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Volumn 21, Issue 12, 2014, Pages 1610-1617

Peptide macrocyclization catalyzed by a prolyl oligopeptidase involved in α-amanitin biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMANITIN; AMINO ACID; MACROCYCLIC COMPOUND; PROLYL ENDOPEPTIDASE; SYNTHETIC PEPTIDE; AMANITIN; PHALLOTOXIN; SERINE PROTEINASE;

EID: 84919903118     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2014.10.015     Document Type: Article
Times cited : (94)

References (41)
  • 1
    • 84870039217 scopus 로고    scopus 로고
    • Structures of cyanobactin maturation enzymes define a family of transamidating proteases
    • V. Agarwal, E. Pierce, J. McIntosh, E.W. Schmidt, and S.K. Nair Structures of cyanobactin maturation enzymes define a family of transamidating proteases Chem. Biol. 19 2012 1411 1422
    • (2012) Chem. Biol. , vol.19 , pp. 1411-1422
    • Agarwal, V.1    Pierce, E.2    McIntosh, J.3    Schmidt, E.W.4    Nair, S.K.5
  • 4
    • 84877149384 scopus 로고    scopus 로고
    • The two-step biosynthesis of cyclic peptides from linear precursors in a member of the plant family Caryophyllaceae involves cyclization by a serine protease-like enzyme
    • C.J.S. Barber, P.T. Pujara, D.W. Reed, S. Chiwocha, H. Zhang, and P.S. Covello The two-step biosynthesis of cyclic peptides from linear precursors in a member of the plant family Caryophyllaceae involves cyclization by a serine protease-like enzyme J. Biol. Chem. 288 2013 12500 12510
    • (2013) J. Biol. Chem. , vol.288 , pp. 12500-12510
    • Barber, C.J.S.1    Pujara, P.T.2    Reed, D.W.3    Chiwocha, S.4    Zhang, H.5    Covello, P.S.6
  • 5
    • 84878789554 scopus 로고    scopus 로고
    • Form and function in cyclic peptide natural products: A pharmacokinetic perspective
    • A.T. Bockus, C.M. McEwen, and R.S. Lokey Form and function in cyclic peptide natural products: a pharmacokinetic perspective Curr. Top. Med. Chem. 13 2013 821 836
    • (2013) Curr. Top. Med. Chem. , vol.13 , pp. 821-836
    • Bockus, A.T.1    McEwen, C.M.2    Lokey, R.S.3
  • 7
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: Alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution
    • D.A. Bushnell, P. Cramer, and R.D. Kornberg Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution Proc. Natl. Acad. Sci. U S A 99 2002 1218 1222
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 1218-1222
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 8
    • 84864557191 scopus 로고    scopus 로고
    • Thematic minireview series on circular proteins
    • D.J. Craik, and N.M. Allewell Thematic minireview series on circular proteins J. Biol. Chem. 287 2012 26999 27000
    • (2012) J. Biol. Chem. , vol.287 , pp. 26999-27000
    • Craik, D.J.1    Allewell, N.M.2
  • 12
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis
    • V. Fülöp, Z. Böcskei, and L. Polgár Prolyl oligopeptidase: an unusual β-propeller domain regulates proteolysis Cell 94 1998 161 170
    • (1998) Cell , vol.94 , pp. 161-170
    • Fülöp, V.1    Böcskei, Z.2    Polgár, L.3
  • 13
    • 0035847042 scopus 로고    scopus 로고
    • Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue
    • V. Fülöp, Z. Szeltner, V. Renner, and L. Polgár Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue J. Biol. Chem. 276 2001 1262 1266
    • (2001) J. Biol. Chem. , vol.276 , pp. 1262-1266
    • Fülöp, V.1    Szeltner, Z.2    Renner, V.3    Polgár, L.4
  • 14
    • 84892163643 scopus 로고    scopus 로고
    • Macrocyclic drugs and clinical candidates: What can medicinal chemists learn from their properties?
    • F. Giordanetto, and J. Kihlberg Macrocyclic drugs and clinical candidates: what can medicinal chemists learn from their properties? J. Med. Chem. 57 2014 278 295
    • (2014) J. Med. Chem. , vol.57 , pp. 278-295
    • Giordanetto, F.1    Kihlberg, J.2
  • 17
    • 78449267410 scopus 로고    scopus 로고
    • Gene knockdown by ihpRNA-triggering in the ectomycorrhizal basidiomycete fungus Laccaria bicolor
    • M.J. Kemppainen, and A.G. Pardo Gene knockdown by ihpRNA-triggering in the ectomycorrhizal basidiomycete fungus Laccaria bicolor Bioeng. Bugs 1 2010 354 358
    • (2010) Bioeng. Bugs , vol.1 , pp. 354-358
    • Kemppainen, M.J.1    Pardo, A.G.2
  • 18
    • 78751619473 scopus 로고    scopus 로고
    • Transformation of the mycorrhizal fungus Laccaria bicolor using Agrobacterium tumefaciens
    • M.J. Kemppainen, and A.G. Pardo Transformation of the mycorrhizal fungus Laccaria bicolor using Agrobacterium tumefaciens Bioeng. Bugs 2 2011 38 44
    • (2011) Bioeng. Bugs , vol.2 , pp. 38-44
    • Kemppainen, M.J.1    Pardo, A.G.2
  • 20
    • 0017085135 scopus 로고
    • Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography
    • M. Koida, and R. Walter Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography J. Biol. Chem. 251 1976 7593 7599
    • (1976) J. Biol. Chem. , vol.251 , pp. 7593-7599
    • Koida, M.1    Walter, R.2
  • 21
    • 67749142086 scopus 로고    scopus 로고
    • Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates
    • J. Lee, J. McIntosh, B.J. Hathaway, and E.W. Schmidt Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates J. Am. Chem. Soc. 131 2009 2122 2124
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2122-2124
    • Lee, J.1    McIntosh, J.2    Hathaway, B.J.3    Schmidt, E.W.4
  • 22
    • 77954367132 scopus 로고    scopus 로고
    • Induced-fit mechanism for prolyl endopeptidase
    • M. Li, C. Chen, D.R. Davies, and T.K. Chiu Induced-fit mechanism for prolyl endopeptidase J. Biol. Chem. 285 2010 21487 21495
    • (2010) J. Biol. Chem. , vol.285 , pp. 21487-21495
    • Li, M.1    Chen, C.2    Davies, D.R.3    Chiu, T.K.4
  • 23
    • 84885378072 scopus 로고    scopus 로고
    • Illumina-based de novo transcriptome sequencing and analysis of Amanita exitialis basidiocarps
    • P. Li, W.Q. Deng, T.H. Li, B. Song, and Y.H. Shen Illumina-based de novo transcriptome sequencing and analysis of Amanita exitialis basidiocarps Gene 532 2013 63 71
    • (2013) Gene , vol.532 , pp. 63-71
    • Li, P.1    Deng, W.Q.2    Li, T.H.3    Song, B.4    Shen, Y.H.5
  • 24
    • 84896980201 scopus 로고    scopus 로고
    • The molecular diversity of toxin gene families in lethal Amanita mushrooms
    • P. Li, W. Deng, and T. Li The molecular diversity of toxin gene families in lethal Amanita mushrooms Toxicon 83 2014 59 68
    • (2014) Toxicon , vol.83 , pp. 59-68
    • Li, P.1    Deng, W.2    Li, T.3
  • 25
    • 67650594524 scopus 로고    scopus 로고
    • Processing of the phalloidin proprotein by prolyl oligopeptidase from the mushroom Conocybe albipes
    • H. Luo, H.E. Hallen-Adams, and J.D. Walton Processing of the phalloidin proprotein by prolyl oligopeptidase from the mushroom Conocybe albipes J. Biol. Chem. 284 2009 18070 18077
    • (2009) J. Biol. Chem. , vol.284 , pp. 18070-18077
    • Luo, H.1    Hallen-Adams, H.E.2    Walton, J.D.3
  • 26
    • 78649816006 scopus 로고    scopus 로고
    • Colocalization of amanitin and a candidate toxin-processing prolyl oligopeptidase in Amanita basidiocarps
    • H. Luo, H.E. Hallen-Adams, J.S. Scott-Craig, and J.D. Walton Colocalization of amanitin and a candidate toxin-processing prolyl oligopeptidase in Amanita basidiocarps Eukaryot. Cell 9 2010 1891 1900
    • (2010) Eukaryot. Cell , vol.9 , pp. 1891-1900
    • Luo, H.1    Hallen-Adams, H.E.2    Scott-Craig, J.S.3    Walton, J.D.4
  • 28
    • 35048844271 scopus 로고    scopus 로고
    • Tryptathionine bridges in peptide synthesis
    • J.P. May, and D.M. Perrin Tryptathionine bridges in peptide synthesis Biopolymers 88 2007 714 724
    • (2007) Biopolymers , vol.88 , pp. 714-724
    • May, J.P.1    Perrin, D.M.2
  • 29
    • 84906318100 scopus 로고    scopus 로고
    • Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis
    • G.K.T. Nguyen, S. Wang, Y. Qiu, X. Hemu, Y. Lian, and J.P. Tam Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis Nat. Chem. Biol. 10 2014 732 738
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 732-738
    • Nguyen, G.K.T.1    Wang, S.2    Qiu, Y.3    Hemu, X.4    Lian, Y.5    Tam, J.P.6
  • 30
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • T.J. Oman, and W.A. van der Donk Follow the leader: the use of leader peptides to guide natural product biosynthesis Nat. Chem. Biol. 6 2010 9 18
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 33
    • 84919923378 scopus 로고    scopus 로고
    • Profiling of amatoxins and phallotoxins in the genus Lepiota by liquid chromatography combined with UV absorbance and mass spectrometry
    • R.M. Sgambelluri, S. Epis, D. Sassera, H. Luo, E.R. Angelos, and J.D. Walton Profiling of amatoxins and phallotoxins in the genus Lepiota by liquid chromatography combined with UV absorbance and mass spectrometry Toxins (Basel) 6 2014 2336 2347
    • (2014) Toxins (Basel) , vol.6 , pp. 2336-2347
    • Sgambelluri, R.M.1    Epis, S.2    Sassera, D.3    Luo, H.4    Angelos, E.R.5    Walton, J.D.6
  • 34
    • 41949135032 scopus 로고    scopus 로고
    • Structure, function and biological relevance of prolyl oligopeptidase
    • Z. Szeltner, and L. Polgár Structure, function and biological relevance of prolyl oligopeptidase Curr. Protein Pept. Sci. 9 2008 96 107
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 96-107
    • Szeltner, Z.1    Polgár, L.2
  • 35
    • 84864452901 scopus 로고    scopus 로고
    • PEP-FOLD: An updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides
    • P. Thévenet, Y. Shen, J. Maupetit, F. Guyon, P. Derreumaux, and P. Tufféry PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides Nucleic Acids Res. 40 2012 W288 W293
    • (2012) Nucleic Acids Res. , vol.40 , pp. 288-W293
    • Thévenet, P.1    Shen, Y.2    Maupetit, J.3    Guyon, F.4    Derreumaux, P.5    Tufféry, P.6
  • 37
    • 0030267197 scopus 로고    scopus 로고
    • Host-selective toxins: Agents of compatibility
    • J.D. Walton Host-selective toxins: agents of compatibility Plant Cell 8 1996 1723 1733
    • (1996) Plant Cell , vol.8 , pp. 1723-1733
    • Walton, J.D.1
  • 40
    • 84861615565 scopus 로고    scopus 로고
    • Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment
    • C.T. Wong, D.K. Rowlands, C.H. Wong, T.W. Lo, G.K. Nguyen, H.Y. Li, and J.P. Tam Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment Angew. Chem. Int. Ed. Engl. 51 2012 5620 5624
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 5620-5624
    • Wong, C.T.1    Rowlands, D.K.2    Wong, C.H.3    Lo, T.W.4    Nguyen, G.K.5    Li, H.Y.6    Tam, J.P.7


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