.
    • (2000) Biochemistry , vol.39 , pp. 4658-4665
    • Gershenson, A.1    Schauerte, J.A.2    Giver, L.3    Arnold, F.H.4
  • 34
    • 0034073503 scopus 로고    scopus 로고
    • Molecular determinants of xylose isomerase thermal stability and activity: Analysis of thermozymes by site-directed mutagenesis
    • Sriprapundh D, Vieille C, &, Zeikus JG, (2000) Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis. Protein Eng 13, 259-265.
    • (2000) Protein Eng , vol.13 , pp. 259-265
    • Sriprapundh, D.1    Vieille, C.2    Zeikus, J.G.3
  • 36
    • 0032703356 scopus 로고    scopus 로고
    • Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specficity and thermostability
    • Li C, Heatwole J, Soelaiman S, &, Shoham M, (1999) Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specficity and thermostability. Proteins 37, 619-627.
    • (1999) Proteins , vol.37 , pp. 619-627
    • Li, C.1    Heatwole, J.2    Soelaiman, S.3    Shoham, M.4
  • 37
    • 0028130117 scopus 로고
    • Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule
    • Watanabe K, Masuda T, Ohashi H, Mihara H, &, Suzuki Y, (1994) Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule. Eur J Biochem 226, 277-283.
    • (1994) Eur J Biochem , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihara, H.4    Suzuki, Y.5
  • 39
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C, &, Zeikus GJ, (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65, 1-43.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 40
    • 0031406580 scopus 로고    scopus 로고
    • Investigations on the thermostability and function of truncated Thermus aquaticus DNA polymerase fragments
    • Villbrandt B, Sagner G, &, Schomburg D, (1997) Investigations on the thermostability and function of truncated Thermus aquaticus DNA polymerase fragments. Protein Eng 10, 1281-1288.
    • (1997) Protein Eng , vol.10 , pp. 1281-1288
    • Villbrandt, B.1    Sagner, G.2    Schomburg, D.3
  • 42
    • 84927602453 scopus 로고    scopus 로고
    • Carbonic anhydrase having increased stability under high temperature conditions. US Patent 7521217, CO2 Solutions Inc. Québec, Canada
    • Daigle R, &, Desrochers M, (2009) Carbonic anhydrase having increased stability under high temperature conditions. US Patent 7521217, CO2 Solutions Inc., Québec, Canada.
    • (2009)
    • Daigle, R.1    Desrochers, M.2
  • 44
    • 0037207131 scopus 로고    scopus 로고
    • Dramatic stabilization of the native state of human carbonic anhydrase II by an engineered disulfide bond
    • Mårtensson L-G, Karlsson M, &, Carlsson U, (2002) Dramatic stabilization of the native state of human carbonic anhydrase II by an engineered disulfide bond. Biochemistry 41, 15867-15875.
    • (2002) Biochemistry , vol.41 , pp. 15867-15875
    • Mårtensson, L.-G.1    Karlsson, M.2    Carlsson, U.3
  • 45
    • 84884919487 scopus 로고    scopus 로고
    • Structural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase II
    • Boone CD, Gill S, Tu C, Silverman DN, &, McKenna R, (2013) Structural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase II. Arch Biochem Biophys 539, 31-37.
    • (2013) Arch Biochem Biophys , vol.539 , pp. 31-37
    • Boone, C.D.1    Gill, S.2    Tu, C.3    Silverman, D.N.4    McKenna, R.5
  • 48
    • 0017378545 scopus 로고
    • Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B
    • Khalifah RG, Strader DJ, Bryant SH, &, Gibson SM, (1977) Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B. Biochemistry 16, 2241-2247.
    • (1977) Biochemistry , vol.16 , pp. 2241-2247
    • Khalifah, R.G.1    Strader, D.J.2    Bryant, S.H.3    Gibson, S.M.4
  • 49
  • 50
    • 0020346412 scopus 로고
    • Carbonic anhydrase: Oxygen-18 exchange catalyzed by an enzyme with rate-contributing proton-transfer steps
    • Silverman DN, (1982) Carbonic anhydrase: oxygen-18 exchange catalyzed by an enzyme with rate-contributing proton-transfer steps. Methods Enzymol 87, 732-752.
    • (1982) Methods Enzymol , vol.87 , pp. 732-752
    • Silverman, D.N.1
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley P, &, Cowtan K, (2004) COOT: model-building tools for molecular graphics. Acta Crystallogr D 60, 2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 57
    • 0030452417 scopus 로고    scopus 로고
    • X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis
    • Scolnick LR, &, Christianson DW, (1996) X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis. Biochemistry 35, 16429-16434.
    • (1996) Biochemistry , vol.35 , pp. 16429-16434
    • Scolnick, L.R.1    Christianson, D.W.2


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