Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense (261 views visite)
Bioorg Med Chem Lett (ISSN: 0960-894x), 2015 May 1; 25(9): 2002-2006.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.486, 5-year impact factor Impact factor a 5 anni: 2.303
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84925690260&partnerID=40&md5=1c09ed44997e4aaa2a21701dc8ffbad8
Keywords Parole chiave: Bacterial Carbonic Anhydrase, Proton Transfer Mechanism, Thermoactive Enzyme, Thermostable Enzyme,
Affiliations Affiliazioni:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy
Seconda Università di Napoli (SUN), 81100 Caserta, Italy
Istituto di Bioscienze e Biorisorse-CNR, Via P. Castellino 111, 80131 Napoli, Italy
Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy
NEUROFARBA Department, Sezione di Scienze Farmaceutiche, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy
References Riferimenti:
Supuran, C.T., (2008) Nat. Rev. Drug Disc., 7, p. 16
Alterio, V., Di Fiore, A., D'Ambrosio, K., Supuran, C.T., De Simone, G., (2012) Chem. Rev., 112, p. 4421
Silverman, D.N., McKenna, R., (2007) Acc. Chem. Res., 40, p. 669
Mikulski, R.L., Silverman, D.N., (2010) Biochim. Biophys. Acta, 1804, p. 422
Boone, C.D., Pinard, M., McKenna, R., Silverman, D., (2014) Sub-cellular Biochem., 75, p. 31
Aggarwal, M., Kondeti, B., Tu, C., Maupin, C.M., Silverman, D.N., McKenna, R., (2014) IUCrJ, 1, p. 129
Mikulski, R., West, D., Sippel, K.H., Avvaru, B.S., Aggarwal, M., Tu, C., McKenna, R., Silverman, D.N., (2013) Biochemistry, 52, p. 125
Fisher, S.Z., Kovalevsky, A.Y., Domsic, J.F., Mustyakimov, M., McKenna, R., Silverman, D.N., Langan, P.A., (2010) Biochemistry, 49, p. 415
Roy, A., Taraphder, S., (2006) Biopolymers, 82, p. 623
Savile, C.K., Lalonde, J.J., (2011) Curr. Opin. Biotechnol., 22, p. 818
Fisher, Z., Boone, C.D., Biswas, S.M., Venkatakrishnan, B., Aggarwal, M., Tu, C., Agbandje-Mckenna, M., McKenna, R., (2012) Protein Eng. Des. Sel., 25, p. 347
Supuran, C.T., (2013) J. Enzyme Inhib. Med. Chem., 28, p. 229
Alterio, V., Monti, S.M., De Simone, G., (2014) Subcell Biochem., 75, p. 387
Alafeefy, A.M., Abdel-Aziz, H.A., Vullo, D., Al-Tamimi, A.M., Al-Jaber, N.A., Capasso, C., Supuran, C.T., (2014) Bioorg. Med. Chem., 22, p. 141
Migliardini, F., De Luca, V., Carginale, V., Rossi, M., Corbo, P., Supuran, C.T., Capasso, C., (2014) J. Enzyme Inhib. Med. Chem., 29, p. 146
Vullo, D., De Luca, V., Scozzafava, A., Carginale, V., Rossi, M., Supuran, C.T., Capasso, C., (2012) Bioorg. Med. Chem. Lett., 22, p. 6324
Borchert, M., Saunders, P., (2008) Heat Stable Carbonic Anhydrases and Their Use, , WO2008095057
Borchert, M.S., (2012) Heat Stable Persephonella Carbonic Anhydrases and Their Use, , WO2012025577
Daigle, R., Desrochers, M., (2009) Carbonic Anhydrase Having Increased Stability under High Temperature Conditions, , US 7,521,217, B2
Akdemir, A., Vullo, D., De Luca, V., Scozzafava, A., Carginale, V., Rossi, M., Supuran, C.T., Capasso, C., (2013) Bioorg. Med. Chem. Lett., 23, p. 1087
Capasso, C., De Luca, V., Carginale, V., Cannio, R., Rossi, M., (2012) J. Enzyme Inhib. Med. Chem., 27, p. 892
De Luca, V., Vullo, D., Scozzafava, A., Carginale, V., Rossi, M., Supuran, C.T., Capasso, C., (2012) Bioorg. Med. Chem. Lett., 22, p. 5630
Di Fiore, A., Capasso, C., De Luca, V., Monti, S.M., Carginale, V., Supuran, C.T., Scozzafava, A., De Simone, G., (2013) Acta Crystallogr.
Sect. D: Biol. Crystallogr., 69, p. 1150
Russo, M.E., Olivieri, G., Capasso, C., De Luca, V., Marzocchella, A., Salatino, P., Rossi, M., (2013) Enzyme Microb. Technol., 53, p. 271
Huang, S., Xue, Y., Sauer-Eriksson, E., Chirica, L., Lindskog, S., Jonsson, B.H., (1998) J. Mol. Biol., 283, p. 301
James, P., Isupov, M.N., Sayer, C., Saneei, V., Berg, S., Lioliou, M., Kotlar, H.K., Littlechild, J.A., (2014) Acta Crystallogr.
Eriksson, A.E., Jones, T.A., Liljas, A., (1988) Proteins, 4, p. 274
Alterio, V., Hilvo, M., Di Fiore, A., Supuran, C.T., Pan, P., Parkkila, S., Scaloni, A., De Simone, G., (2009) Proc. Natl. Acad. Sci. U.S.A., 106, p. 16233
Cuesta-Seijo, J.A., Borchert, M.S., Navarro-Poulsen, J.C., Schnorr, K.M., Mortensen, S.B., Lo Leggio, L., (2011) FEBS Lett., 585, p. 1042
Pilka, E.S., Kochan, G., Oppermann, U., Yue, W.W., (2012) Biochem. Biophys. Res. Commun., 419, p. 485
Premkumar, L., Greenblatt, H.M., Bageshwar, U.K., Savchenko, T., Gokhman, I., Sussman, J.L., Zamir, A., (2005) Proc. Natl. Acad. Sci. U.S.A., 102, p. 7493
Stams, T., Nair, S.K., Okuyama, T., Waheed, A., Sly, W.S., Christianson, D.W., (1996) Proc. Natl. Acad. Sci. U.S.A., 93, p. 13589
Suzuki, K., Yang, S.Y., Shimizu, S., Morishita, E.C., Jiang, J., Zhang, F., Hoque, M.M., Takenaka, A., (2011) Acta Crystallogr.
Whittington, D.A., Grubb, J.H., Waheed, A., Shah, G.N., Sly, W.S., Christianson, D.W., (2004) J. Biol. Chem., 279, p. 7223
Whittington, D.A., Waheed, A., Ulmasov, B., Shah, G.N., Grubb, J.H., Sly, W.S., Christianson, D.W., (2001) Proc. Natl. Acad. Sci. U.S.A., 98, p. 9545
De Simone, G., Alterio, V., Supuran, C.T., (2013) Expert Opin. Drug Discov., 8, p. 793
D'Ambrosio, K., De Simone, G., Supuran C. ., T., (2015) Carbonic Anydrases As Biocatalysts: From Theory to Medical and Industrial Applications, pp. 17-30. , De Simone, G.
Domsic, J.F., Williams, W., Fisher, S.Z., Tu, C., Agbandje-Mckenna, M., Silverman, D.N., McKenna, R., (2010) Biochemistry, 49, p. 6394
Truppo, E., Supuran, C.T., Sandomenico, A., Vullo, D., Innocenti, A., Di Fiore, A., Alterio, V., Monti, S.M., (2012) Bioorg. Med. Chem. Lett., 22, p. 1560
Khalifah, R.G., (1977) Biochemistry, 16, p. 2236
Bradford, M.M., (1976) Anal. Biochem., 72, p. 248
Ascione, G., De Pascale, D., De Santi, C., Pedone, C., Dathan, N.A., Monti, S.M., (2012) Biochem. Biophys. Res. Commun., 420, p. 542
Alterio, V., De Simone, G., Monti, S.M., Scozzafava, A., Supuran, C.T., (2007) Bioorg. Med. Chem. Lett., 17, p. 4201
Di Fiore, A., Scozzafava, A., Winum, J.Y., Montero, J.L., Pedone, C., Supuran, C.T., De Simone, G., (2007) Bioorg. Med. Chem. Lett., 17, p. 1726
Di Fiore, A., Monti, S.M., Hilvo, M., Parkkila, S., Romano, V., Scaloni, A., Pedone, C., De Simone, G., (2009) Proteins, 74, p. 164
Di Fiore, A., Truppo, E., Supuran, C.T., Alterio, V., Dathan, N., Bootorabi, F., Parkkila, S., De Simone, G., (2010) Bioorg. Med. Chem. Lett., 20, p. 5023
Otwinowski, Z., Minor, W., (1997) Methods Enzymol., 276, p. 307
Navaza, J., (1994) Acta Crystallogr.
Brunger, A.T., (2007) Nat. Protoc., 2, p. 2728
Brunger, A.T., Adams, P.D., Clore, G.M., Delano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Warren, G.L., (1998) Acta Crystallogr.
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., (1991) Acta Crystallogr.
Krissinel, E., Henrick, K., (2007) J. Mol. Biol., 372, p. 774
Bioorg Med Chem Lett (ISSN: 0960-894x), 2015 May 1; 25(9): 2002-2006.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.486, 5-year impact factor Impact factor a 5 anni: 2.303
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84925690260&partnerID=40&md5=1c09ed44997e4aaa2a21701dc8ffbad8
Keywords Parole chiave: Bacterial Carbonic Anhydrase, Proton Transfer Mechanism, Thermoactive Enzyme, Thermostable Enzyme,
Affiliations Affiliazioni:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy
Seconda Università di Napoli (SUN), 81100 Caserta, Italy
Istituto di Bioscienze e Biorisorse-CNR, Via P. Castellino 111, 80131 Napoli, Italy
Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy
NEUROFARBA Department, Sezione di Scienze Farmaceutiche, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy
References Riferimenti:
Supuran, C.T., (2008) Nat. Rev. Drug Disc., 7, p. 16
Alterio, V., Di Fiore, A., D'Ambrosio, K., Supuran, C.T., De Simone, G., (2012) Chem. Rev., 112, p. 4421
Silverman, D.N., McKenna, R., (2007) Acc. Chem. Res., 40, p. 669
Mikulski, R.L., Silverman, D.N., (2010) Biochim. Biophys. Acta, 1804, p. 422
Boone, C.D., Pinard, M., McKenna, R., Silverman, D., (2014) Sub-cellular Biochem., 75, p. 31
Aggarwal, M., Kondeti, B., Tu, C., Maupin, C.M., Silverman, D.N., McKenna, R., (2014) IUCrJ, 1, p. 129
Mikulski, R., West, D., Sippel, K.H., Avvaru, B.S., Aggarwal, M., Tu, C., McKenna, R., Silverman, D.N., (2013) Biochemistry, 52, p. 125
Fisher, S.Z., Kovalevsky, A.Y., Domsic, J.F., Mustyakimov, M., McKenna, R., Silverman, D.N., Langan, P.A., (2010) Biochemistry, 49, p. 415
Roy, A., Taraphder, S., (2006) Biopolymers, 82, p. 623
Savile, C.K., Lalonde, J.J., (2011) Curr. Opin. Biotechnol., 22, p. 818
Fisher, Z., Boone, C.D., Biswas, S.M., Venkatakrishnan, B., Aggarwal, M., Tu, C., Agbandje-Mckenna, M., McKenna, R., (2012) Protein Eng. Des. Sel., 25, p. 347
Supuran, C.T., (2013) J. Enzyme Inhib. Med. Chem., 28, p. 229
Alterio, V., Monti, S.M., De Simone, G., (2014) Subcell Biochem., 75, p. 387
Alafeefy, A.M., Abdel-Aziz, H.A., Vullo, D., Al-Tamimi, A.M., Al-Jaber, N.A., Capasso, C., Supuran, C.T., (2014) Bioorg. Med. Chem., 22, p. 141
Migliardini, F., De Luca, V., Carginale, V., Rossi, M., Corbo, P., Supuran, C.T., Capasso, C., (2014) J. Enzyme Inhib. Med. Chem., 29, p. 146
Vullo, D., De Luca, V., Scozzafava, A., Carginale, V., Rossi, M., Supuran, C.T., Capasso, C., (2012) Bioorg. Med. Chem. Lett., 22, p. 6324
Borchert, M., Saunders, P., (2008) Heat Stable Carbonic Anhydrases and Their Use, , WO2008095057
Borchert, M.S., (2012) Heat Stable Persephonella Carbonic Anhydrases and Their Use, , WO2012025577
Daigle, R., Desrochers, M., (2009) Carbonic Anhydrase Having Increased Stability under High Temperature Conditions, , US 7,521,217, B2
Akdemir, A., Vullo, D., De Luca, V., Scozzafava, A., Carginale, V., Rossi, M., Supuran, C.T., Capasso, C., (2013) Bioorg. Med. Chem. Lett., 23, p. 1087
Capasso, C., De Luca, V., Carginale, V., Cannio, R., Rossi, M., (2012) J. Enzyme Inhib. Med. Chem., 27, p. 892
De Luca, V., Vullo, D., Scozzafava, A., Carginale, V., Rossi, M., Supuran, C.T., Capasso, C., (2012) Bioorg. Med. Chem. Lett., 22, p. 5630
Di Fiore, A., Capasso, C., De Luca, V., Monti, S.M., Carginale, V., Supuran, C.T., Scozzafava, A., De Simone, G., (2013) Acta Crystallogr.
Sect. D: Biol. Crystallogr., 69, p. 1150
Russo, M.E., Olivieri, G., Capasso, C., De Luca, V., Marzocchella, A., Salatino, P., Rossi, M., (2013) Enzyme Microb. Technol., 53, p. 271
Huang, S., Xue, Y., Sauer-Eriksson, E., Chirica, L., Lindskog, S., Jonsson, B.H., (1998) J. Mol. Biol., 283, p. 301
James, P., Isupov, M.N., Sayer, C., Saneei, V., Berg, S., Lioliou, M., Kotlar, H.K., Littlechild, J.A., (2014) Acta Crystallogr.
Eriksson, A.E., Jones, T.A., Liljas, A., (1988) Proteins, 4, p. 274
Alterio, V., Hilvo, M., Di Fiore, A., Supuran, C.T., Pan, P., Parkkila, S., Scaloni, A., De Simone, G., (2009) Proc. Natl. Acad. Sci. U.S.A., 106, p. 16233
Cuesta-Seijo, J.A., Borchert, M.S., Navarro-Poulsen, J.C., Schnorr, K.M., Mortensen, S.B., Lo Leggio, L., (2011) FEBS Lett., 585, p. 1042
Pilka, E.S., Kochan, G., Oppermann, U., Yue, W.W., (2012) Biochem. Biophys. Res. Commun., 419, p. 485
Premkumar, L., Greenblatt, H.M., Bageshwar, U.K., Savchenko, T., Gokhman, I., Sussman, J.L., Zamir, A., (2005) Proc. Natl. Acad. Sci. U.S.A., 102, p. 7493
Stams, T., Nair, S.K., Okuyama, T., Waheed, A., Sly, W.S., Christianson, D.W., (1996) Proc. Natl. Acad. Sci. U.S.A., 93, p. 13589
Suzuki, K., Yang, S.Y., Shimizu, S., Morishita, E.C., Jiang, J., Zhang, F., Hoque, M.M., Takenaka, A., (2011) Acta Crystallogr.
Whittington, D.A., Grubb, J.H., Waheed, A., Shah, G.N., Sly, W.S., Christianson, D.W., (2004) J. Biol. Chem., 279, p. 7223
Whittington, D.A., Waheed, A., Ulmasov, B., Shah, G.N., Grubb, J.H., Sly, W.S., Christianson, D.W., (2001) Proc. Natl. Acad. Sci. U.S.A., 98, p. 9545
De Simone, G., Alterio, V., Supuran, C.T., (2013) Expert Opin. Drug Discov., 8, p. 793
D'Ambrosio, K., De Simone, G., Supuran C. ., T., (2015) Carbonic Anydrases As Biocatalysts: From Theory to Medical and Industrial Applications, pp. 17-30. , De Simone, G.
Domsic, J.F., Williams, W., Fisher, S.Z., Tu, C., Agbandje-Mckenna, M., Silverman, D.N., McKenna, R., (2010) Biochemistry, 49, p. 6394
Truppo, E., Supuran, C.T., Sandomenico, A., Vullo, D., Innocenti, A., Di Fiore, A., Alterio, V., Monti, S.M., (2012) Bioorg. Med. Chem. Lett., 22, p. 1560
Khalifah, R.G., (1977) Biochemistry, 16, p. 2236
Bradford, M.M., (1976) Anal. Biochem., 72, p. 248
Ascione, G., De Pascale, D., De Santi, C., Pedone, C., Dathan, N.A., Monti, S.M., (2012) Biochem. Biophys. Res. Commun., 420, p. 542
Alterio, V., De Simone, G., Monti, S.M., Scozzafava, A., Supuran, C.T., (2007) Bioorg. Med. Chem. Lett., 17, p. 4201
Di Fiore, A., Scozzafava, A., Winum, J.Y., Montero, J.L., Pedone, C., Supuran, C.T., De Simone, G., (2007) Bioorg. Med. Chem. Lett., 17, p. 1726
Di Fiore, A., Monti, S.M., Hilvo, M., Parkkila, S., Romano, V., Scaloni, A., Pedone, C., De Simone, G., (2009) Proteins, 74, p. 164
Di Fiore, A., Truppo, E., Supuran, C.T., Alterio, V., Dathan, N., Bootorabi, F., Parkkila, S., De Simone, G., (2010) Bioorg. Med. Chem. Lett., 20, p. 5023
Otwinowski, Z., Minor, W., (1997) Methods Enzymol., 276, p. 307
Navaza, J., (1994) Acta Crystallogr.
Brunger, A.T., (2007) Nat. Protoc., 2, p. 2728
Brunger, A.T., Adams, P.D., Clore, G.M., Delano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Warren, G.L., (1998) Acta Crystallogr.
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., (1991) Acta Crystallogr.
Krissinel, E., Henrick, K., (2007) J. Mol. Biol., 372, p. 774
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense
Two thermostable α-carbonic anhydrases (α-CAs) isolated from thermophilic Sulfurihydrogenibium spp.; namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active α-CA known to date for the CO2 hydration reaction. Here we report the crystallographic structure of SazCA and the identification of the structural features responsible for its high catalytic activity, by comparing it with SspCA structure. These data are of relevance for the design of engineered proteins showing higher stability and catalytic activity than other α-CAs known to date. © 2015 Elsevier Ltd.
Two thermostable α-carbonic anhydrases (α-CAs) isolated from thermophilic Sulfurihydrogenibium spp.; namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active α-CA known to date for the CO
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense
| ▼ Structural characterization of proteins and enzymes isolated from organisms living under unusual conditions |
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense
Di Fiore A, Alterio V, Monti SM, De Simone G, D’Ambrosio K
* Thermostable carbonic anhydrases in biotechnological applications (429 visite)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(7): 15456-15480.
Impact Factor: 3.257
Dettagli Esporta in BibTeX Esporta in EndNote
1 Records (1 escludendo Abstract e Conferenze).
Impact factor totale: 3.257 (3.257 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 3.213 (3.213 escludendo Abstract e Conferenze).
Vai a fine pagina Versione per copia e incolla facile Esporta tutto in BibTeX Esporta tutto in EndNote
Di Fiore A, Alterio V, Monti SM, De Simone G, D’Ambrosio K
* Thermostable carbonic anhydrases in biotechnological applications (429 visite)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(7): 15456-15480.
Impact Factor: 3.257
Dettagli Esporta in BibTeX Esporta in EndNote
1 Records (1 escludendo Abstract e Conferenze).
Impact factor totale: 3.257 (3.257 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 3.213 (3.213 escludendo Abstract e Conferenze).
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