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 (229 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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Ruggiero A, Marasco D, Squeglia F, Soldini S, Pedone E, Pedone C, Berisio R
* Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation (225 visite)
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 (203 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 (249 visite)
Bba-Gen Subjects (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 (320 visite)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2010; 17(15): 1516-1526.
Impact Factor: 4.63
Dettagli Esporta in BibTeX Esporta in EndNote
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 (275 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 (208 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 (268 visite)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864, 1523-0864linking), 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 (237 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 (147 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 (247 visite)
Drug Des Of Zinc Enzyme Inhibitors (ISSN: 9780-4702, 9780-470275009), 2009; N/D: 73-138.
Impact Factor: 1.156
Dettagli Esporta in BibTeX Esporta in EndNote
Merlino A, Sica F, Mazzarella L, Zagari A, Vergara A
* Correlation between Raman and X-ray crystallography data of (Pro-Pro-Gly)(10) (291 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 (255 visite)
Febs J (ISSN: 1742-464x), 2008; 275(17): 4389-4402.
Impact Factor: 3.139
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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 (224 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Sep 1; 17(15): 4201-4207.
Impact Factor: 2.604
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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 (290 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Mar 15; 17(6): 1726-1731.
Impact Factor: 2.604
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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 (194 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 (215 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 (216 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 (248 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 (275 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 (303 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 Sunday 12 July 2020, 13:14:47
229 visite. Ultima visita in data Monday 14 September 2020, 11:38:48
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