The maturation mechanism of γ-glutamyl transpeptidases: Insights from the crystal structure of a precursor mimic of the enzyme from Bacillus licheniformis and from site-directed mutagenesis studies (126 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2016; 1864(2): 195-203.
Tipo di articolo: Journal Article,
Impact factor: 5.476, Impact factor a 5 anni: 5.725
Url: https://www2.scopus.com/inward/record.uri?eid=2-s2.0-84948453364&partnerID=40&md5=6569aec1c5036717080cf6d0ed6aa37a
Parole chiave: Autoprocessing, Single-Point Mutation, X-Ray Crystallography, γ-Glutamyltranspeptidase, γ-Gt Precursor, Alanine, Bacterial Enzyme, Carbonyl Derivative, Enzyme Precursor, Gamma Glutamyltransferase, Hydroxyl Group, Threonine, Article, Bacillus Licheniformis, Controlled Study, Crystal Structure, Enzyme Activity, Enzyme Mechanism, Enzyme Structure, Hydrogen Bond, Nonhuman, Nucleophilicity, Priority Journal, Site Directed Mutagenesis, X Ray Crystallography,
Affiliazioni:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone, 16, Naples, Italy
Department of Applied Chemistry, National Chiayi University, 300 Syuefu Road, Chiayi City, Taiwan
Riferimenti:
Castellano, I., Merlino, A., (2012) Cell. Mol. Life Sci., 69, pp. 3381-339
Stole, E., Smith, T.K., Manning, J.M., Meister, A., (1994) J. Biol. Chem., 269, pp. 21435-21439
Tate, S.S., Meister, A., (1981) Mol. Cell. Biochem., p. 39
Hanigan, M.H., Ricketts, W.A., (1993) Biochemistry, 32, pp. 6302-6306
Taniguchi, N., Ikeda, Y., (1998) Adv. Enzymol. Relat. Areas Mol. Biol., p. 72
Hanigan, M.H., Gallagher, B.C., Townsend, D.M., Gabarra, V., (1999) Carcinogenesis, 20, pp. 553-559
Wilk, S., Mizoguchi, H., Orlowski, M., (1978) J. Pharmacol. Exp. Ther., 206, pp. 227-232
Zhang, Q., Kulczynska, A., Webb, D.J., Megson, I.L., Botting, N.P., (2013) Chem. Commun., 49, pp. 1389-1391
Allison, R.D., (1985) Methods Enzymol., 113, pp. 419-437
Tate, S.S., (1986) FEBS Lett., 194, pp. 33-38
Inoue, M., Hiratake, J., Suzuki, H., Kumagai, H., Sakata, K., (2000) Biochemistry, 39, pp. 7764-7771
Xu, Q., Buckley, D., Guan, C., Guo, H.-C., (1999) Cell, 98, pp. 651-661
Qian, X., Guan, C., Guo, H.-C., (2003) Structure, 11, pp. 997-1003
Kim, Y., Yoon, K.-H., Khang, Y., Turley, S., Hol, W.G., (2000) Structure, 8, pp. 1059-1068
Hewitt, L., Kasche, V., Lummer, K., Lewis, R., Murshudov, G., Verma, C., Dodson, G., Wilson, K., (2000) J. Mol. Biol., 302, pp. 887-898
Ditzel, L., Huber, R., Mann, K., Heinemeyer, W., Wolf, D.H., Groll, M., (1998) J. Mol. Biol., 279, pp. 1187-1191
Bokhove, M., Yoshida, H., Hensgens, C.M., Van Der Laan, J.M., Sutherland, J.D., Dijkstra, B.W., (2010) Structure, 18, pp. 301-308
Minami, H., Suzuki, H., Kumagai, H., (2003) FEMS Microbiol. Lett., 224, pp. 169-173
Boanca, G., Sand, A., Barycki, J.J., (2006) J. Biol. Chem., 281, pp. 19029-19037
Hung, C.-P., Yang, J.-C., Chen, J.-H., Chi, M.-C., Lin, L.-L., (2011) J. Biol. Phys., 37, pp. 463-475
Murty, N.A., Tiwary, E., Sharma, R., Nair, N., Gupta, R., (2012) Enzym. Microb. Technol., 50, pp. 159-164
Chang, H.P., Liang, W.C., Lyu, R.C., Chi, M.C., Wang, T.F., Su, K.L., Hung, H.C., Lin, L.L., (2010) Biochemistry (Mosc), 75, pp. 919-929
Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K., (2006) Proc. Natl. Acad. Sci. U. S. A., 103, pp. 6471-6476
Wada, K., Irie, M., Suzuki, H., Fukuyama, K., (2010) FEBS J., 277, pp. 1000-1009
Oinonen, C., Rouvinen, J., (2000) Protein Sci., p. 9
Lee, Y.S., Kim, H.W., Lee, K.B., Park, S.S., (2000) Biochim. Biophys. Acta, 1523, pp. 123-127
Kim, Y., Kim, S., Earnest, T.N., Hol, W.G., (2002) J. Biol. Chem., 277, pp. 2823-2829
West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H., (2013) J. Biol. Chem., 288, pp. 31902-31913
Lin, L.L., Chen, Y.Y., Chi, M.C., Merlino, A., (2014) Biochim. Biophys. Acta, Proteins Proteomics, 1844, pp. 1523-1529
Moallic, C., Dabonne, S., Colas, B., Sine, J.P., (2006) Protein J., 25, pp. 391-397
Castellano, I., Di Salle, A., Merlino, A., Rossi, M., Laara, F., (2011) Extremophiles, 15, pp. 259-270
Chi, M.C., Lo, Y.H., Chen, Y.Y., Lin, L.L., Merlino, A., (2014) Biochim. Biophys. Acta, Proteins Proteomics, 1844, pp. 2290-2297
Lyu, R.C., Hu, H.Y., Kuo, L.Y., Lo, H.F., Ong, P.L., Chang, H.P., Lin, L.L., (2009) Curr. Microbiol., 59, pp. 101-106
Otwinowski, Z., Minor, W., (1997) Methods in Enzymology, 276, pp. 307-326. , ed. J. Charles W. Carter, Academic Press
Emsley, P., Cowtan, K., (2004) Acta Crystallogr. Sect. D: Biol. Crystallogr., 60, pp. 2126-2132
Adams, P.D., Afonine, P.V., Bunkoczi, G., Chen, V.B., Davis, I.W., Echols, N., Headd, J.J., Zwart, P.H., (2010) Acta Crystallogr. Sect. D: Biol. Crystallogr., 66, pp. 213-221
Noren, C.J., Wang, J., Perler, F.B., (2000) Angew. Chem., 39, pp. 450-466
Chi, M.C., Chen, Y.Y., Lo, H.F., Lin, L.L., (2012) FEBS Open Bio, 2, pp. 298-304
Hashimoto, W., Suzuki, H., Nohara, S., Kumagai, H., (1992) Biochem. Biophys. Res. Commun., 189, pp. 173-178
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2016; 1864(2): 195-203.
Tipo di articolo: Journal Article,
Impact factor: 5.476, Impact factor a 5 anni: 5.725
Url: https://www2.scopus.com/inward/record.uri?eid=2-s2.0-84948453364&partnerID=40&md5=6569aec1c5036717080cf6d0ed6aa37a
Parole chiave: Autoprocessing, Single-Point Mutation, X-Ray Crystallography, γ-Glutamyltranspeptidase, γ-Gt Precursor, Alanine, Bacterial Enzyme, Carbonyl Derivative, Enzyme Precursor, Gamma Glutamyltransferase, Hydroxyl Group, Threonine, Article, Bacillus Licheniformis, Controlled Study, Crystal Structure, Enzyme Activity, Enzyme Mechanism, Enzyme Structure, Hydrogen Bond, Nonhuman, Nucleophilicity, Priority Journal, Site Directed Mutagenesis, X Ray Crystallography,
Affiliazioni:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone, 16, Naples, Italy
Department of Applied Chemistry, National Chiayi University, 300 Syuefu Road, Chiayi City, Taiwan
Riferimenti:
Castellano, I., Merlino, A., (2012) Cell. Mol. Life Sci., 69, pp. 3381-339
Stole, E., Smith, T.K., Manning, J.M., Meister, A., (1994) J. Biol. Chem., 269, pp. 21435-21439
Tate, S.S., Meister, A., (1981) Mol. Cell. Biochem., p. 39
Hanigan, M.H., Ricketts, W.A., (1993) Biochemistry, 32, pp. 6302-6306
Taniguchi, N., Ikeda, Y., (1998) Adv. Enzymol. Relat. Areas Mol. Biol., p. 72
Hanigan, M.H., Gallagher, B.C., Townsend, D.M., Gabarra, V., (1999) Carcinogenesis, 20, pp. 553-559
Wilk, S., Mizoguchi, H., Orlowski, M., (1978) J. Pharmacol. Exp. Ther., 206, pp. 227-232
Zhang, Q., Kulczynska, A., Webb, D.J., Megson, I.L., Botting, N.P., (2013) Chem. Commun., 49, pp. 1389-1391
Allison, R.D., (1985) Methods Enzymol., 113, pp. 419-437
Tate, S.S., (1986) FEBS Lett., 194, pp. 33-38
Inoue, M., Hiratake, J., Suzuki, H., Kumagai, H., Sakata, K., (2000) Biochemistry, 39, pp. 7764-7771
Xu, Q., Buckley, D., Guan, C., Guo, H.-C., (1999) Cell, 98, pp. 651-661
Qian, X., Guan, C., Guo, H.-C., (2003) Structure, 11, pp. 997-1003
Kim, Y., Yoon, K.-H., Khang, Y., Turley, S., Hol, W.G., (2000) Structure, 8, pp. 1059-1068
Hewitt, L., Kasche, V., Lummer, K., Lewis, R., Murshudov, G., Verma, C., Dodson, G., Wilson, K., (2000) J. Mol. Biol., 302, pp. 887-898
Ditzel, L., Huber, R., Mann, K., Heinemeyer, W., Wolf, D.H., Groll, M., (1998) J. Mol. Biol., 279, pp. 1187-1191
Bokhove, M., Yoshida, H., Hensgens, C.M., Van Der Laan, J.M., Sutherland, J.D., Dijkstra, B.W., (2010) Structure, 18, pp. 301-308
Minami, H., Suzuki, H., Kumagai, H., (2003) FEMS Microbiol. Lett., 224, pp. 169-173
Boanca, G., Sand, A., Barycki, J.J., (2006) J. Biol. Chem., 281, pp. 19029-19037
Hung, C.-P., Yang, J.-C., Chen, J.-H., Chi, M.-C., Lin, L.-L., (2011) J. Biol. Phys., 37, pp. 463-475
Murty, N.A., Tiwary, E., Sharma, R., Nair, N., Gupta, R., (2012) Enzym. Microb. Technol., 50, pp. 159-164
Chang, H.P., Liang, W.C., Lyu, R.C., Chi, M.C., Wang, T.F., Su, K.L., Hung, H.C., Lin, L.L., (2010) Biochemistry (Mosc), 75, pp. 919-929
Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K., (2006) Proc. Natl. Acad. Sci. U. S. A., 103, pp. 6471-6476
Wada, K., Irie, M., Suzuki, H., Fukuyama, K., (2010) FEBS J., 277, pp. 1000-1009
Oinonen, C., Rouvinen, J., (2000) Protein Sci., p. 9
Lee, Y.S., Kim, H.W., Lee, K.B., Park, S.S., (2000) Biochim. Biophys. Acta, 1523, pp. 123-127
Kim, Y., Kim, S., Earnest, T.N., Hol, W.G., (2002) J. Biol. Chem., 277, pp. 2823-2829
West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H., (2013) J. Biol. Chem., 288, pp. 31902-31913
Lin, L.L., Chen, Y.Y., Chi, M.C., Merlino, A., (2014) Biochim. Biophys. Acta, Proteins Proteomics, 1844, pp. 1523-1529
Moallic, C., Dabonne, S., Colas, B., Sine, J.P., (2006) Protein J., 25, pp. 391-397
Castellano, I., Di Salle, A., Merlino, A., Rossi, M., Laara, F., (2011) Extremophiles, 15, pp. 259-270
Chi, M.C., Lo, Y.H., Chen, Y.Y., Lin, L.L., Merlino, A., (2014) Biochim. Biophys. Acta, Proteins Proteomics, 1844, pp. 2290-2297
Lyu, R.C., Hu, H.Y., Kuo, L.Y., Lo, H.F., Ong, P.L., Chang, H.P., Lin, L.L., (2009) Curr. Microbiol., 59, pp. 101-106
Otwinowski, Z., Minor, W., (1997) Methods in Enzymology, 276, pp. 307-326. , ed. J. Charles W. Carter, Academic Press
Emsley, P., Cowtan, K., (2004) Acta Crystallogr. Sect. D: Biol. Crystallogr., 60, pp. 2126-2132
Adams, P.D., Afonine, P.V., Bunkoczi, G., Chen, V.B., Davis, I.W., Echols, N., Headd, J.J., Zwart, P.H., (2010) Acta Crystallogr. Sect. D: Biol. Crystallogr., 66, pp. 213-221
Noren, C.J., Wang, J., Perler, F.B., (2000) Angew. Chem., 39, pp. 450-466
Chi, M.C., Chen, Y.Y., Lo, H.F., Lin, L.L., (2012) FEBS Open Bio, 2, pp. 298-304
Hashimoto, W., Suzuki, H., Nohara, S., Kumagai, H., (1992) Biochem. Biophys. Res. Commun., 189, pp. 173-178
γ-Glutamyl transpeptidases (γ-GTs) are members of N-terminal nucleophile hydrolase superfamily. They are synthetized as single-chain precursors, which are then cleaved to form mature enzymes. Basic aspects of autocatalytic processing of these pro-enzymes are still unknown. Here we describe the X-ray structure of the precursor mimic of Bacillus licheniformis γ-GT (BlGT), obtained by mutating catalytically important threonine to alanine (T399A-BlGT), and report results of autoprocessing of mutants of His401, Thr415, Thr417, Glu419 and Arg571. Data suggest that Thr417 is in a competent position to activate the catalytic threonine (Thr399) for nucleophilic attack of the scissile peptide bond and that Thr415 plays a major role in assisting the process. On the basis of these new structural results, a possible mechanism of autoprocessing is proposed. This mechanism, which guesses the existence of a six-membered transition state involving one carbonyl and two hydroxyl groups, is in agreement with all the available experimental data collected on γ-GTs from different species and with our new Ala-scanning mutagenesis data. © 2015 Elsevier B.V. All rights reserved.
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Structure (ISSN: 0969-2126, 1878-4186), 2010 Sep 8; 18(9): 1184-1190.
Impact Factor: 6.337
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Di Fiore A, Monti SM, Innocenti A, Winum J-Y, De Simone G, Supuran CT
* Carbonic anhydrase inhibitors: Crystallographic and solution binding studies for the interaction of a boron-containing aromatic sulfamide with mammalian isoforms I-XV (133 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2010 Jun 15; 20(12): 3601-3605.
Impact Factor: 2.661
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De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (184 visite)
Bba-Mol Basis Dis (ISSN: 1570-9639, 0006-3002, 0925-4439), 2010 Feb; 1804(2): 404-409.
Impact Factor: 2.773
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Guler OO, De Simone G, Supuran CT
* Drug design studies of the novel antitumor targets carbonic anhydrase IX and XII (245 visite)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2010; 17(15): 1516-1526.
Impact Factor: 4.63
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Merlino A, Vitagliano L, Howes BD, Verde C, Di Prisco G, Smulevich G, Sica F, Vergara A
* Combined Crystallographic and Spectroscopic Analysis of Trematomus bernacchii Hemoglobin Highlights Analogies and Differences in the Peculiar Oxidation Pathway of Antarctic Fish Hemoglobins (178 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
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Ruggiero A, Masullo M, Marasco D, Ruocco MR, Grimaldi P, Arcari P, Zagari A, Vitagliano L
* The dimeric structure of Sulfolobus solfataricus thioredoxin A2 and the basis of its thermostability (137 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2009 Dec; 77(4): 1004-1008.
Impact Factor: 3.085
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Bellia F, Calabrese V, Guarino F, Cavallaro M, Cornelius C, De Pinto V, Rizzarelli E
* Carnosinase levels in aging brain: redox state induction and cellular stress response (179 visite)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864), 2009 Nov; 11(11): 2759-2775.
Impact Factor: 7.581
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Wekselman I, Davidovich C, Agmon I, Zimmerman E, Rozenberg H, Bashan A, Berisio R, Yonath A
* Ribosome's mode of function: Myths, facts and recent results (154 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 122-130.
Impact Factor: 1.807
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Limauro D, Saviano M, Galdi I, Rossi M, Bartolucci S, Pedone E
* Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (105 visite)
Protein Engineering Design & Selection (ISSN: 1741-0126), 2009 Jan; 22(1): 19-26.
Impact Factor: 2.596
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, Di Fiore A, D'Ambrosio K, Supuran CT, De Simone G
* X-Ray Crystallography of Carbonic Anhydrase Inhibitors and Its Importance in Drug Design (156 visite)
Drug Des Of Zinc Enzyme Inhibitors (ISSN: 9780-4702, 9780-470275009), 2009; N/D: 73-138.
Impact Factor: 1.156
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Merlino A, Sica F, Mazzarella L, Zagari A, Vergara A
* Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)(10) (142 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2008 Sep; 137(1): 24-27.
Impact Factor: 2.362
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Prato S, Vitale RM, Contursi P, Lipps G, Saviano M, Rossi M, Bartolucci S
* Molecular modeling and functional characterization of the monomeric primase-polymerase domain from the Sulfolobus solfataricus plasmid pIT3 (170 visite)
Febs J (ISSN: 1742-464x), 2008; 275(17): 4389-4402.
Impact Factor: 3.139
Dettagli Esporta in BibTeX Esporta in EndNote
Alterio V, De Simone G, Monti SM, Scozzafava A, Supuran CT
* Carbonic anhydrase inhibitors: Inhibition of human, bacterial, and archaeal isozymes with benzene-1, 3-disulfonamides-Solution and crystallographic studies (157 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Sep 1; 17(15): 4201-4207.
Impact Factor: 2.604
Dettagli Esporta in BibTeX Esporta in EndNote
Di Fiore A, Scozzafava A, Winum JY, Montero JL, Pedone C, Supuran CT, De Simone G
* Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties (178 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Mar 15; 17(6): 1726-1731.
Impact Factor: 2.604
Dettagli Esporta in BibTeX Esporta in EndNote
Menchise V, De Simone G, Di Fiore A, Scozzafava A, Supuran CT
* Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1, 3, 4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)1, 3, 4-thiadiazole-2-sulfon amide to human isoform II (136 visite)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Dec 15; 16(24): 6204-6208.
Impact Factor: 2.538
Dettagli Esporta in BibTeX Esporta in EndNote
Di Fiore A, Pedone C, D'Ambrosio K, Scozzafava A, De Simone G, Supuran CT
* Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib (150 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Jan 15; 16(2): 437-442.
Impact Factor: 2.538
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Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (124 visite)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
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Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus (166 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2003 Dec 16; 42(49): 14397-14407.
Impact Factor: 3.922
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal Structure Of The Alcohol Dehydrogenase From The Hyperthermophilic Archaeon Sulfolobus Solfataricus At 1. 85 Angstrom Resolution (149 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
Dettagli Esporta in BibTeX Esporta in EndNote
Esposito L, Vitagliano L, Zagari A, Mazzarella L
Pyramidalization of backbone carbonyl carbon atoms in proteins (147 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Oct; 9(10): 2038-2042.
Impact Factor: 3.869
Dettagli Esporta in BibTeX Esporta in EndNote
47 Records (47 escludendo Abstract e Conferenze).
Impact factor totale: 179.086 (179.086 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 167.613 (167.613 escludendo Abstract e Conferenze).
Impact factor totale: 179.086 (179.086 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 167.613 (167.613 escludendo Abstract e Conferenze).
Esporta in BibTeX Esporta in EndNote
Ultima modifica di Gennaro Angrisano in data Thursday 12 May 2016, 13:21:16
126 visite. Ultima visita in data Friday 06 December 2019, 18:33:48
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