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Volumn 7, Issue 9, 2012, Pages 1137-1146

Enzyme-mediated methodologies for protein modification and bioconjugate synthesis

Author keywords

Bioconjugate; Enzyme; Protein immobilization; Protein modification

Indexed keywords

ACYLTRANSFERASES; BIOCONJUGATES; CHEMICAL METHOD; ENZYMATIC METHODS; FUNCTIONAL MOLECULES; HETEROGENEOUS PRODUCTS; LIGASES; NONCOVALENT; PROTEIN ACTIVITY; PROTEIN ENGINEERING; PROTEIN IMMOBILIZATION; PROTEIN MODIFICATIONS; PROTEIN-SPLICING; SITE-SPECIFIC; SUBSTRATE SPECIFICITY; THERAPEUTIC RESEARCH;

EID: 84866050073     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201200022     Document Type: Review
Times cited : (25)

References (97)
  • 1
    • 0347926091 scopus 로고    scopus 로고
    • Drug delivery strategy utilizing conjugation via reversible disulfide linkages: Role and site of cellular reducing activities.
    • Saito, G., Swanson, J. A., Lee, K., Drug delivery strategy utilizing conjugation via reversible disulfide linkages: Role and site of cellular reducing activities. Adv. Drug Deliv. Rev. 2003, 55, 199-215.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 199-215
    • Saito, G.1    Swanson, J.A.2    Lee, K.3
  • 2
    • 34248551662 scopus 로고    scopus 로고
    • Antibody engineering and modification technologies.
    • Filpula, D., Antibody engineering and modification technologies. Biomol. Eng. 2007, 24, 201-215.
    • (2007) Biomol. Eng. , vol.24 , pp. 201-215
    • Filpula, D.1
  • 4
    • 76949103845 scopus 로고    scopus 로고
    • PEGylated polymers for medicine: From conjugation to self-assembled systems.
    • Joralemon, M. J., McRae, S., Emrick, T., PEGylated polymers for medicine: From conjugation to self-assembled systems. Chem. Commun. 2010, 46, 1377-1393.
    • (2010) Chem. Commun. , vol.46 , pp. 1377-1393
    • Joralemon, M.J.1    McRae, S.2    Emrick, T.3
  • 6
    • 79961039002 scopus 로고    scopus 로고
    • The controlled display of biomolecules on nanoparticles: A challenge suited to bioorthogonal chemistry.
    • Algar, W. R., Prasuhn, D. E., Stewart, M. H., Jennings, T. L. et al., The controlled display of biomolecules on nanoparticles: A challenge suited to bioorthogonal chemistry. Bioconjug. Chem. 2011, 22, 825-858.
    • (2011) Bioconjug. Chem. , vol.22 , pp. 825-858
    • Algar, W.R.1    Prasuhn, D.E.2    Stewart, M.H.3    Jennings, T.L.4
  • 7
    • 69249229900 scopus 로고    scopus 로고
    • Temperature influence on fluorescence intensity and enzyme activity of the fusion protein of GFP and hyperthermophilic xylanase.
    • Zhang, C., Liu, M. S., Xing, X. H., Temperature influence on fluorescence intensity and enzyme activity of the fusion protein of GFP and hyperthermophilic xylanase. Appl. Microbiol. Biotechnol. 2009, 84, 511-517.
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 511-517
    • Zhang, C.1    Liu, M.S.2    Xing, X.H.3
  • 8
    • 34250825351 scopus 로고    scopus 로고
    • The click reaction in the luminescent probing of metal ions, and its implications on biolabeling techniques.
    • Wolfbeis, O. S., The click reaction in the luminescent probing of metal ions, and its implications on biolabeling techniques. Angew. Chem. Int. Ed. 2007, 46, 2980-2982.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 2980-2982
    • Wolfbeis, O.S.1
  • 9
    • 34248230589 scopus 로고    scopus 로고
    • Convergent chemical synthesis and crystal structure of a 203 amino acid ''covalent dimer'' HIV-1 protease enzyme molecule.
    • Torbeev, V. Y., Kent, S. B., Convergent chemical synthesis and crystal structure of a 203 amino acid ''covalent dimer'' HIV-1 protease enzyme molecule. Angew. Che. Int. Ed. 2007, 46, 1667-1670.
    • (2007) Angew. Che. Int. Ed. , vol.46 , pp. 1667-1670
    • Torbeev, V.Y.1    Kent, S.B.2
  • 10
    • 4344639697 scopus 로고    scopus 로고
    • The Staudinger ligation-a gift to chemical biology.
    • Köhn, M., Breinbauer, R., The Staudinger ligation-a gift to chemical biology. Angew. Che. Int. Ed. 2004, 43, 3106-3116.
    • (2004) Angew. Che. Int. Ed. , vol.43 , pp. 3106-3116
    • Köhn, M.1    Breinbauer, R.2
  • 11
    • 0347613015 scopus 로고    scopus 로고
    • Current and prospective applications of metal ion-protein binding.
    • Ueda, E. K., Gout, P. W., Morganti, L., Current and prospective applications of metal ion-protein binding. J. Chromatogr. A. 2003, 988, 1-23.
    • (2003) J. Chromatogr. A. , vol.988 , pp. 1-23
    • Ueda, E.K.1    Gout, P.W.2    Morganti, L.3
  • 12
    • 36448929836 scopus 로고    scopus 로고
    • Noncovalent, site-specific biotinylation of histidine-tagged proteins.
    • Reichel, A., Schaible, D., Furoukh, N. A., Cohen, M. et al., Noncovalent, site-specific biotinylation of histidine-tagged proteins. Anal. Chem. 2007, 79, 8590-8600.
    • (2007) Anal. Chem. , vol.79 , pp. 8590-8600
    • Reichel, A.1    Schaible, D.2    Furoukh, N.A.3    Cohen, M.4
  • 13
    • 84863155417 scopus 로고    scopus 로고
    • Site-specific PEGylation at histidine tags.
    • Cong, Y., Pawlisz, E., Bryant, P., Balan, S. et al., Site-specific PEGylation at histidine tags. Bioconjug. Chem. 2012, 23, 248-263.
    • (2012) Bioconjug. Chem. , vol.23 , pp. 248-263
    • Cong, Y.1    Pawlisz, E.2    Bryant, P.3    Balan, S.4
  • 14
    • 84859711910 scopus 로고    scopus 로고
    • Microplate assay for aptamer-based thrombin detection using a DNA-enzyme conjugate based on histidine-tag chemistry.
    • Shimada, J., Maruyama, T., Kitaoka, M., Kamiya, N. et al., Microplate assay for aptamer-based thrombin detection using a DNA-enzyme conjugate based on histidine-tag chemistry. Anal. Biochem. 2012, 421, 541-546.
    • (2012) Anal. Biochem. , vol.421 , pp. 541-546
    • Shimada, J.1    Maruyama, T.2    Kitaoka, M.3    Kamiya, N.4
  • 15
    • 67749130626 scopus 로고    scopus 로고
    • Characteristics of low molecular weight heparin production by an ultrafiltration membrane bioreactor using maltose binding protein fused heparinase I.
    • Ye, F., Kuang, Y., Chen, S., Zhang, C. et al., Characteristics of low molecular weight heparin production by an ultrafiltration membrane bioreactor using maltose binding protein fused heparinase I. Biochem. Eng. J. 2009, 46, 193-198.
    • (2009) Biochem. Eng. J. , vol.46 , pp. 193-198
    • Ye, F.1    Kuang, Y.2    Chen, S.3    Zhang, C.4
  • 16
    • 79959199497 scopus 로고    scopus 로고
    • Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: Implications for a comprehensive thermostabilization strategy.
    • Chen, S., Ye, F., Chen, Y., Chen, Y. et al., Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: Implications for a comprehensive thermostabilization strategy. Biotechnol. Bioeng. 2011, 108, 1841-1851.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1841-1851
    • Chen, S.1    Ye, F.2    Chen, Y.3    Chen, Y.4
  • 17
    • 0033176011 scopus 로고    scopus 로고
    • Enzymatic mutation detection: Enrichment of heteroduplexes from hybrid DNA mixtures by cleavage-deficient GST-tagged endonuclease VII.
    • Golz, S., Kemper, B., Enzymatic mutation detection: Enrichment of heteroduplexes from hybrid DNA mixtures by cleavage-deficient GST-tagged endonuclease VII. Nucleic. Acids. Res. 1999, 27, e7.
    • (1999) Nucleic. Acids. Res. , vol.27
    • Golz, S.1    Kemper, B.2
  • 18
    • 84555177672 scopus 로고    scopus 로고
    • SNAP-tag technology mediates site specific conjugation of antibody fragments with a photosensitizer and improves target specific phototoxicity in tumor cells.
    • Hussain, A. F., Kampmeier, F., Felbert, V., Merk, H. et al., SNAP-tag technology mediates site specific conjugation of antibody fragments with a photosensitizer and improves target specific phototoxicity in tumor cells. Bioconjug. Chem. 2011, 22, 2487-2495.
    • (2011) Bioconjug. Chem. , vol.22 , pp. 2487-2495
    • Hussain, A.F.1    Kampmeier, F.2    Felbert, V.3    Merk, H.4
  • 19
    • 79960562309 scopus 로고    scopus 로고
    • Small-molecule hydrophobic tagging-induced degradation of Halo Tag fusion proteins.
    • Neklesa, T. K., Tae, H. S., Schneekloth, A. R., Stulberg, M. J. et al., Small-molecule hydrophobic tagging-induced degradation of Halo Tag fusion proteins. Nat. Chem. Biol. 2011, 7, 538-543.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 538-543
    • Neklesa, T.K.1    Tae, H.S.2    Schneekloth, A.R.3    Stulberg, M.J.4
  • 20
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells.
    • Griffin, B. A., Adams, S. R., Tsien, R. Y., Specific covalent labeling of recombinant protein molecules inside live cells. Science 1998, 281, 269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 21
    • 65349158569 scopus 로고    scopus 로고
    • Fluorescent labeling of proteins in living cells using the FKBP12 (F36V) tag.
    • Robers, M., Pinson, P., Leong, L., Batchelor, R. H. et al., Fluorescent labeling of proteins in living cells using the FKBP12 (F36V) tag. Cytometry A 2009, 75, 207-224.
    • (2009) Cytometry A , vol.75 , pp. 207-224
    • Robers, M.1    Pinson, P.2    Leong, L.3    Batchelor, R.H.4
  • 22
    • 77957758860 scopus 로고    scopus 로고
    • Biological applications of protein splicing.
    • Vila-Perelló, M., Muir, T. W., Biological applications of protein splicing. Cell 2010, 143, 191-200.
    • (2010) Cell , vol.143 , pp. 191-200
    • Vila-Perelló, M.1    Muir, T.W.2
  • 23
    • 79952850251 scopus 로고    scopus 로고
    • Modification of transmembrane and GPI-anchored proteins on living cells by efficient protein trans-splicing using the Npu DnaE intein.
    • Dhar, T., Mootz, H. D., Modification of transmembrane and GPI-anchored proteins on living cells by efficient protein trans-splicing using the Npu DnaE intein. Chem. Commun. 2011, 47, 3063-3065.
    • (2011) Chem. Commun. , vol.47 , pp. 3063-3065
    • Dhar, T.1    Mootz, H.D.2
  • 24
    • 84863337696 scopus 로고    scopus 로고
    • The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures.
    • Rossi, E. A., Goldenberg, D. M., Chang, C., The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures. Bioconjug. Chem. 2012, 23, 309-323.
    • (2012) Bioconjug. Chem. , vol.23 , pp. 309-323
    • Rossi, E.A.1    Goldenberg, D.M.2    Chang, C.3
  • 25
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids.
    • Aeschlimann, D., Paulsson, M., Transglutaminases: Protein cross-linking enzymes in tissues and body fluids. Thromb. Haemost. 1994, 71, 402-415.
    • (1994) Thromb. Haemost. , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 26
    • 0031690193 scopus 로고    scopus 로고
    • Transglutaminase and its use for food processing.
    • Motoki, M., Seguro, K., Transglutaminase and its use for food processing. Trends Food Sci. Technol. 1998, 9, 204-210.
    • (1998) Trends Food Sci. Technol. , vol.9 , pp. 204-210
    • Motoki, M.1    Seguro, K.2
  • 27
    • 0033885714 scopus 로고    scopus 로고
    • Transglutaminase-mediated dual and site-specific incorporation of poly(ethylene glycol) derivatives into a chimeric interleukin-2.
    • Sato, H., Yamamoto, K., Hayashi, E., Takahara, Y., Transglutaminase-mediated dual and site-specific incorporation of poly(ethylene glycol) derivatives into a chimeric interleukin-2. Bioconjug. Chem. 2000, 11, 502-509.
    • (2000) Bioconjug. Chem. , vol.11 , pp. 502-509
    • Sato, H.1    Yamamoto, K.2    Hayashi, E.3    Takahara, Y.4
  • 28
    • 33646038598 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed site-specific conjugation of small- molecule probes to proteins in vitro and on the surface of living cells.
    • Lin, C., Ting, A. Y., Transglutaminase-catalyzed site-specific conjugation of small- molecule probes to proteins in vitro and on the surface of living cells. J. Am. Chem. Soc. 2006, 128, 4542-4543.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4542-4543
    • Lin, C.1    Ting, A.Y.2
  • 29
    • 0034809776 scopus 로고    scopus 로고
    • Further studies on the site-specific protein modification by microbial transglutaminase.
    • Sato, H., Hayashi, E., Yamada, N., Yatagai, M., Takahara, Y., Further studies on the site-specific protein modification by microbial transglutaminase. Bioconjug. Chem. 2001, 12, 701-710.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 701-710
    • Sato, H.1    Hayashi, E.2    Yamada, N.3    Yatagai, M.4    Takahara, Y.5
  • 30
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase.
    • Yokoyama, K., Nio, N., Kikuchi, Y., Properties and applications of microbial transglutaminase. Appl. Microbiol. Biotechnol. 2004, 64, 447-454.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 31
    • 62549119508 scopus 로고    scopus 로고
    • Transglutaminase-mediated PEGylation of proteins: Direct identification of the sites of protein modification by mass spectrometry using a novel monodisperse PEG.
    • Mero, A., Spolaor, B., Veronese, F. M., Fontana, A., Transglutaminase-mediated PEGylation of proteins: Direct identification of the sites of protein modification by mass spectrometry using a novel monodisperse PEG. Bioconjug. Chem. 2009, 20, 384-389.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 384-389
    • Mero, A.1    Spolaor, B.2    Veronese, F.M.3    Fontana, A.4
  • 32
    • 79960925703 scopus 로고    scopus 로고
    • A new method to increase selectivity of transglutaminase mediated PEGylation of salmon calcitonin and human growth hormone.
    • Mero, A., Schiavon, M., Veronese, F. M., Pasut, G., A new method to increase selectivity of transglutaminase mediated PEGylation of salmon calcitonin and human growth hormone. J. Control. Release 2011, 154, 27-34.
    • (2011) J. Control. Release , vol.154 , pp. 27-34
    • Mero, A.1    Schiavon, M.2    Veronese, F.M.3    Pasut, G.4
  • 33
    • 36549039553 scopus 로고    scopus 로고
    • Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase.
    • Fontana, A., Spolaore, B., Mero, A., Veronese, F. M., Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase. Adv. Drug Deliv. Rev. 2008, 60, 13-28.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 13-28
    • Fontana, A.1    Spolaore, B.2    Mero, A.3    Veronese, F.M.4
  • 34
    • 2442683103 scopus 로고    scopus 로고
    • Enzymatic labeling of a single chain variable fragment of an antibody with alkaline phosphatase by microbial transglutaminase.
    • Takazawa, T., Kamiya, N., Ueda, H., Nagamune, T., Enzymatic labeling of a single chain variable fragment of an antibody with alkaline phosphatase by microbial transglutaminase. Biotechnol. Bioeng. 2004, 86, 399-404.
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 399-404
    • Takazawa, T.1    Kamiya, N.2    Ueda, H.3    Nagamune, T.4
  • 35
    • 2442679406 scopus 로고    scopus 로고
    • Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase.
    • Tanaka, T., Kamiya, N., Nagamune, T., Peptidyl linkers for protein heterodimerization catalyzed by microbial transglutaminase. Bioconjug. Chem. 2004, 15, 491-497.
    • (2004) Bioconjug. Chem. , vol.15 , pp. 491-497
    • Tanaka, T.1    Kamiya, N.2    Nagamune, T.3
  • 36
    • 77956855417 scopus 로고    scopus 로고
    • Enzymatic single-step preparation of multifunctional proteins.
    • Abe, H., Goto, M., Kamiya, N., Enzymatic single-step preparation of multifunctional proteins. Chem. Commun. 2010, 46, 7160-7162.
    • (2010) Chem. Commun. , vol.46 , pp. 7160-7162
    • Abe, H.1    Goto, M.2    Kamiya, N.3
  • 38
    • 82955200056 scopus 로고    scopus 로고
    • Protein lipidation catalyzed by microbial transglutaminase.
    • Abe, H., Goto, M., Kamiya, N., Protein lipidation catalyzed by microbial transglutaminase. Chem. Eur. J. 2011, 17, 14004-14008.
    • (2011) Chem. Eur. J. , vol.17 , pp. 14004-14008
    • Abe, H.1    Goto, M.2    Kamiya, N.3
  • 39
    • 64249109023 scopus 로고    scopus 로고
    • Using phosphopantetheinyl transferases for enzyme posttranslational activation, site specific protein labeling and identification of natural product biosynthetic gene clusters from bacterial genomes.
    • Sunbul, M., Zhang, K., Yin, J., Using phosphopantetheinyl transferases for enzyme posttranslational activation, site specific protein labeling and identification of natural product biosynthetic gene clusters from bacterial genomes. Methods Enzymol. 2009, 458, 255-275.
    • (2009) Methods Enzymol. , vol.458 , pp. 255-275
    • Sunbul, M.1    Zhang, K.2    Yin, J.3
  • 40
    • 3042546498 scopus 로고    scopus 로고
    • Labeling proteins with small molecules by site-specific posttranslational modification.
    • Yin, J., Liu, F., Li, X., Walsh, C. T., Labeling proteins with small molecules by site-specific posttranslational modification. J. Am. Chem. Soc. 2004, 126, 7754-7755.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7754-7755
    • Yin, J.1    Liu, F.2    Li, X.3    Walsh, C.T.4
  • 41
    • 67650555677 scopus 로고    scopus 로고
    • Phosphopantetheinyl transferase catalyzed site-specific protein labeling with ADP conjugated chemical probes.
    • Zou, Y., Yin, J., Phosphopantetheinyl transferase catalyzed site-specific protein labeling with ADP conjugated chemical probes. J. Am. Chem. Soc. 2009, 131, 7548-7549.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7548-7549
    • Zou, Y.1    Yin, J.2
  • 42
    • 27644508250 scopus 로고    scopus 로고
    • Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase.
    • Yin, J., Straight, P. D., McLoughlin, S. M., Zhou, Z. et al., Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase. Proc. Natl. Acad. Sci. USA 2005, 102, 15815-15820.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15815-15820
    • Yin, J.1    Straight, P.D.2    McLoughlin, S.M.3    Zhou, Z.4
  • 43
    • 51949086070 scopus 로고    scopus 로고
    • Direct site-selective covalent protein immobilization catalyzed by a phosphopantetheinyl transferase.
    • Wong, L. S., Thirlway, J., Micklefield, J., Direct site-selective covalent protein immobilization catalyzed by a phosphopantetheinyl transferase. J. Am. Chem. Soc. 2008, 130, 12456-12464.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12456-12464
    • Wong, L.S.1    Thirlway, J.2    Micklefield, J.3
  • 44
    • 76249129408 scopus 로고    scopus 로고
    • Site-selective immobilisation of functional enzymes onto polystyrene nanoparticles.
    • Wong, L. S., Okrasa, K., Micklefield, J., Site-selective immobilisation of functional enzymes onto polystyrene nanoparticles. Org. Biomol. Chem. 2010, 8, 782-787.
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 782-787
    • Wong, L.S.1    Okrasa, K.2    Micklefield, J.3
  • 45
    • 35348938968 scopus 로고    scopus 로고
    • Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase.
    • Watanabe, K., Toh, Y., Suto, K., Shimizu, Y. et al., Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase. Nature 2007, 449, 867-872.
    • (2007) Nature , vol.449 , pp. 867-872
    • Watanabe, K.1    Toh, Y.2    Suto, K.3    Shimizu, Y.4
  • 46
    • 34247509275 scopus 로고    scopus 로고
    • Leucyl/phenylalanyl (L/F)-tRNA-protein transferase-mediated aminoacyl transfer of a nonnatural amino acid to the N-terminus of peptides and proteins and subsequent functionalization by bioorthogonal reactions.
    • Taki, M., Sisido, M., Leucyl/phenylalanyl (L/F)-tRNA-protein transferase-mediated aminoacyl transfer of a nonnatural amino acid to the N-terminus of peptides and proteins and subsequent functionalization by bioorthogonal reactions. Biopolymers 2007, 88, 263-271.
    • (2007) Biopolymers , vol.88 , pp. 263-271
    • Taki, M.1    Sisido, M.2
  • 47
    • 0029788178 scopus 로고    scopus 로고
    • Aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase.
    • Abramochkin, G., Shrader, T. E., Aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase. J. Biol. Chem. 1996, 271, 22901-22907.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22901-22907
    • Abramochkin, G.1    Shrader, T.E.2
  • 48
    • 80053069963 scopus 로고    scopus 로고
    • N-terminal protein modification using simple aminoacyl transferase substrates.
    • Wagner, A. M., Fegley, M. W., Warner, J. B., Grindley, C. L. J. et al., N-terminal protein modification using simple aminoacyl transferase substrates. J. Am. Chem. Soc. 2011, 133, 15139-15147.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15139-15147
    • Wagner, A.M.1    Fegley, M.W.2    Warner, J.B.3    Grindley, C.L.J.4
  • 49
    • 77956286293 scopus 로고    scopus 로고
    • Sortase transpeptidases: Insights into mechanism, substrate specificity, and inhibition.
    • Clancy, K. W., Melvin, J. A., McCafferty, D. G., Sortase transpeptidases: Insights into mechanism, substrate specificity, and inhibition. Biopolymers 2010, 94, 385-396.
    • (2010) Biopolymers , vol.94 , pp. 385-396
    • Clancy, K.W.1    Melvin, J.A.2    McCafferty, D.G.3
  • 50
    • 1542317850 scopus 로고    scopus 로고
    • Sortase-mediated protein ligation: A new method for protein engineering.
    • Mao, H., Hart, S. A., Schink, A., Pollok, B. A., Sortase-mediated protein ligation: A new method for protein engineering. J. Am. Chem. Soc. 2004, 126, 2670-2671.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2670-2671
    • Mao, H.1    Hart, S.A.2    Schink, A.3    Pollok, B.A.4
  • 51
    • 65549164210 scopus 로고    scopus 로고
    • Sortase-mediated ligation: A gift from Gram-positive bacteria to protein engineering.
    • Tsukiji, S., Nagamune, T., Sortase-mediated ligation: A gift from Gram-positive bacteria to protein engineering. Chembiochem 2009, 10, 787-798.
    • (2009) Chembiochem , vol.10 , pp. 787-798
    • Tsukiji, S.1    Nagamune, T.2
  • 52
    • 69349099057 scopus 로고    scopus 로고
    • Sortase-mediated protein ligation: An emerging biotechnology tool for protein modification and immobilization.
    • Proft, T., Sortase-mediated protein ligation: An emerging biotechnology tool for protein modification and immobilization. Biotechnol. Lett. 2010, 32, 1-10.
    • (2010) Biotechnol. Lett. , vol.32 , pp. 1-10
    • Proft, T.1
  • 53
    • 79956154315 scopus 로고    scopus 로고
    • Making and breaking peptide bonds: Protein engineering using sortase.
    • Popp, M. W., Ploegh, H. L., Making and breaking peptide bonds: Protein engineering using sortase. Angew. Chem. Int. Ed. 2011, 50, 5024-5032.
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 5024-5032
    • Popp, M.W.1    Ploegh, H.L.2
  • 54
    • 78650363751 scopus 로고    scopus 로고
    • Enzyme-mediated site-specific antibody-protein modification using a ZZ domain as a linker.
    • Sakamoto, T., Sawamoto, S., Tanaka, T., Fukuda, H. et al., Enzyme-mediated site-specific antibody-protein modification using a ZZ domain as a linker. Bioconjug. Chem. 2010, 21, 2227-2233.
    • (2010) Bioconjug. Chem. , vol.21 , pp. 2227-2233
    • Sakamoto, T.1    Sawamoto, S.2    Tanaka, T.3    Fukuda, H.4
  • 55
    • 79952043134 scopus 로고    scopus 로고
    • Site-specific tetrameric streptavidin-protein conjugation using sortase A.
    • Matsumoto, T., Sawamoto, S., Sakamoto, T., Tanaka, T. et al., Site-specific tetrameric streptavidin-protein conjugation using sortase A. J. Biotechnol. 2011, 152, 37-42.
    • (2011) J. Biotechnol. , vol.152 , pp. 37-42
    • Matsumoto, T.1    Sawamoto, S.2    Sakamoto, T.3    Tanaka, T.4
  • 56
    • 39549097968 scopus 로고    scopus 로고
    • Peptide-sugar ligation catalyzed by transpeptidase sortase: A facile approach to neoglycoconjugate synthesis.
    • Samantaray, S., Marathe, U., Dasgupta, S., Nandicoori, V. K. et al., Peptide-sugar ligation catalyzed by transpeptidase sortase: A facile approach to neoglycoconjugate synthesis. J. Am. Chem. Soc. 2008, 130, 2132-2133.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2132-2133
    • Samantaray, S.1    Marathe, U.2    Dasgupta, S.3    Nandicoori, V.K.4
  • 57
    • 57149115773 scopus 로고    scopus 로고
    • Lipid modification of proteins through sortase-catalyzed transpeptidation.
    • Antos, J. M., Miller, G. M., Grotenbreg, G. M., Ploegh, H. L., Lipid modification of proteins through sortase-catalyzed transpeptidation. J. Am. Chem. Soc. 2008, 130, 16338-16343.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16338-16343
    • Antos, J.M.1    Miller, G.M.2    Grotenbreg, G.M.3    Ploegh, H.L.4
  • 58
    • 34248575231 scopus 로고    scopus 로고
    • Synthesis of biologically active peptide nucleic acid-peptide conjugates by sortase-mediated ligation.
    • Pritz, S., Wolf, Y., Kraetke, O., Klose, J. et al., Synthesis of biologically active peptide nucleic acid-peptide conjugates by sortase-mediated ligation. J. Org. Chem. 2007, 72, 3909-3912.
    • (2007) J. Org. Chem. , vol.72 , pp. 3909-3912
    • Pritz, S.1    Wolf, Y.2    Kraetke, O.3    Klose, J.4
  • 60
    • 43149123357 scopus 로고    scopus 로고
    • Site-specific protein modification on living cells catalyzed by sortase.
    • Tanaka, T., Yamamoto, T., Tsukiji, S., Nagamune, T., Site-specific protein modification on living cells catalyzed by sortase. Chembiochem 2008, 9, 802-807.
    • (2008) Chembiochem , vol.9 , pp. 802-807
    • Tanaka, T.1    Yamamoto, T.2    Tsukiji, S.3    Nagamune, T.4
  • 61
    • 3543063548 scopus 로고    scopus 로고
    • A self-cleavable sortase fusion for one-step purification of free recombinant proteins.
    • Mao, H., A self-cleavable sortase fusion for one-step purification of free recombinant proteins. Protein Expr. Purif. 2004, 37, 253-263.
    • (2004) Protein Expr. Purif. , vol.37 , pp. 253-263
    • Mao, H.1
  • 62
    • 77952964100 scopus 로고    scopus 로고
    • Biotinylated-sortase self-cleavage purification (BISOP) method for cell-free produced proteins.
    • Matsunaga, S., Matsuoka, K., Shimizu, K., Endo, Y. et al., Biotinylated-sortase self-cleavage purification (BISOP) method for cell-free produced proteins. BMC Biotechnol. 2010, 10, 42.
    • (2010) BMC Biotechnol. , vol.10 , pp. 42
    • Matsunaga, S.1    Matsuoka, K.2    Shimizu, K.3    Endo, Y.4
  • 63
    • 77949533713 scopus 로고    scopus 로고
    • Highly oriented recombinant glycosyltransferases: Site-specific immobilization of unstable membrane proteins by using Staphylococcus aureus sortase A.
    • Ito, T., Sadamoto, R., Naruchi, K., Togame, H. et al., Highly oriented recombinant glycosyltransferases: Site-specific immobilization of unstable membrane proteins by using Staphylococcus aureus sortase A. Biochemistry 2010, 49, 2604-2614.
    • (2010) Biochemistry , vol.49 , pp. 2604-2614
    • Ito, T.1    Sadamoto, R.2    Naruchi, K.3    Togame, H.4
  • 64
    • 33947664974 scopus 로고    scopus 로고
    • Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation.
    • Parthasarathy, R., Subramanian, S., Boder, E. T., Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation. Bioconjug. Chem. 2007, 18, 469-476.
    • (2007) Bioconjug. Chem. , vol.18 , pp. 469-476
    • Parthasarathy, R.1    Subramanian, S.2    Boder, E.T.3
  • 65
    • 84859799135 scopus 로고    scopus 로고
    • Sortase A-catalyzed site-specific coimmobilization on microparticles via streptavidin.
    • Matsumoto, T., Tanaka, T., Kondo, A., Sortase A-catalyzed site-specific coimmobilization on microparticles via streptavidin. Langmuir 2012, 28, 3553-3557.
    • (2012) Langmuir , vol.28 , pp. 3553-3557
    • Matsumoto, T.1    Tanaka, T.2    Kondo, A.3
  • 66
    • 80051675805 scopus 로고    scopus 로고
    • Sortase A as a tool for high-yield histatin cyclization.
    • Bolscher, J. G., Oudhoff, M. J., Nazmi, K., Antos, J. M. et al., Sortase A as a tool for high-yield histatin cyclization. FASEB. J. 2011, 25, 2650-2658.
    • (2011) FASEB. J. , vol.25 , pp. 2650-2658
    • Bolscher, J.G.1    Oudhoff, M.J.2    Nazmi, K.3    Antos, J.M.4
  • 67
    • 79960976516 scopus 로고    scopus 로고
    • Sortase A-catalyzed peptide cyclization for the synthesis of macrocyclic peptides and glycopeptides.
    • Wu, Z., Guo, X., Guo, Z., Sortase A-catalyzed peptide cyclization for the synthesis of macrocyclic peptides and glycopeptides. Chem. Commun. 2011, 47, 9218-9220.
    • (2011) Chem. Commun. , vol.47 , pp. 9218-9220
    • Wu, Z.1    Guo, X.2    Guo, Z.3
  • 68
    • 84858715052 scopus 로고    scopus 로고
    • New method for site-specific modification of liposomes with proteins using sortase A-mediated transpeptidation.
    • Guo, X., Wu, Z., Guo, Z., New method for site-specific modification of liposomes with proteins using sortase A-mediated transpeptidation. Bioconjug. Chem. 2012, 23, 650-655.
    • (2012) Bioconjug. Chem. , vol.23 , pp. 650-655
    • Guo, X.1    Wu, Z.2    Guo, Z.3
  • 69
    • 44049095122 scopus 로고    scopus 로고
    • Synthesis of protein mimics with nonlinear backbone topology by combined recombinant, enzymatic, and chemical synthesis strategy.
    • Pritz, S., Kraetke, O., Klose, A., Klose, J., Synthesis of protein mimics with nonlinear backbone topology by combined recombinant, enzymatic, and chemical synthesis strategy. Angew. Chem. Int. Ed. 2008, 47, 3642-3645.
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 3642-3645
    • Pritz, S.1    Kraetke, O.2    Klose, A.3    Klose, J.4
  • 70
    • 61849124088 scopus 로고    scopus 로고
    • Expansion of the sortase-mediated labeling method for site-specific N-terminal labeling of cell surface proteins on living cells.
    • Yamamoto, T., Nagamune, T., Expansion of the sortase-mediated labeling method for site-specific N-terminal labeling of cell surface proteins on living cells. Chem. Commun. 2009, 9, 1022-1024.
    • (2009) Chem. Commun. , vol.9 , pp. 1022-1024
    • Yamamoto, T.1    Nagamune, T.2
  • 71
    • 65449140986 scopus 로고    scopus 로고
    • Crystal structure of Streptococcus pyogenes sortase A.
    • Race, P. R., Bentley, M. L., Melvin, J. A., Crow, A. et al., Crystal structure of Streptococcus pyogenes sortase A. J. Biol. Chem. 2009, 284, 6924-6933.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6924-6933
    • Race, P.R.1    Bentley, M.L.2    Melvin, J.A.3    Crow, A.4
  • 72
    • 68249159439 scopus 로고    scopus 로고
    • Site-specific N- and C-terminal labeling of a single polypeptide using sortases of different specificity.
    • Antos, J. M., Chew, G., Guimaraes, C. P., Yoder, N. C. et al., Site-specific N- and C-terminal labeling of a single polypeptide using sortases of different specificity. J. Am. Chem. Soc. 2009, 131, 10800-10801.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10800-10801
    • Antos, J.M.1    Chew, G.2    Guimaraes, C.P.3    Yoder, N.C.4
  • 73
    • 79952768710 scopus 로고    scopus 로고
    • Sortase-catalyzed transformations that improve the properties of cytokines.
    • Popp, M. W., Dougan, S. K., Chuang, T., Spooner, E. et al., Sortase-catalyzed transformations that improve the properties of cytokines. Proc. Natl. Acad. Sci. USA 2011, 108, 3169-3174.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3169-3174
    • Popp, M.W.1    Dougan, S.K.2    Chuang, T.3    Spooner, E.4
  • 74
    • 84860917024 scopus 로고    scopus 로고
    • Protein ligation in living cells using sortase.
    • Strijbis, K., Spooner, E., Ploegh, H. L., Protein ligation in living cells using sortase. Traffic 2012, 13, 780-789.
    • (2012) Traffic , vol.13 , pp. 780-789
    • Strijbis, K.1    Spooner, E.2    Ploegh, H.L.3
  • 75
    • 80455129492 scopus 로고    scopus 로고
    • Directed evolution of sortase A mutants with altered substrate selectivity profiles.
    • Piotukh, K., Geltinger, B., Heinrich, N., Gerth, F. et al., Directed evolution of sortase A mutants with altered substrate selectivity profiles. J. Am. Chem. Soc. 2011, 133, 17536-17539.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 17536-17539
    • Piotukh, K.1    Geltinger, B.2    Heinrich, N.3    Gerth, F.4
  • 76
    • 84860271647 scopus 로고    scopus 로고
    • Site-specific protein labeling with amine-containing molecules using Lactobacillus plantarum sortase.
    • Matsumoto, T., Takase, R., Tanaka, T., Fukuda, H., Site-specific protein labeling with amine-containing molecules using Lactobacillus plantarum sortase. Biotechnol. J. 2012, 7, 642-648.
    • (2012) Biotechnol. J. , vol.7 , pp. 642-648
    • Matsumoto, T.1    Takase, R.2    Tanaka, T.3    Fukuda, H.4
  • 77
    • 79960980943 scopus 로고    scopus 로고
    • A general strategy for the evolution of bond-forming enzymes using yeast display.
    • Chen, I., Dorr, B. M., Liu, D. R., A general strategy for the evolution of bond-forming enzymes using yeast display. Proc. Natl. Acad. Sci. USA 2011, 108, 11399-11404.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 11399-11404
    • Chen, I.1    Dorr, B.M.2    Liu, D.R.3
  • 78
    • 0025288944 scopus 로고
    • Avidin and streptavidin.
    • Green, N. M., Avidin and streptavidin. Methods Enzymol. 1990, 184, 51-67.
    • (1990) Methods Enzymol. , vol.184 , pp. 51-67
    • Green, N.M.1
  • 80
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation.
    • Beckett, D., Kovaleva, E., Schatz, P. J., A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 1999, 8, 921-929.
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 81
    • 0038611015 scopus 로고    scopus 로고
    • Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice.
    • de Boer, E., Rodriguez, P., Bonte, E., Krijgsveld, J. et al., Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice. Proc. Natl. Acad. Sci. USA 2003, 100, 7480-7485.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7480-7485
    • de Boer, E.1    Rodriguez, P.2    Bonte, E.3    Krijgsveld, J.4
  • 82
    • 18744401100 scopus 로고    scopus 로고
    • Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase.
    • Chen, I., Howarth, M., Lin, W., Ting, A. Y., Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat. Methods 2005, 2, 99-104.
    • (2005) Nat. Methods , vol.2 , pp. 99-104
    • Chen, I.1    Howarth, M.2    Lin, W.3    Ting, A.Y.4
  • 83
    • 34248993985 scopus 로고    scopus 로고
    • Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins.
    • Chen, I., Choi, Y., Ting, A. Y., Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins. J. Am. Chem. Soc. 2007, 129, 6619-6625.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6619-6625
    • Chen, I.1    Choi, Y.2    Ting, A.Y.3
  • 84
    • 38649113240 scopus 로고    scopus 로고
    • Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species.
    • Slavoff, S. A., Chen, I., Choi, Y., Ting, A. Y., Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species. J. Am. Chem. Soc. 2008, 130, 1160-1162.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1160-1162
    • Slavoff, S.A.1    Chen, I.2    Choi, Y.3    Ting, A.Y.4
  • 86
    • 36849084059 scopus 로고    scopus 로고
    • Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes.
    • Fernández-Suárez, M., Baruah, H., Martínez-Hernández, L., Xie, K. T. et al., Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes. Nat. Biotechnol. 2007, 25, 1483-1487.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1483-1487
    • Fernández-Suárez, M.1    Baruah, H.2    Martínez-Hernández, L.3    Xie, K.T.4
  • 87
    • 70450158888 scopus 로고    scopus 로고
    • Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase.
    • Puthenveetil, S., Liu, D. S., White, K. A., Thompson, S. et al., Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase. J. Am. Chem. Soc. 2009, 131, 16430-16438.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16430-16438
    • Puthenveetil, S.1    Liu, D.S.2    White, K.A.3    Thompson, S.4
  • 88
    • 77954633083 scopus 로고    scopus 로고
    • A fluorophore ligase for site-specific protein labeling inside living cells.
    • Uttamapinant, C., White, K. A., Baruah, H., Thompson, S. et al., A fluorophore ligase for site-specific protein labeling inside living cells. Proc. Natl. Acad. Sci. USA 2010, 107, 10914-10919.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 10914-10919
    • Uttamapinant, C.1    White, K.A.2    Baruah, H.3    Thompson, S.4
  • 89
    • 70449258565 scopus 로고
    • The oxidation of tyramine, tyrosine, and related compounds by peroxidaes.
    • Gross, A. J., Sizer, I. W., The oxidation of tyramine, tyrosine, and related compounds by peroxidaes. J. Biol. Chem. 1959, 234, 1611-1614.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1611-1614
    • Gross, A.J.1    Sizer, I.W.2
  • 90
    • 33846353512 scopus 로고    scopus 로고
    • Specific covalent immobilization of proteins through dityrosine cross-links.
    • Endrizzi, B. J., Huang, G., Kiser, P. F., Stewart, R. J., Specific covalent immobilization of proteins through dityrosine cross-links. Langmuir 2006, 22, 11305-11310.
    • (2006) Langmuir , vol.22 , pp. 11305-11310
    • Endrizzi, B.J.1    Huang, G.2    Kiser, P.F.3    Stewart, R.J.4
  • 91
    • 6344237489 scopus 로고    scopus 로고
    • Horseradish peroxidase-catalyzed cross-linking of feruloylated arabinoxylans with beta-casein.
    • Boeriu, C. G., Oudgenoeg, G., Spekking, W. T., Berendsen, L. B., Horseradish peroxidase-catalyzed cross-linking of feruloylated arabinoxylans with beta-casein. J. Agric. Food Chem. 2004, 52, 6633-6639.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 6633-6639
    • Boeriu, C.G.1    Oudgenoeg, G.2    Spekking, W.T.3    Berendsen, L.B.4
  • 92
    • 78751614082 scopus 로고    scopus 로고
    • Site-specific protein cross-linking by peroxidase-catalyzed activation of a tyrosine-containing peptide tag.
    • Minamihata, K., Goto, M., Kamiya, N., Site-specific protein cross-linking by peroxidase-catalyzed activation of a tyrosine-containing peptide tag. Bioconjug. Chem. 2011, 22, 74-81.
    • (2011) Bioconjug. Chem. , vol.22 , pp. 74-81
    • Minamihata, K.1    Goto, M.2    Kamiya, N.3
  • 93
    • 81255143187 scopus 로고    scopus 로고
    • Protein heteroconjugation by the peroxidase-catalyzed tyrosine coupling reaction.
    • Mianmihata, K., Goto, M., Kamiya, N., Protein heteroconjugation by the peroxidase-catalyzed tyrosine coupling reaction. Bioconjug. Chem. 2011, 22, 2332-2338.
    • (2011) Bioconjug. Chem. , vol.22 , pp. 2332-2338
    • Mianmihata, K.1    Goto, M.2    Kamiya, N.3
  • 94
  • 95
    • 79956291603 scopus 로고    scopus 로고
    • Site-specific enzymatic polysialylation of therapeutic proteins using bacterial enzymes.
    • Lindhout, T., Iqbal, U., Willis, L. M., Reid, A. N. et al., Site-specific enzymatic polysialylation of therapeutic proteins using bacterial enzymes. Proc. Natl. Acad. Sci. USA 2011, 108, 7397-7402.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7397-7402
    • Lindhout, T.1    Iqbal, U.2    Willis, L.M.3    Reid, A.N.4
  • 96
    • 81355139629 scopus 로고    scopus 로고
    • Choosing an effective protein bioconjugation strategy.
    • Stephanopoulos, N., Francis, M. B., Choosing an effective protein bioconjugation strategy. Nat. Chem. Biol. 2011, 7, 876-884.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 876-884
    • Stephanopoulos, N.1    Francis, M.B.2
  • 97
    • 38949104404 scopus 로고    scopus 로고
    • Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase.
    • Mindt, T. L., Jungi, V., Wyss, S., Friedli, A., Pla, G. et al., Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase. Bioconjug. Chem. 2008, 19, 271-278.
    • (2008) Bioconjug. Chem. , vol.19 , pp. 271-278
    • Mindt, T.L.1    Jungi, V.2    Wyss, S.3    Friedli, A.4    Pla, G.5


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