메뉴 건너뛰기




Volumn 291, Issue 17, 2016, Pages 8877-8884

Demonstration that the radical s-adenosylmethionine (SAM) Enzyme PqqE catalyzes de novo carbon-carbon cross-linking within a peptide substrate PqqA in the presence of the peptide chaperone PqqD

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; CHAINS; COVALENT BONDS; ENZYME ACTIVITY; PROTEINS;

EID: 84965043992     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C115.699918     Document Type: Article
Times cited : (102)

References (32)
  • 1
    • 0033199638 scopus 로고    scopus 로고
    • The PQQ story
    • Duine, J. A. (1999) The PQQ story. J. Biosci. Bioeng. 88, 231-236
    • (1999) J. Biosci. Bioeng , vol.88 , pp. 231-236
    • Duine, J.A.1
  • 2
    • 84858693177 scopus 로고    scopus 로고
    • Distribution and properties of the genes encoding the biosyn thesis of the bacterial cofactor, pyrroloquinoline quinone
    • Shen, Y.-Q., Bonnot, F., Imsand, E.M., RoseFigura, J.M., Sjölander, K., and Klinman, J.P. (2012) Distribution and properties of the genes encoding the biosyn thesis of the bacterial cofactor, pyrroloquinoline quinone. Biochemistry 51, 2265-2275
    • (2012) Biochemistry , vol.51 , pp. 2265-2275
    • Shen, Y.-Q.1    Bonnot, F.2    Imsand, E.M.3    RoseFigura, J.M.4    Sjölander, K.5    Klinman, J.P.6
  • 3
    • 0024264166 scopus 로고
    • A search for intermediates in the bacterial biosynthesis of PQQ
    • van Kleef, M. A., and Duine, J. A. (1988) A search for intermediates in the bacterial biosynthesis of PQQ. Biofactors 1, 297-302
    • (1988) Biofactors , vol.1 , pp. 297-302
    • Van Kleef, M.A.1    Duine, J.A.2
  • 4
    • 0023129319 scopus 로고
    • Cloning of the genes involved in synthesis of coenzyme pyrrolo-quinoline-quinone from acinetobacter calcoaceticus
    • Goosen, N., and Vermaas., D. A., and van de Putte, P. (1987) Cloning of the genes involved in synthesis of coenzyme pyrrolo-quinoline-quinone from Acinetobacter calcoaceticus. J. Bacteriol. 169, 303-307
    • (1987) J. Bacteriol , vol.169 , pp. 303-307
    • Goosen, N.1    Vermaas, D.A.2    Van De Putte, P.3
  • 6
    • 84880073719 scopus 로고    scopus 로고
    • Multistep, eightelectron oxidation catalyzed by the cofactorless oxidase, PqqC: Identification of chemical intermediates and their dependence on molecular oxygen
    • Bonnot, F., and Iavarone., A. T., and Klinman, J. P. (2013) Multistep, eightelectron oxidation catalyzed by the cofactorless oxidase, PqqC: identification of chemical intermediates and their dependence on molecular oxygen. Biochemistry 52, 4667-4675
    • (2013) Biochemistry , vol.52 , pp. 4667-4675
    • Bonnot, F.1    Iavarone, A.T.2    Klinman, J.P.3
  • 7
    • 84897981321 scopus 로고    scopus 로고
    • The intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: Pqq, TTQ, CTQ, TPQ and LTQ
    • Klinman, J. P., and Bonnot, F. (2014) The intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ and LTQ. Chem. Rev. 114, 4343-4365
    • (2014) Chem. Rev , vol.114 , pp. 4343-4365
    • Klinman, J.P.1    Bonnot, F.2
  • 10
    • 79958173211 scopus 로고    scopus 로고
    • Biological systems discovery in silico: Radical S-adenosylmethionine protein families and their target peptides for posttranslational modification
    • Haft, D. H., and Basu, M. K. (2011) Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification. J. Bacteriol. 193, 2745-2755
    • (2011) J. Bacteriol , vol.193 , pp. 2745-2755
    • Haft, D.H.1    Basu, M.K.2
  • 11
    • 84922901929 scopus 로고    scopus 로고
    • SPASM and twitch domains in AdoMet radical enzyme structures
    • Grell, T. A. J., and Goldman., P. J., and Drennan, C. L. (2015) SPASM and Twitch domains in AdoMet radical enzyme structures. J. Biol. Chem. 290, 3964-3971
    • (2015) J. Biol. Chem , vol.290 , pp. 3964-3971
    • Grell, T.A.J.1    Goldman, P.J.2    Drennan, C.L.3
  • 12
    • 84929340856 scopus 로고    scopus 로고
    • PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway
    • Latham, J. A., and Iavarone., A. T., Barr, I., Juthani, P. V., and Klinman, J. P. (2015) PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway. J. Biol. Chem. 290, 12908-12918
    • (2015) J. Biol. Chem , vol.290 , pp. 12908-12918
    • Latham, J.A.1    Iavarone, A.T.2    Barr, I.3    Juthani, P.V.4    Klinman, J.P.5
  • 13
    • 84937438220 scopus 로고    scopus 로고
    • A prevalent peptide-binding domain guides ribosomal natural product biosynthesis
    • Burkhart, B. J., and Hudson., G. A., Dunbar, K. L., and Mitchell, D. A. (2015) A prevalent peptide-binding domain guides ribosomal natural product biosynthesis. Nat Chem. Biol. 11, 564-570
    • (2015) Nat Chem. Biol , vol.11 , pp. 564-570
    • Burkhart, B.J.1    Hudson, G.A.2    Dunbar, K.L.3    Mitchell, D.A.4
  • 14
    • 84937415883 scopus 로고    scopus 로고
    • Biosynthesis: Leading the way to RiPPs
    • Link, A. J. (2015) Biosynthesis: leading the way to RiPPs. Nat. Chem. Biol. 11, 551-552
    • (2015) Nat. Chem. Biol , vol.11 , pp. 551-552
    • Link, A.J.1
  • 16
    • 0031282326 scopus 로고    scopus 로고
    • Escherichia coli flavodoxin sepharose as an affinity resin for cytochromes P450 and use to identify a putative cytochrome P450c17ββ-hydroxysteroid dehydrogenase interaction
    • Jenkins, CM, Pikuleva, I., Kagawa, N., and Waterman, M. R. (1997) Escherichia coli flavodoxin Sepharose as an affinity resin for cytochromes P450 and use to identify a putative cytochrome P450c17ββ-hydroxysteroid dehydrogenase interaction. Arch. Biochem. Biophys. 347, 93-102
    • (1997) Arch. Biochem. Biophys , vol.347 , pp. 93-102
    • Jenkins, C.M.1    Pikuleva, I.2    Kagawa, N.3    Waterman, M.R.4
  • 17
    • 0032574756 scopus 로고    scopus 로고
    • NADPH-flavodoxin reductase and flavodoxin from Escherichia coli: Characteristics as a soluble microsomal P450 reductase
    • Jenkins, C. M., and Waterman, M. R. (1998) NADPH-flavodoxin reductase and flavodoxin from Escherichia coli: characteristics as a soluble microsomal P450 reductase. Biochemistry 37, 6106-6113
    • (1998) Biochemistry , vol.37 , pp. 6106-6113
    • Jenkins, C.M.1    Waterman, M.R.2
  • 18
    • 84908105194 scopus 로고    scopus 로고
    • Techniques for the production, isolation, and analysis of iron-sulfur proteins
    • Crack, J. C, Green, J., and Thomson., A. J., and Le Brun, N. E. (2014) Techniques for the production, isolation, and analysis of iron-sulfur proteins. Methods Mol Biol. 1122, 33-48
    • (2014) Methods Mol Biol , vol.1122 , pp. 33-48
    • Crack, J.C.1    Green, J.2    Thomson, A.J.3    Le Brun, N.E.4
  • 19
    • 0001401289 scopus 로고
    • A systematic approach to standard addition methods in instrumental analysis
    • Bader, M. (1980) A systematic approach to standard addition methods in instrumental analysis. J. Chem. Educ. 57, 703
    • (1980) J. Chem. Educ , vol.57 , pp. 703
    • Bader, M.1
  • 20
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 21
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • Zor, T., and Selinger, Z. (1996) Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal. Biochem. 236, 302-308
    • (1996) Anal. Biochem , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2
  • 22
    • 70350236635 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone biogenesis: Demonstration that PqqE from klebsiella pneumoniae is a radical S-adenosyl-L-methionine enzyme
    • Wecksler, S. R., Stoll, S., Tran, H., Magnusson, O. T., Wu, S.-P., King, D., and Britt., R. D., and Klinman, J. P. (2009) Pyrroloquinoline quinone biogenesis: demonstration that PqqE from Klebsiella pneumoniae is a radical S-adenosyl-L-methionine enzyme. Biochemistry 48, 10151-10161
    • (2009) Biochemistry , vol.48 , pp. 10151-10161
    • Wecksler, S.R.1    Stoll, S.2    Tran, H.3    Magnusson, O.T.4    Wu, S.-P.5    King, D.6    Britt, R.D.7    Klinman, J.P.8
  • 23
    • 84964871897 scopus 로고    scopus 로고
    • PqqE from methylobacterium extorquens AM1: A radical S-adenosyl-L-methionine enzyme with an unusual tolerance to oxygen
    • Saichana, N., Tanizawa, K., Pechousek, J., Novák, P., Yakushi, T., Toyama, H, and Frébortová, J. (2016) PqqE from Methylobacterium extorquens AM1: a radical S-adenosyl-L-methionine enzyme with an unusual tolerance to oxygen. J. Biochem. 159, 87-99
    • (2016) J. Biochem , vol.159 , pp. 87-99
    • Saichana, N.1    Tanizawa, K.2    Pechousek, J.3    Novák, P.4    Yakushi, T.5    Toyama, H.6    Frébortová, J.7
  • 25
    • 84878137190 scopus 로고    scopus 로고
    • X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification
    • Goldman, P. J., and Grove., T. L., Sites, L. A., McLaughlin, M. I., and Booker., S. J., and Drennan, C. L. (2013) X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification. Proc. Natl. Acad. Sci. U.S.A. 110, 8519-8524
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 8519-8524
    • Goldman, P.J.1    Grove, T.L.2    Sites, L.A.3    McLaughlin, M.I.4    Booker, S.J.5    Drennan, C.L.6
  • 26
    • 78149460648 scopus 로고    scopus 로고
    • A "radical dance" in thiamin biosynthesis: Mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase
    • Chatterjee, A., and Hazra., A. B., Abdelwahed, S., Hilmey, D. G., and Begley, T. P. (2010) A "radical dance" in thiamin biosynthesis: mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase. Angew. Chem. Int. Ed. Engl. 49, 8653-8656
    • (2010) Angew. Chem. Int. Ed. Engl , vol.49 , pp. 8653-8656
    • Chatterjee, A.1    Hazra, A.B.2    Abdelwahed, S.3    Hilmey, D.G.4    Begley, T.P.5
  • 28
    • 84934434331 scopus 로고    scopus 로고
    • The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation
    • Wieckowski, B. M., and Hegemann., J. D., Mielcarek, A., Boss, L., Burghaus, O., and Marahiel, M. A. (2015) The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation. FEBS Lett. 589, 1802-1806
    • (2015) FEBS Lett , vol.589 , pp. 1802-1806
    • Wieckowski, B.M.1    Hegemann, J.D.2    Mielcarek, A.3    Boss, L.4    Burghaus, O.5    Marahiel, M.A.6
  • 29
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff, P., and Fohlman, J. (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11, 601
    • (1984) Biomed. Mass Spectrom , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 32
    • 84928680795 scopus 로고    scopus 로고
    • Structure and biosynthesis of a macrocyclic peptide containing an unprecedented lysine-to-tryptophan crosslink
    • Schramma, K. R., and Bushin., L. B., and Seyedsayamdost, M. R. (2015) Structure and biosynthesis of a macrocyclic peptide containing an unprecedented lysine-to-tryptophan crosslink. Nat. Chem. 7, 431-437
    • (2015) Nat. Chem , vol.7 , pp. 431-437
    • Schramma, K.R.1    Bushin, L.B.2    Seyedsayamdost, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.