Making and Breaking Peptide Bonds: Protein Engineering Using Sortase
Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a r...
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Published in | Angewandte Chemie (International ed.) Vol. 50; no. 22; pp. 5024 - 5032 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Weinheim
WILEY-VCH Verlag
23.05.2011
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Edition | International ed. in English |
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Abstract | Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a range of applications, from chemistry‐based to cell biology and technology. In this Minireview we provide a brief overview of the biology of sortase enzymes and current applications in protein engineering. We identify areas that lend themselves to further innovation and that suggest new applications.
It takes all sortases: Enzymatic formation of a peptide bond using the sortase A transpeptidase (SrtA) provides a convenient and mild means for engineering proteins to contain nongenetically templated modifications. Myriad applications are possible, from producing homogeneous post‐translational modification mimics, assembling protein domains, to anchoring proteins to solid surfaces. |
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AbstractList | Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site-specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a range of applications, from chemistry-based to cell biology and technology. In this Minireview we provide a brief overview of the biology of sortase enzymes and current applications in protein engineering. We identify areas that lend themselves to further innovation and that suggest new applications. Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a range of applications, from chemistry‐based to cell biology and technology. In this Minireview we provide a brief overview of the biology of sortase enzymes and current applications in protein engineering. We identify areas that lend themselves to further innovation and that suggest new applications. It takes all sortases: Enzymatic formation of a peptide bond using the sortase A transpeptidase (SrtA) provides a convenient and mild means for engineering proteins to contain nongenetically templated modifications. Myriad applications are possible, from producing homogeneous post‐translational modification mimics, assembling protein domains, to anchoring proteins to solid surfaces. Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site-specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a range of applications, from chemistry-based to cell biology and technology. In this Minireview we provide a brief overview of the biology of sortase enzymes and current applications in protein engineering. We identify areas that lend themselves to further innovation and that suggest new applications. [PUBLICATION ABSTRACT] Abstract Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then reform a new bond with an incoming nucleophile that makes sortase an attractive tool for protein engineering. This technique has been adopted for a range of applications, from chemistry‐based to cell biology and technology. In this Minireview we provide a brief overview of the biology of sortase enzymes and current applications in protein engineering. We identify areas that lend themselves to further innovation and that suggest new applications. |
Author | Ploegh, Hidde L. Popp, Maximilian Wei-Lin |
Author_xml | – sequence: 1 givenname: Maximilian Wei-Lin surname: Popp fullname: Popp, Maximilian Wei-Lin organization: Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142 (USA) – sequence: 2 givenname: Hidde L. surname: Ploegh fullname: Ploegh, Hidde L. email: ploegh@wi.mit.edu organization: Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142 (USA) |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21538739$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1021/bc060339w 10.1046/j.1365-2958.2001.02411.x 10.1002/ange.200705718 10.1073/pnas.96.22.12424 10.1023/A:1011299500628 10.1016/j.tim.2007.10.010 10.1074/jbc.M109945200 10.1016/j.jbiotec.2005.09.012 10.1073/pnas.0806350105 10.1126/science.285.5428.760 10.1021/bi100094g 10.1128/iai.60.5.1902-1907.1992 10.1074/jbc.M806796200 10.1039/c0cc00828a 10.1002/psc.1264 10.1007/s10529-008-9718-1 10.1039/b818792d 10.1073/pnas.101064198 10.1111/j.1365-2958.2006.05279.x 10.1128/IAI.73.8.5222-5228.2005 10.1124/pr.107.07110 10.1002/anie.200705718 10.1007/s10529-010-0349-y 10.1021/ja903231v 10.1016/S0968-0004(02)02057-1 10.1128/JB.186.17.5865-5875.2004 10.1016/j.str.2008.10.007 10.1016/S0076-6879(10)78023-X 10.1007/s00018-008-8477-4 10.1126/science.1125248 10.1021/bi901261y 10.1074/jbc.M109.066282 10.1021/bi901557a 10.1074/jbc.M109194200 10.1021/bc100206z 10.1074/jbc.M405282200 10.1073/pnas.0504613102 10.1128/IAI.72.5.2710-2722.2004 10.1128/JB.01011-06 10.1016/j.ab.2003.10.023 10.1074/jbc.M805406200 10.1074/jbc.M506123200 10.1021/ja039915e 10.1016/j.pep.2004.06.013 10.1074/jbc.M610519200 10.1016/j.micinf.2005.06.009 10.1074/jbc.M901752200 10.1074/jbc.M800974200 10.1021/ja906611x 10.1128/IAI.69.6.4019-4026.2001 10.1016/j.ab.2006.10.021 10.1371/journal.pone.0001164 10.1074/jbc.M500071200 10.1074/jbc.275.13.9876 10.1021/bi034391g 10.1073/pnas.0803565105 10.1007/s10858-010-9464-2 10.1016/j.cell.2010.09.031 10.1002/cbic.200700614 10.1016/j.jmb.2009.08.058 10.1038/nchembio.2007.31 10.1021/bi035920j 10.1016/0092-8674(92)90101-H 10.1021/bi700448e 10.1111/j.1365-2958.2004.04117.x 10.1021/cb100195d 10.1073/pnas.032523999 10.1016/j.febslet.2004.06.070 10.1021/ja077358g 10.1074/jbc.M110.135434 10.1016/j.tim.2004.03.004 10.1016/j.pep.2009.10.012 10.1021/ja902681k 10.1021/ja806779e 10.1186/1472-6750-10-42 10.1073/pnas.080520697 10.1074/jbc.M305245200 10.1021/bi050141j 10.1016/j.tim.2003.12.007 10.1002/anie.201000620 10.1128/JB.187.13.4646-4655.2005 10.1074/jbc.M401374200 10.1074/jbc.M109.022624 10.1016/S0966-842X(01)01956-4 10.1128/JB.187.14.4928-4934.2005 10.1002/pmic.200402075 10.1021/jo062331l 10.1002/ange.201000620 10.1128/MMBR.70.1.192-221.2006 10.1016/j.resmic.2004.10.011 10.1046/j.1365-2958.2003.03782.x 10.1074/jbc.274.34.24316 10.1074/jbc.M807172200 10.1007/s10858-008-9296-5 10.2174/138955707782110097 |
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PublicationDecade | 2010 |
PublicationPlace | Weinheim |
PublicationPlace_xml | – name: Weinheim – name: Germany |
PublicationTitle | Angewandte Chemie (International ed.) |
PublicationTitleAlternate | Angew. Chem. Int. Ed |
PublicationYear | 2011 |
Publisher | WILEY-VCH Verlag WILEY‐VCH Verlag Wiley Subscription Services, Inc |
Publisher_xml | – name: WILEY-VCH Verlag – name: WILEY‐VCH Verlag – name: Wiley Subscription Services, Inc |
References | J. Caswell, P. Snoddy, D. McMeel, R. J. Buick, C. J. Scott, Protein Expression Purif. 2010, 70, 143. S. Pritz, Y. Wolf, O. Kraetke, J. Klose, M. Bienert, M. Beyermann, J. Org. Chem. 2007, 72, 3909. G. K. Paterson, T. J. Mitchell, Trends Microbiol. 2004, 12, 89. A. S. Andersen, E. Palmqvist, S. Bang, A. C. Shaw, F. Hubalek, U. Ribel, T. Hoeg-Jensen, J. Pept. Sci. 2010, 16, 473. A. Aulabaugh, W. Ding, B. Kapoor, K. Tabei, L. Alksne, R. Dushin, T. Zatz, G. Ellestad, X. Huang, Anal. Biochem. 2007, 360, 14. P. R. Race, M. L. Bentley, J. A. Melvin, A. Crow, R. K. Hughes, W. D. Smith, R. B. Sessions, M. A. Kehoe, D. G. McCafferty, M. J. Banfield, J. Biol. Chem. 2009, 284, 6924. Y. Kobashigawa, H. Kumeta, K. Ogura, F. Inagaki, J. Biomol. NMR 2009, 43, 145. B. A. Frankel, Y. Tong, M. L. Bentley, M. C. Fitzgerald, D. G. McCafferty, Biochemistry 2007, 46, 7269. N. Hirota, D. Yasuda, T. Hashidate, T. Yamamoto, S. Yamaguchi, T. Nagamune, T. Nagase, T. Shimizu, M. Nakamura, J. Biol. Chem. 2010, 285, 5931. H. Mao, Protein Expression Purif. 2004, 37, 253. T. C. Barnett, A. R. Patel, J. R. Scott, J. Bacteriol. 2004, 186, 5865. S. D. Zink, D. L. Burns, Infect. Immun. 2005, 73, 5222. J. M. Antos, G. M. Miller, G. M. Grotenbreg, H. L. Ploegh, J. Am. Chem. Soc. 2008, 130, 16338. M. J. Pallen, A. C. Lam, M. Antonio, K. Dunbar, Trends Microbiol. 2001, 9, 97. B. A. Frankel, R. G. Kruger, D. E. Robinson, N. L. Kelleher, D. G. McCafferty, Biochemistry 2005, 44, 11188. C. Manzano, T. Izore, V. Job, A. M. Di Guilmi, A. Dessen, Biochemistry 2009, 48, 10549. R. G. Kruger, B. Otvos, B. A. Frankel, M. Bentley, P. Dostal, D. G. McCafferty, Biochemistry 2004, 43, 1541. L. A. Marraffini, A. C. Dedent, O. Schneewind, Microbiol. Mol. Biol. Rev. 2006, 70, 192. G. Pozzi, M. Contorni, M. R. Oggioni, R. Manganelli, M. Tommasino, F. Cavalieri, V. A. Fischetti, Infect. Immun. 1992, 60, 1902. S. Pritz, O. Kraetke, A. Klose, J. Klose, S. Rothemund, K. Fechner, M. Bienert, M. Beyermann, Angew. Chem. 2008, 120, 3698 T. Ito, R. Sadamoto, K. Naruchi, H. Togame, H. Takemoto, H. Kondo, S. Nishimura, Biochemistry 2010, 49, 2604. G. K. Paterson, T. J. Mitchell, Microbes Infect. 2006, 8, 145. M. Trabi, D. J. Craik, Trends Biochem. Sci. 2002, 27, 132. M. A. Refaei, A. Combs, D. J. Kojetin, J. Cavanagh, C. Caperelli, M. Rance, J. Sapitro, P. Tsang, J. Biomol. NMR 2011, 49, 3. L. A. Marraffini, O. Schneewind, J. Biol. Chem. 2005, 280, 16263. S. K. Mazmanian, G. Liu, E. R. Jensen, E. Lenoy, O. Schneewind, Proc. Natl. Acad. Sci. USA 2000, 97, 5510. T. Matsushita, S. Nishimura, Methods Enzymol. 2010, 478, 485. E. M. Weiner, S. Robson, M. Marohn, R. T. Clubb, J. Biol. Chem. 2010, 285, 23433. M. W. Popp, J. M. Antos, G. M. Grotenbreg, E. Spooner, H. L. Ploegh, Nat. Chem. Biol. 2007, 3, 707. Angew. Chem. Int. Ed. 2008, 47, 3642. N. Suree, M. E. Jung, R. T. Clubb, Mini-Rev. Med. Chem. 2007, 7, 991. M. T. Naik, N. Suree, U. Ilangovan, C. K. Liew, W. Thieu, D. O. Campbell, J. J. Clemens, M. E. Jung, R. T. Clubb, J. Biol. Chem. 2006, 281, 1817. M. G. Pucciarelli, E. Calvo, C. Sabet, H. Bierne, P. Cossart, F. Garcia-del Portillo, Proteomics 2005, 5, 4808. T. Sakamoto, S. Sawamoto, T. Tanaka, H. Fukuda, A. Kondo, Bioconjugate Chem. 2010, 21, 2227. D. J. Craik, Science 2006, 311, 1563. F. Clow, J. D. Fraser, T. Proft, Biotechnol. Lett. 2008, 30, 1603. U. Ilangovan, H. Ton-That, J. Iwahara, O. Schneewind, R. T. Clubb, Proc. Natl. Acad. Sci. USA 2001, 98, 6056. R. J. Clark, H. Fischer, L. Dempster, N. L. Daly, K. J. Rosengren, S. T. Nevin, F. A. Meunier, D. J. Adams, D. J. Craik, Proc. Natl. Acad. Sci. USA 2005, 102, 13767. R. J. Clark, J. Jensen, S. T. Nevin, B. P. Callaghan, D. J. Adams, D. J. Craik, Angew. Chem. 2010, 122, 6695 A. Mandlik, A. Das, H. Ton-That, Proc. Natl. Acad. Sci. USA 2008, 105, 14147. M. W. Popp, K. Artavanis-Tsakonas, H. L. Ploegh, J. Biol. Chem. 2009, 284, 3593. J. M. Antos, M. W. Popp, R. Ernst, G. L. Chew, E. Spooner, H. L. Ploegh, J. Biol. Chem. 2009, 284, 16028. J. M. Budzik, S. Y. Oh, O. Schneewind, J. Biol. Chem. 2008, 283, 36676. F. Neiers, C. Madhurantakam, S. Falker, C. Manzano, A. Dessen, S. Normark, B. Henriques-Normark, A. Achour, J. Mol. Biol. 2009, 393, 704. H. Mao, S. A. Hart, A. Schink, B. A. Pollok, J. Am. Chem. Soc. 2004, 126, 2670. A. H. Gaspar, L. A. Marraffini, E. M. Glass, K. L. Debord, H. Ton-That, O. Schneewind, J. Bacteriol. 2005, 187, 4646. X. Huang, A. Aulabaugh, W. Ding, B. Kapoor, L. Alksne, K. Tabei, G. Ellestad, Biochemistry 2003, 42, 11307. S. K. Mazmanian, H. Ton-That, K. Su, O. Schneewind, Proc. Natl. Acad. Sci. USA 2002, 99, 2293. H. Ton-That, O. Schneewind, Mol. Microbiol. 2003, 50, 1429. H. D. Nguyen, W. Schumann, J. Biotechnol. 2006, 122, 473. T. Tanaka, T. Yamamoto, S. Tsukiji, T. Nagamune, ChemBioChem 2008, 9, 802. Z. Wu, X. Guo, Q. Wang, B. M. Swarts, Z. Guo, J. Am. Chem. Soc. 2010, 132, 1567. U. Ilangovan, J. Iwahara, H. Ton-That, O. Schneewind, R. T. Clubb, J. Biomol. NMR 2001, 19, 379. M. Vila-Perelló, T. W. Muir, Cell 2010, 143, 191. H. Ton-That, G. Liu, S. K. Mazmanian, K. F. Faull, O. Schneewind, Proc. Natl. Acad. Sci. USA 1999, 96, 12424. Z. Wu, X. Guo, Z. Guo, Chem. Commun. 2010, 46, 5773. A. W. Maresso, O. Schneewind, Pharmacol. Rev. 2008, 60, 128. L. Chan, H. F. Cross, J. K. She, G. Cavalli, H. F. Martins, C. Neylon, PLoS One 2007, 2, e1164. H. Ton-That, S. K. Mazmanian, L. Alksne, O. Schneewind, J. Biol. Chem. 2002, 277, 7447. H. Ton-That, O. Schneewind, J. Biol. Chem. 1999, 274, 24316. D. Comfort, R. T. Clubb, Infect. Immun. 2004, 72, 2710. C. Manzano, C. Contreras-Martel, L. El Mortaji, T. Izore, D. Fenel, T. Vernet, G. Schoehn, A. M. Di Guilmi, A. Dessen, Structure 2008, 16, 1838. A. Mandlik, A. Swierczynski, A. Das, H. Ton-That, Trends Microbiol. 2008, 16, 33. H. Ton-That, O. Schneewind, Trends Microbiol. 2004, 12, 228. J. M. Budzik, L. A. Marraffini, P. Souda, J. P. Whitelegge, K. F. Faull, O. Schneewind, Proc. Natl. Acad. Sci. USA 2008, 105, 10215. M. L. Bentley, H. Gaweska, J. M. Kielec, D. G. McCafferty, J. Biol. Chem. 2007, 282, 6571. J. W. Nelson, A. G. Chamessian, P. J. McEnaney, R. P. Murelli, B. I. Kazmiercak, D. A. Spiegel, ACS Chem. Biol. 2010, 5, 1147. J. M. Antos, G. L. Chew, C. P. Guimaraes, N. C. Yoder, G. M. Grotenbreg, M. W. Popp, H. L. Ploegh, J. Am. Chem. Soc. 2009, 131, 10800. J. Boekhorst, M. W. de Been, M. Kleerebezem, R. J. Siezen, J. Bacteriol. 2005, 187, 4928. R. Janulczyk, M. Rasmussen, Infect. Immun. 2001, 69, 4019. L. A. Marraffini, H. Ton-That, Y. Zong, S. V. Narayana, O. Schneewind, J. Biol. Chem. 2004, 279, 37763. S. Samantaray, U. Marathe, S. Dasgupta, V. K. Nandicoori, R. P. Roy, J. Am. Chem. Soc. 2008, 130, 2132. N. Suree, C. K. Liew, V. A. Villareal, W. Thieu, E. A. Fadeev, J. J. Clemens, M. E. Jung, R. T. Clubb, J. Biol. Chem. 2009, 284, 24465. A. W. Maresso, T. J. Chapa, O. Schneewind, J. Bacteriol. 2006, 188, 8145. S. Wu, T. Proft, Biotechnol. Lett. 2010, 32, 1713. S. K. Mazmanian, H. Ton-That, O. Schneewind, Mol. Microbiol. 2001, 40, 1049. H. Ton-That, S. K. Mazmanian, K. F. Faull, O. Schneewind, J. Biol. Chem. 2000, 275, 9876. O. Schneewind, P. Model, V. A. Fischetti, Cell 1992, 70, 267. M. L. Bentley, E. C. Lamb, D. G. McCafferty, J. Biol. Chem. 2008, 283, 14762. Y. Zong, T. W. Bice, H. Ton-That, O. Schneewind, S. V. Narayana, J. Biol. Chem. 2004, 279, 31383. T. Matsushita, R. Sadamoto, N. Ohyabu, H. Nakata, M. Fumoto, N. Fujitani, Y. Takegawa, T. Sakamoto, M. Kurogochi, H. Hinou, H. Shimizu, T. Ito, K. Naruchi, H. Togame, H. Takemoto, H. Kondo, S. Nishimura, Biochemistry 2009, 48, 11117. T. Proft, E. N. Baker, Cell. Mol. Life Sci. 2009, 66, 613. S. Dramsi, P. Trieu-Cuot, H. Bierne, Res. Microbiol. 2005, 156, 289. Angew. Chem. Int. Ed. 2010, 49, 6545. R. Parthasarathy, S. Subramanian, E. T. Boder, Bioconjugate Chem. 2007, 18, 469. J. R. Scott, D. Zahner, Mol. Microbiol. 2006, 62, 320. X. Guo, Q. Wang, B. M. Swarts, Z. Guo, J. Am. Chem. Soc. 2009, 131, 9878. K. M. Connolly, B. T. Smith, R. Pilpa, U. Ilangovan, M. E. Jung, R. T. Clubb, J. Biol. Chem. 2003, 278, 34061. H. Ton-That, L. A. Marraffini, O. Schneewind, Mol. Microbiol. 2004, 53, 251. C. K. Liew, B. T. Smith, R. Pilpa, N. Suree, U. Ilangovan, K. M. Connolly, M. E. Jung, R. T. Clubb, FEBS Lett. 2004, 571, 221. S. K. Mazmanian, G. Liu, H. Ton-That, O. Schneewind, Science 1999, 285, 760. R. G. Kruger, P. Dostal, D. G. McCafferty, Anal. Biochem. 2004, 326, 42. A. M. Perry, H. Ton-That, S. K. Mazmanian, O. Schneewind, J. Biol. Chem. 2002, 277, 16241. T. Yamamoto, T. Nagamune, Chem. Commun. 2009, 1022. S. Matsunaga, K. Matsuoka, K. Shimizu, Y. Endo, T. Sawasaki, BMC Biotechnol. 2010, 10, 42. 2006; 70 2010; 10 2010; 16 2004; 126 2009; 43 2002; 277 2010 2010; 122 49 2002; 99 1999; 285 2008; 9 2010; 143 2008; 105 2009; 393 2007; 72 2008; 30 2003; 50 2003; 278 2004; 326 2001; 40 2009; 48 2010; 21 2004; 571 2004; 72 2006; 62 2005; 187 2005; 102 2010; 478 2004; 37 2000; 97 2005; 73 2001; 19 2007; 7 1999; 96 2009; 284 2007; 2 2007; 3 2006; 281 2010; 70 2010; 5 2008; 60 2003; 42 2006; 122 2001; 98 2004; 43 2009; 66 2007; 18 2010; 32 2004; 186 2007; 282 2007; 360 2005; 156 2008; 16 2009 2006; 8 2010; 285 2000; 275 2009; 131 2001; 69 2005; 44 2008; 283 2006; 311 2002; 27 2005; 280 2004; 53 1992; 70 2010; 49 2004; 279 2010; 46 2001; 9 2004; 12 1999; 274 2005; 5 2010; 132 2011; 49 2008 2008; 120 47 2007; 46 1992; 60 2008; 130 2006; 188 e_1_2_11_93_2 e_1_2_11_70_2 e_1_2_11_55_2 e_1_2_11_78_2 e_1_2_11_13_2 e_1_2_11_51_2 e_1_2_11_97_2 e_1_2_11_32_2 e_1_2_11_74_2 e_1_2_11_4_2 e_1_2_11_25_2 e_1_2_11_48_2 e_1_2_11_29_2 e_1_2_11_81_2 e_1_2_11_20_2 e_1_2_11_43_2 e_1_2_11_66_2 e_1_2_11_89_2 e_1_2_11_24_2 e_1_2_11_62_2 e_1_2_11_85_2 e_1_2_11_8_2 e_1_2_11_17_2 e_1_2_11_36_2 e_1_2_11_59_2 e_1_2_11_92_2 e_1_2_11_31_2 e_1_2_11_54_2 e_1_2_11_77_2 e_1_2_11_35_2 e_1_2_11_50_2 e_1_2_11_73_2 e_1_2_11_96_2 e_1_2_11_12_2 e_1_2_11_28_2 e_1_2_11_5_2 e_1_2_11_47_2 e_1_2_11_1_2 e_1_2_11_80_2 e_1_2_11_65_2 e_1_2_11_46_2 e_1_2_11_88_2 e_1_2_11_9_2 e_1_2_11_23_2 e_1_2_11_61_2 e_1_2_11_42_2 e_1_2_11_84_2 e_1_2_11_16_2 e_1_2_11_58_2 e_1_2_11_39_2 e_1_2_11_91_2 e_1_2_11_30_2 e_1_2_11_76_2 e_1_2_11_57_2 e_1_2_11_72_3 e_1_2_11_34_2 e_1_2_11_72_2 e_1_2_11_11_2 e_1_2_11_53_2 e_1_2_11_95_2 e_1_2_11_6_2 e_1_2_11_27_2 e_1_2_11_2_2 e_1_2_11_69_2 e_1_2_11_60_2 e_1_2_11_45_2 e_1_2_11_68_2 e_1_2_11_87_2 e_1_2_11_22_2 e_1_2_11_41_2 e_1_2_11_64_2 e_1_2_11_83_2 e_1_2_11_15_2 e_1_2_11_19_2 e_1_2_11_38_2 e_1_2_11_71_2 e_1_2_11_90_2 e_1_2_11_75_3 e_1_2_11_56_2 e_1_2_11_79_2 e_1_2_11_33_2 e_1_2_11_52_2 e_1_2_11_75_2 e_1_2_11_94_2 e_1_2_11_10_2 e_1_2_11_26_2 e_1_2_11_3_2 e_1_2_11_49_2 e_1_2_11_82_2 e_1_2_11_44_2 e_1_2_11_67_2 e_1_2_11_40_2 e_1_2_11_86_2 e_1_2_11_7_2 e_1_2_11_21_2 e_1_2_11_63_2 e_1_2_11_14_2 e_1_2_11_37_2 e_1_2_11_18_2 |
References_xml | – volume: 43 start-page: 1541 year: 2004 publication-title: Biochemistry – volume: 9 start-page: 97 year: 2001 publication-title: Trends Microbiol. – volume: 46 start-page: 7269 year: 2007 publication-title: Biochemistry – volume: 9 start-page: 802 year: 2008 publication-title: ChemBioChem – volume: 282 start-page: 6571 year: 2007 publication-title: J. Biol. Chem. – volume: 188 start-page: 8145 year: 2006 publication-title: J. Bacteriol. – volume: 8 start-page: 145 year: 2006 publication-title: Microbes Infect. – volume: 37 start-page: 253 year: 2004 publication-title: Protein Expression Purif. – volume: 16 start-page: 33 year: 2008 publication-title: Trends Microbiol. – volume: 131 start-page: 10800 year: 2009 publication-title: J. Am. Chem. Soc. – volume: 70 start-page: 143 year: 2010 publication-title: Protein Expression Purif. – volume: 277 start-page: 7447 year: 2002 publication-title: J. Biol. Chem. – volume: 275 start-page: 9876 year: 2000 publication-title: J. Biol. Chem. – volume: 7 start-page: 991 year: 2007 publication-title: Mini‐Rev. Med. Chem. – volume: 279 start-page: 31383 year: 2004 publication-title: J. Biol. Chem. – volume: 105 start-page: 10215 year: 2008 publication-title: Proc. Natl. Acad. Sci. USA – volume: 122 start-page: 473 year: 2006 publication-title: J. Biotechnol. – volume: 96 start-page: 12424 year: 1999 publication-title: Proc. Natl. Acad. Sci. USA – volume: 284 start-page: 3593 year: 2009 publication-title: J. Biol. Chem. – volume: 186 start-page: 5865 year: 2004 publication-title: J. Bacteriol. – volume: 131 start-page: 9878 year: 2009 publication-title: J. Am. Chem. Soc. – volume: 311 start-page: 1563 year: 2006 publication-title: Science – volume: 285 start-page: 23433 year: 2010 publication-title: J. Biol. Chem. – volume: 72 start-page: 3909 year: 2007 publication-title: J. Org. Chem. – start-page: 1022 year: 2009 publication-title: Chem. Commun. – volume: 360 start-page: 14 year: 2007 publication-title: Anal. Biochem. – volume: 53 start-page: 251 year: 2004 publication-title: Mol. Microbiol. – volume: 284 start-page: 6924 year: 2009 publication-title: J. Biol. Chem. – volume: 120 47 start-page: 3698 3642 year: 2008 2008 publication-title: Angew. Chem. Angew. Chem. Int. Ed. – volume: 46 start-page: 5773 year: 2010 publication-title: Chem. Commun. – volume: 132 start-page: 1567 year: 2010 publication-title: J. Am. Chem. Soc. – volume: 280 start-page: 16263 year: 2005 publication-title: J. Biol. Chem. – volume: 274 start-page: 24316 year: 1999 publication-title: J. Biol. Chem. – volume: 279 start-page: 37763 year: 2004 publication-title: J. Biol. Chem. – volume: 73 start-page: 5222 year: 2005 publication-title: Infect. Immun. – volume: 278 start-page: 34061 year: 2003 publication-title: J. Biol. Chem. – volume: 72 start-page: 2710 year: 2004 publication-title: Infect. Immun. – volume: 49 start-page: 3 year: 2011 publication-title: J. Biomol. NMR – volume: 97 start-page: 5510 year: 2000 publication-title: Proc. Natl. Acad. Sci. USA – volume: 18 start-page: 469 year: 2007 publication-title: Bioconjugate Chem. – volume: 478 start-page: 485 year: 2010 publication-title: Methods Enzymol. – volume: 284 start-page: 16028 year: 2009 publication-title: J. Biol. Chem. – volume: 21 start-page: 2227 year: 2010 publication-title: Bioconjugate Chem. – volume: 571 start-page: 221 year: 2004 publication-title: FEBS Lett. – volume: 42 start-page: 11307 year: 2003 publication-title: Biochemistry – volume: 283 start-page: 14762 year: 2008 publication-title: J. Biol. Chem. – volume: 187 start-page: 4646 year: 2005 publication-title: J. Bacteriol. – volume: 69 start-page: 4019 year: 2001 publication-title: Infect. Immun. – volume: 60 start-page: 1902 year: 1992 publication-title: Infect. Immun. – volume: 130 start-page: 16338 year: 2008 publication-title: J. Am. Chem. Soc. – volume: 32 start-page: 1713 year: 2010 publication-title: Biotechnol. Lett. – volume: 285 start-page: 760 year: 1999 publication-title: Science – volume: 60 start-page: 128 year: 2008 publication-title: Pharmacol. Rev. – volume: 44 start-page: 11188 year: 2005 publication-title: Biochemistry – volume: 102 start-page: 13767 year: 2005 publication-title: Proc. Natl. Acad. Sci. USA – volume: 283 start-page: 36676 year: 2008 publication-title: J. Biol. Chem. – volume: 66 start-page: 613 year: 2009 publication-title: Cell. Mol. Life Sci. – volume: 3 start-page: 707 year: 2007 publication-title: Nat. Chem. Biol. – volume: 187 start-page: 4928 year: 2005 publication-title: J. Bacteriol. – volume: 43 start-page: 145 year: 2009 publication-title: J. Biomol. NMR – volume: 16 start-page: 473 year: 2010 publication-title: J. Pept. Sci. – volume: 62 start-page: 320 year: 2006 publication-title: Mol. Microbiol. – volume: 277 start-page: 16241 year: 2002 publication-title: J. Biol. Chem. – volume: 30 start-page: 1603 year: 2008 publication-title: Biotechnol. Lett. – volume: 326 start-page: 42 year: 2004 publication-title: Anal. Biochem. – volume: 98 start-page: 6056 year: 2001 publication-title: Proc. Natl. Acad. Sci. USA – volume: 285 start-page: 5931 year: 2010 publication-title: J. Biol. Chem. – volume: 12 start-page: 89 year: 2004 publication-title: Trends Microbiol. – volume: 126 start-page: 2670 year: 2004 publication-title: J. Am. Chem. Soc. – volume: 5 start-page: 4808 year: 2005 publication-title: Proteomics – volume: 40 start-page: 1049 year: 2001 publication-title: Mol. Microbiol. – volume: 156 start-page: 289 year: 2005 publication-title: Res. Microbiol. – volume: 143 start-page: 191 year: 2010 publication-title: Cell – volume: 130 start-page: 2132 year: 2008 publication-title: J. Am. Chem. Soc. – volume: 50 start-page: 1429 year: 2003 publication-title: Mol. Microbiol. – volume: 281 start-page: 1817 year: 2006 publication-title: J. Biol. Chem. – volume: 284 start-page: 24465 year: 2009 publication-title: J. Biol. Chem. – volume: 99 start-page: 2293 year: 2002 publication-title: Proc. Natl. Acad. Sci. USA – volume: 48 start-page: 10549 year: 2009 publication-title: Biochemistry – volume: 122 49 start-page: 6695 6545 year: 2010 2010 publication-title: Angew. Chem. Angew. Chem. Int. Ed. – volume: 12 start-page: 228 year: 2004 publication-title: Trends Microbiol. – volume: 5 start-page: 1147 year: 2010 publication-title: ACS Chem. Biol. – volume: 27 start-page: 132 year: 2002 publication-title: Trends Biochem. Sci. – volume: 19 start-page: 379 year: 2001 publication-title: J. Biomol. NMR – volume: 48 start-page: 11117 year: 2009 publication-title: Biochemistry – volume: 49 start-page: 2604 year: 2010 publication-title: Biochemistry – volume: 393 start-page: 704 year: 2009 publication-title: J. Mol. Biol. – volume: 70 start-page: 192 year: 2006 publication-title: Microbiol. Mol. Biol. Rev. – volume: 10 start-page: 42 year: 2010 publication-title: BMC Biotechnol. – volume: 105 start-page: 14147 year: 2008 publication-title: Proc. Natl. Acad. Sci. USA – volume: 70 start-page: 267 year: 1992 publication-title: Cell – volume: 2 start-page: 1164 year: 2007 publication-title: PLoS One – volume: 16 start-page: 1838 year: 2008 publication-title: Structure – ident: e_1_2_11_56_2 doi: 10.1021/bc060339w – ident: e_1_2_11_3_2 doi: 10.1046/j.1365-2958.2001.02411.x – ident: e_1_2_11_72_2 doi: 10.1002/ange.200705718 – ident: e_1_2_11_6_2 doi: 10.1073/pnas.96.22.12424 – ident: e_1_2_11_37_2 doi: 10.1023/A:1011299500628 – ident: e_1_2_11_20_2 doi: 10.1016/j.tim.2007.10.010 – ident: e_1_2_11_45_2 doi: 10.1074/jbc.M109945200 – ident: e_1_2_11_51_2 doi: 10.1016/j.jbiotec.2005.09.012 – ident: e_1_2_11_28_2 doi: 10.1073/pnas.0806350105 – ident: e_1_2_11_2_2 doi: 10.1126/science.285.5428.760 – ident: e_1_2_11_82_2 doi: 10.1021/bi100094g – ident: e_1_2_11_50_2 doi: 10.1128/iai.60.5.1902-1907.1992 – ident: e_1_2_11_91_2 doi: 10.1074/jbc.M806796200 – ident: e_1_2_11_65_2 doi: 10.1039/c0cc00828a – ident: e_1_2_11_78_2 doi: 10.1002/psc.1264 – ident: e_1_2_11_81_2 doi: 10.1007/s10529-008-9718-1 – ident: e_1_2_11_59_2 doi: 10.1039/b818792d – ident: e_1_2_11_38_2 doi: 10.1073/pnas.101064198 – ident: e_1_2_11_19_2 doi: 10.1111/j.1365-2958.2006.05279.x – ident: e_1_2_11_4_2 doi: 10.1128/IAI.73.8.5222-5228.2005 – ident: e_1_2_11_31_2 doi: 10.1124/pr.107.07110 – ident: e_1_2_11_72_3 doi: 10.1002/anie.200705718 – ident: e_1_2_11_79_2 doi: 10.1007/s10529-010-0349-y – ident: e_1_2_11_63_2 doi: 10.1021/ja903231v – ident: e_1_2_11_76_2 doi: 10.1016/S0968-0004(02)02057-1 – ident: e_1_2_11_86_2 doi: 10.1128/JB.186.17.5865-5875.2004 – ident: e_1_2_11_24_2 doi: 10.1016/j.str.2008.10.007 – ident: e_1_2_11_70_2 doi: 10.1016/S0076-6879(10)78023-X – ident: e_1_2_11_21_2 doi: 10.1007/s00018-008-8477-4 – ident: e_1_2_11_77_2 doi: 10.1126/science.1125248 – ident: e_1_2_11_26_2 doi: 10.1021/bi901261y – ident: e_1_2_11_60_2 doi: 10.1074/jbc.M109.066282 – ident: e_1_2_11_71_2 doi: 10.1021/bi901557a – ident: e_1_2_11_17_2 doi: 10.1074/jbc.M109194200 – ident: e_1_2_11_69_2 doi: 10.1021/bc100206z – ident: e_1_2_11_42_2 doi: 10.1074/jbc.M405282200 – ident: e_1_2_11_74_2 doi: 10.1073/pnas.0504613102 – ident: e_1_2_11_10_2 doi: 10.1128/IAI.72.5.2710-2722.2004 – ident: e_1_2_11_89_2 doi: 10.1128/JB.01011-06 – ident: e_1_2_11_41_2 doi: 10.1016/j.ab.2003.10.023 – ident: e_1_2_11_61_2 doi: 10.1074/jbc.M805406200 – ident: e_1_2_11_44_2 doi: 10.1074/jbc.M506123200 – ident: e_1_2_11_55_2 doi: 10.1021/ja039915e – ident: e_1_2_11_83_2 doi: 10.1016/j.pep.2004.06.013 – ident: e_1_2_11_95_2 doi: 10.1074/jbc.M610519200 – ident: e_1_2_11_33_2 doi: 10.1016/j.micinf.2005.06.009 – ident: e_1_2_11_73_2 doi: 10.1074/jbc.M901752200 – ident: e_1_2_11_96_2 doi: 10.1074/jbc.M800974200 – ident: e_1_2_11_12_2 – ident: e_1_2_11_64_2 doi: 10.1021/ja906611x – ident: e_1_2_11_93_2 doi: 10.1128/IAI.69.6.4019-4026.2001 – ident: e_1_2_11_16_2 doi: 10.1016/j.ab.2006.10.021 – ident: e_1_2_11_80_2 doi: 10.1371/journal.pone.0001164 – ident: e_1_2_11_87_2 doi: 10.1074/jbc.M500071200 – ident: e_1_2_11_15_2 doi: 10.1074/jbc.275.13.9876 – ident: e_1_2_11_48_2 doi: 10.1021/bi034391g – ident: e_1_2_11_27_2 doi: 10.1073/pnas.0803565105 – ident: e_1_2_11_68_2 doi: 10.1007/s10858-010-9464-2 – ident: e_1_2_11_53_2 doi: 10.1016/j.cell.2010.09.031 – ident: e_1_2_11_36_2 – ident: e_1_2_11_97_2 – ident: e_1_2_11_35_2 doi: 10.1002/cbic.200700614 – ident: e_1_2_11_25_2 doi: 10.1016/j.jmb.2009.08.058 – ident: e_1_2_11_34_2 doi: 10.1038/nchembio.2007.31 – ident: e_1_2_11_7_2 doi: 10.1021/bi035920j – ident: e_1_2_11_49_2 doi: 10.1016/0092-8674(92)90101-H – ident: e_1_2_11_43_2 doi: 10.1021/bi700448e – ident: e_1_2_11_23_2 doi: 10.1111/j.1365-2958.2004.04117.x – ident: e_1_2_11_52_2 doi: 10.1021/cb100195d – ident: e_1_2_11_88_2 doi: 10.1073/pnas.032523999 – ident: e_1_2_11_94_2 doi: 10.1016/j.febslet.2004.06.070 – ident: e_1_2_11_62_2 doi: 10.1021/ja077358g – ident: e_1_2_11_92_2 doi: 10.1074/jbc.M110.135434 – ident: e_1_2_11_18_2 doi: 10.1016/j.tim.2004.03.004 – ident: e_1_2_11_85_2 doi: 10.1016/j.pep.2009.10.012 – ident: e_1_2_11_58_2 doi: 10.1021/ja902681k – ident: e_1_2_11_66_2 doi: 10.1021/ja806779e – ident: e_1_2_11_84_2 doi: 10.1186/1472-6750-10-42 – ident: e_1_2_11_11_2 – ident: e_1_2_11_29_2 doi: 10.1073/pnas.080520697 – ident: e_1_2_11_46_2 doi: 10.1074/jbc.M305245200 – ident: e_1_2_11_47_2 doi: 10.1021/bi050141j – ident: e_1_2_11_30_2 doi: 10.1016/j.tim.2003.12.007 – ident: e_1_2_11_75_3 doi: 10.1002/anie.201000620 – ident: e_1_2_11_90_2 doi: 10.1128/JB.187.13.4646-4655.2005 – ident: e_1_2_11_39_2 doi: 10.1074/jbc.M401374200 – ident: e_1_2_11_40_2 doi: 10.1074/jbc.M109.022624 – ident: e_1_2_11_14_2 doi: 10.1016/S0966-842X(01)01956-4 – ident: e_1_2_11_13_2 doi: 10.1128/JB.187.14.4928-4934.2005 – ident: e_1_2_11_9_2 doi: 10.1002/pmic.200402075 – ident: e_1_2_11_54_2 doi: 10.1021/jo062331l – ident: e_1_2_11_75_2 doi: 10.1002/ange.201000620 – ident: e_1_2_11_1_2 doi: 10.1128/MMBR.70.1.192-221.2006 – ident: e_1_2_11_8_2 doi: 10.1016/j.resmic.2004.10.011 – ident: e_1_2_11_22_2 doi: 10.1046/j.1365-2958.2003.03782.x – ident: e_1_2_11_5_2 doi: 10.1074/jbc.274.34.24316 – ident: e_1_2_11_57_2 doi: 10.1074/jbc.M807172200 – ident: e_1_2_11_67_2 doi: 10.1007/s10858-008-9296-5 – ident: e_1_2_11_32_2 doi: 10.2174/138955707782110097 |
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Snippet | Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then reform a... Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site-specifically break a peptide bond and then reform a... Abstract Sortases are a class of bacterial enzymes that possess transpeptidase activity. It is their ability to site‐specifically break a peptide bond and then... |
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SubjectTerms | Amino Acid Motifs Aminoacyltransferases - chemistry Aminoacyltransferases - genetics Aminoacyltransferases - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Cysteine Endopeptidases - chemistry Cysteine Endopeptidases - genetics Cysteine Endopeptidases - metabolism Enzymes Protein Engineering Protein folding protein modifications Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism site specificity sortase Staphylococcus aureus - enzymology transpeptidation |
Title | Making and Breaking Peptide Bonds: Protein Engineering Using Sortase |
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