메뉴 건너뛰기




Volumn 51, Issue 11, 2012, Pages 2265-2275

Distribution and properties of the genes encoding the biosynthesis of the bacterial cofactor, pyrroloquinoline quinone

Author keywords

[No Author keywords available]

Indexed keywords

CARBON UTILIZATION; COFACTORS; DESIGN AND APPLICATION; EVOLUTIONARY CONSERVATIONS; GENE ORDERS; GENE PRODUCTS; GENES ENCODING; PROTEIN-PROTEIN INTERACTIONS; PYRROLOQUINOLINE QUINONE; REDOX ACTIVE MOLECULES; STRUCTURE-BASED; THREE-DIMENSIONAL STRUCTURE;

EID: 84858693177     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201763d     Document Type: Article
Times cited : (99)

References (57)
  • 1
    • 0035212690 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes
    • Anthony, C. (2001) Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes Antioxid. Redox Signaling 3, 757-774 (Pubitemid 33131268)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.5 , pp. 757-774
    • Anthony, C.1
  • 2
    • 0031733482 scopus 로고    scopus 로고
    • The biochemistry, physiology and genetics of PQQ and PQQ-containing enzymes
    • Goodwin, P. M. and Anthony, C. (1998) The biochemistry, physiology and genetics of PQQ and PQQ-containing enzymes Adv. Microb. Physiol. 40, 1-80 (Pubitemid 28537738)
    • (1998) Advances in Microbial Physiology , vol.40 , pp. 1-80
    • Goodwin, P.M.1    Anthony, C.2
  • 3
    • 0030595043 scopus 로고    scopus 로고
    • Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically engineered Escherichia coli strain capable of PQQ biosynthesis
    • DOI 10.1016/0168-1656(96)01540-4
    • Sode, K., Ito, K., Witarto, A. B., Watanabe, K., Yoshida, H., and Postma, P. (1996) Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically engineered Escherichia coli strain capable of PQQ biosynthesis J. Biotechnol. 49, 239-243 (Pubitemid 26316259)
    • (1996) Journal of Biotechnology , vol.49 , Issue.1-3 , pp. 239-243
    • Sode, K.1    Ito, K.2    Witarto, A.B.3    Watanabe, K.4    Yoshida, H.5    Postma, P.6
  • 4
    • 0026549104 scopus 로고
    • Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon
    • Meulenberg, J. J., Sellink, E., Riegman, N. H., and Postma, P. W. (1992) Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon Mol. Gen. Genet. 232, 284-294
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 284-294
    • Meulenberg, J.J.1    Sellink, E.2    Riegman, N.H.3    Postma, P.W.4
  • 5
    • 0029148096 scopus 로고
    • Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection of an intermediate in the biosynthetic pathway
    • Velterop, J. S., Sellink, E., Meulenberg, J. J., David, S., Bulder, I., and Postma, P. W. (1995) Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection of an intermediate in the biosynthetic pathway J. Bacteriol. 177, 5088-5098
    • (1995) J. Bacteriol. , vol.177 , pp. 5088-5098
    • Velterop, J.S.1    Sellink, E.2    Meulenberg, J.J.3    David, S.4    Bulder, I.5    Postma, P.W.6
  • 7
    • 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., 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
  • 9
    • 77956457511 scopus 로고    scopus 로고
    • Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily
    • Wecksler, S. R., Stoll, S., Iavarone, A. T., Imsand, E. M., Tran, H., Britt, R. D., and Klinman, J. P. (2010) Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily Chem. Commun. 46, 7031-7033
    • (2010) Chem. Commun. , vol.46 , pp. 7031-7033
    • Wecksler, S.R.1    Stoll, S.2    Iavarone, A.T.3    Imsand, E.M.4    Tran, H.5    Britt, R.D.6    Klinman, J.P.7
  • 10
    • 0024074157 scopus 로고
    • Localization of a pyrroloquinoline quinone biosynthesis gene near the methanol dehydrogenase structural gene in Methylobacterium organophilum DSM 760
    • Mazodier, P., Biville, F., Turlin, E., and Gasser, F. (1988) Localization of a pyrroloquinoline quinone biosynthesis gene near the methanol dehydrogenase structural gene in Methylobacterium organophilum DSM 760 J. Gen. Microbiol. 134, 2513-2524
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2513-2524
    • Mazodier, P.1    Biville, F.2    Turlin, E.3    Gasser, F.4
  • 12
    • 0032558419 scopus 로고    scopus 로고
    • ATP/GTP hydrolysis is required for oxazole and thiazole biosynthesis in the peptide antibiotic microcin B17
    • DOI 10.1021/bi980996e
    • Milne, J. C., Eliot, A. C., Kelleher, N. L., and Walsh, C. T. (1998) ATP/GTP hydrolysis is required for oxazole and thiazole biosynthesis in the peptide antibiotic microcin B17 Biochemistry 37, 13250-13261 (Pubitemid 28449569)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13250-13261
    • Milne, J.C.1    Eliot, A.C.2    Kelleher, N.L.3    Walsh, C.T.4
  • 13
    • 79851508812 scopus 로고    scopus 로고
    • Genome mining for ribosomally synthesized natural products
    • Velasquez, J. E. and van der Donk, W. A. (2011) Genome mining for ribosomally synthesized natural products Curr. Opin. Chem. Biol. 15, 11-21
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 11-21
    • Velasquez, J.E.1    Van Der Donk, W.A.2
  • 14
    • 77957256569 scopus 로고    scopus 로고
    • A family of diiron monooxygenases catalyzing amino acid β-hydroxylation in antibiotic biosynthesis
    • Makris, T. M., Chakrabarti, M., Muenck, E., and Lipscomb, J. D. (2010) A family of diiron monooxygenases catalyzing amino acid β-hydroxylation in antibiotic biosynthesis Proc. Natl. Acad. Sci. U.S.A. 107, 15391-15396
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15391-15396
    • Makris, T.M.1    Chakrabarti, M.2    Muenck, E.3    Lipscomb, J.D.4
  • 15
    • 77950626884 scopus 로고    scopus 로고
    • Cofactor-independent oxidases and oxygenases
    • Fetzner, S. and Steiner, R. A. (2010) Cofactor-independent oxidases and oxygenases Appl. Microbiol. Biotechnol. 86, 791-804
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 791-804
    • Fetzner, S.1    Steiner, R.A.2
  • 16
    • 33745171769 scopus 로고    scopus 로고
    • Structure of trichamide, a cyclic peptide from the bloom-forming cyanobacterium Tnchodesmium erythraeum, predicted from the genome sequence
    • DOI 10.1128/AEM.00380-06
    • Sudek, S., Haygood, M. G., Youssef, D. T., and Schmidt, E. W. (2006) Structure of trichamide, a cyclic peptide from the bloom-forming cyanobacterium Trichodesmium erythraeum, predicted from the genome sequence Appl. Environ. Microbiol. 72, 4382-4387 (Pubitemid 43894908)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.6 , pp. 4382-4387
    • Sudek, S.1    Haygood, M.G.2    Youssef, D.T.A.3    Schmidt, E.W.4
  • 17
    • 78651081719 scopus 로고    scopus 로고
    • Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners
    • Haft, D. H. (2011) Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners BMC Genomics 12, 21
    • (2011) BMC Genomics , vol.12 , pp. 21
    • Haft, D.H.1
  • 18
    • 76749158462 scopus 로고    scopus 로고
    • Getting started in structural phylogenomics
    • Sjolander, K. (2010) Getting started in structural phylogenomics PLoS Comput. Biol. 6, e1000621
    • (2010) PLoS Comput. Biol. , vol.6 , pp. 1000621
    • Sjolander, K.1
  • 19
    • 14144253677 scopus 로고    scopus 로고
    • Cyclization mechanism for the synthesis of macrocyclic antibiotic lankacidin in Streptomyces rochei
    • DOI 10.1016/j.chembiol.2005.01.009
    • Arakawa, K., Sugino, F., Kodama, K., Ishii, T., and Kinashi, H. (2005) Cyclization mechanism for the synthesis of macrocyclic antibiotic lankacidin in Streptomyces rochei Chem. Biol. 12, 249-256 (Pubitemid 40281332)
    • (2005) Chemistry and Biology , vol.12 , Issue.2 , pp. 249-256
    • Arakawa, K.1    Sugino, F.2    Kodama, K.3    Ishii, T.4    Kinashi, H.5
  • 20
    • 0029148096 scopus 로고
    • Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection of an intermediate in the biosynthetic pathway
    • Velterop, J. S., Sellink, E., Meulenberg, J. J., David, S., Bulder, I., and Postma, P. W. (1995) Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection of an intermediate in the biosynthetic pathway J. Bacteriol. 177, 5088-5098
    • (1995) J. Bacteriol. , vol.177 , pp. 5088-5098
    • Velterop, J.S.1    Sellink, E.2    Meulenberg, J.J.3    David, S.4    Bulder, I.5    Postma, P.W.6
  • 21
    • 0031049495 scopus 로고    scopus 로고
    • Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate
    • Toyama, H., Chistoserdova, L., and Lidstrom, M. E. (1997) Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate Microbiology (Reading, U.K.) 143, 595-602 (Pubitemid 27092198)
    • (1997) Microbiology , vol.143 , Issue.2 , pp. 595-602
    • Toyama, H.1    Chistoserdova, L.2    Lidstrom, M.E.3
  • 22
    • 33750467665 scopus 로고    scopus 로고
    • Knockout and overexpression of pyrroloquinoline quinone biosynthetic genes in Gluconobacter oxydans 621H
    • Hoelscher, T. and Goerisch, H. (2006) Knockout and overexpression of pyrroloquinoline quinone biosynthetic genes in Gluconobacter oxydans 621H J. Bacteriol. 188, 7668-7676
    • (2006) J. Bacteriol. , vol.188 , pp. 7668-7676
    • Hoelscher, T.1    Goerisch, H.2
  • 23
    • 70350520165 scopus 로고    scopus 로고
    • Mutations that disrupt either the pqq or the gdh gene of Rahnella aquatilis abolish the production of an antibacterial substance and result in reduced biological control of grapevine crown gall
    • Guo, Y. B., Li, J., Li, L., Chen, F., Wu, W., Wang, J., and Wang, H. (2009) Mutations that disrupt either the pqq or the gdh gene of Rahnella aquatilis abolish the production of an antibacterial substance and result in reduced biological control of grapevine crown gall Appl. Environ. Microbiol. 75, 6792-6803
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 6792-6803
    • Guo, Y.B.1    Li, J.2    Li, L.3    Chen, F.4    Wu, W.5    Wang, J.6    Wang, H.7
  • 25
    • 34248145506 scopus 로고    scopus 로고
    • FlowerPower: Clustering proteins into domain architecture classes for phylogenomic inference of protein function
    • Krishnamurthy, N., Brown, D., and Sjolander, K. (2007) FlowerPower: Clustering proteins into domain architecture classes for phylogenomic inference of protein function BMC Evol. Biol. 7 (Suppl. 1) S12
    • (2007) BMC Evol. Biol. , vol.7 , Issue.SUPPL. 1 , pp. 12
    • Krishnamurthy, N.1    Brown, D.2    Sjolander, K.3
  • 26
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh, K., Misawa, K., Kuma, K., and Miyata, T. (2002) MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform Nucleic Acids Res. 30, 3059-3066 (Pubitemid 34851225)
    • (2002) Nucleic Acids Research , vol.30 , Issue.14 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.-I.3    Miyata, T.4
  • 27
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • DOI 10.1093/bioinformatics/btl446
    • Stamatakis, A. (2006) RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models Bioinformatics 22, 2688-2690 (Pubitemid 44642609)
    • (2006) Bioinformatics , vol.22 , Issue.21 , pp. 2688-2690
    • Stamatakis, A.1
  • 30
    • 68149098461 scopus 로고    scopus 로고
    • Xanthomonas campestris PqqD in the pyrroloquinoline quinone biosynthesis operon adopts a novel saddle-like fold that possibly serves as a PQQ carrier
    • Tsai, T. Y., Yang, C. Y., Shih, H. L., Wang, A. H., and Chou, S. H. (2009) Xanthomonas campestris PqqD in the pyrroloquinoline quinone biosynthesis operon adopts a novel saddle-like fold that possibly serves as a PQQ carrier Proteins 76, 1042-1048
    • (2009) Proteins , vol.76 , pp. 1042-1048
    • Tsai, T.Y.1    Yang, C.Y.2    Shih, H.L.3    Wang, A.H.4    Chou, S.H.5
  • 31
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L. A. and Sternberg, M. J. (2009) Protein structure prediction on the Web: A case study using the Phyre server Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 32
    • 54949145058 scopus 로고    scopus 로고
    • INTREPID: Information-theoretic TREe traversal for Protein functional site identification
    • Sankararaman, S. and Sjolander, K. (2008) INTREPID: Information-theoretic TREe traversal for Protein functional site identification Bioinformatics 24, 2445-2452
    • (2008) Bioinformatics , vol.24 , pp. 2445-2452
    • Sankararaman, S.1    Sjolander, K.2
  • 34
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, Q., and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs Nucleic Acids Res. 25, 3389-3402 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 35
    • 0025830659 scopus 로고
    • Quinoproteins: Enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone, or tryptophan-tryptophan quinone
    • Duine, J. A. (1991) Quinoproteins: Enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone, or tryptophan-tryptophan quinone Eur. J. Biochem. 200, 271-284
    • (1991) Eur. J. Biochem. , vol.200 , pp. 271-284
    • Duine, J.A.1
  • 36
    • 84858662419 scopus 로고    scopus 로고
    • Use of GDH-PQQ glucose meter systems in patients receiving maltose-containing therapies
    • Vol. Springer, Berlin
    • Virdi, N. S., Price, D., Ellison, J., Yadalam, S., and Nigam, S. (2010) Use of GDH-PQQ glucose meter systems in patients receiving maltose-containing therapies. Diabetologia, Vol. 53, Springer, Berlin.
    • (2010) Diabetologia , vol.53
    • Virdi, N.S.1    Price, D.2    Ellison, J.3    Yadalam, S.4    Nigam, S.5
  • 37
    • 0030210340 scopus 로고    scopus 로고
    • Gene order is not conserved in bacterial evolution
    • Mushegian, A. R. and Koonin, E. V. (1996) Gene order is not conserved in bacterial evolution Trends Genet. 12, 289-290
    • (1996) Trends Genet. , vol.12 , pp. 289-290
    • Mushegian, A.R.1    Koonin, E.V.2
  • 38
    • 0642312313 scopus 로고    scopus 로고
    • Evolution of mosaic operons by horizontal gene transfer and gene displacement in situ
    • Omelchendo, M. V., Makarova, K. S., Wolf, Y. I., Rogozin, I. B., and Koonin, E. V. (2003) Evolution of mosaic operons by horizontal gene transfer and gene displacement in situ Fenome Biol. 4, R55
    • (2003) Fenome Biol. , vol.4 , pp. 55
    • Omelchendo, M.V.1    Makarova, K.S.2    Wolf, Y.I.3    Rogozin, I.B.4    Koonin, E.V.5
  • 39
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: A fingerprint of proteins that physically interact
    • Dendekar, T., Snel, B., Huynen, M., and Bork, P. (1998) Conservation of gene order: A fingerprint of proteins that physically interact Trends Biochem. Sci. 23, 432-328
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 432-328
    • Dendekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 40
    • 70349979682 scopus 로고    scopus 로고
    • Origin and evolution of operons and metabolic pathways
    • Fondi, M., Emiliani, G., and Fani, R. (2009) Origin and evolution of operons and metabolic pathways Res. Microbiol. 160, 502-512
    • (2009) Res. Microbiol. , vol.160 , pp. 502-512
    • Fondi, M.1    Emiliani, G.2    Fani, R.3
  • 41
    • 42149106127 scopus 로고    scopus 로고
    • The pyrroloquinoline quinone biosynthesis pathway revisited: A structural approach
    • Puehringer, S., Metlitzky, M., and Schwarzenbacher, R. (2008) The pyrroloquinoline quinone biosynthesis pathway revisited: A structural approach BMC Biochem. 9, 8
    • (2008) BMC Biochem. , vol.9 , pp. 8
    • Puehringer, S.1    Metlitzky, M.2    Schwarzenbacher, R.3
  • 43
    • 1642264726 scopus 로고    scopus 로고
    • Crystallographic Comparison of Manganese- and Iron-Dependent Homoprotocatechuate 2,3-Dioxygenases
    • DOI 10.1128/JB.186.7.1945-1958.2004
    • Vetting, M. W., Wackett, L. P., Que, L., Jr., Lipscomb, J. D., and Ohlendorf, D. H. (2004) Crystaollographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygnases J. Bacteriol. 186, 1945-1958 (Pubitemid 38381182)
    • (2004) Journal of Bacteriology , vol.186 , Issue.7 , pp. 1945-1958
    • Vetting, M.W.1    Wackett, L.P.2    Que Jr., L.3    Lipscomb, J.D.4    Ohlendorf, D.H.5
  • 44
    • 56549087893 scopus 로고    scopus 로고
    • Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: Recent developments in enzymology and modeling studies
    • Bruijnincx, P. C. A., van Koten, G., and Gebbink, R. J. M. K. (2008) Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent developments in enzymology and modeling studies Chem. Soc. Rev. 37, 2716-2744
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 2716-2744
    • Bruijnincx, P.C.A.1    Van Koten, G.2    Gebbink, R.J.M.K.3
  • 45
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
    • DOI 10.1007/s00775-005-0624-x
    • Koehntop, K. D., Emerson, J. P., and Que, L., Jr. (2005) The 2-His-1-carboxylate facial triad: A versatile platform for dioxyygen activation by mononuclear non-heme iron(II) enzymes J. Biol. Inorg. Chem. 10, 87-93 (Pubitemid 40569003)
    • (2005) Journal of Biological Inorganic Chemistry , vol.10 , Issue.2 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que Jr., L.3
  • 46
    • 77957256569 scopus 로고    scopus 로고
    • A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis
    • Makris, T. M., Chakrabarti, M., Münck, E., and Lipscomb, J. D. (2010) A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis Proc. Natl. Acad. Sci. U.S.A. 107, 15391-15396
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15391-15396
    • Makris, T.M.1    Chakrabarti, M.2    Münck, E.3    Lipscomb, J.D.4
  • 47
    • 0029845902 scopus 로고    scopus 로고
    • The nicotinamide dinucleotide binding motif: A comparison of nucleotide binding proteins
    • Bellamacina, C. R. (1996) Protein motifs. 9. The nicotinamide dinucleotide binding motif: A comparison of nucleotide binding proteins FASEB J. 10, 1257-1269 (Pubitemid 26307511)
    • (1996) FASEB Journal , vol.10 , Issue.11 , pp. 1257-1269
    • Bellamacina, C.R.1
  • 48
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • DOI 10.1110/ps.12801
    • Dym, O. and Eisenber, D. (2001) Sequence-structure analysis of FAD-containing proteins Protein Sci. 10, 1712-1728 (Pubitemid 32848768)
    • (2001) Protein Science , vol.10 , Issue.9 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 49
    • 2342652839 scopus 로고    scopus 로고
    • The Structure of a Biosynthetic Intermediate of Pyrroloquinoline Quinone (PQQ) and Elucidation of the Final Step of PQQ Biosynthesis
    • DOI 10.1021/ja0493852
    • Magnusson, O. T., Toyama, H., Saeki, M., Schwarzenbacher, R., and Klinman, J. P. (2004) The structure of a biosynthetic intermediate of pyrroloquinoline quinone (PQQ) and elucidation of the final step of PQQ biosynthesis J. Am. Chem. Soc. 126, 5342-5343 (Pubitemid 38596330)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.17 , pp. 5342-5343
    • Magnusson, O.T.1    Toyama, H.2    Saeki, M.3    Schwarzenbacher, R.4    Klinman, J.P.5
  • 50
    • 14044270800 scopus 로고    scopus 로고
    • Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II
    • DOI 10.1021/bi0478648
    • Toms, A. V., Haas, A. L., Park, J. H., Begley, T. P., and Ealick, S. E. (2005) Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II Biochemistry 44, 2319-2329 (Pubitemid 40279536)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2319-2329
    • Toms, A.V.1    Haas, A.L.2    Park, J.-H.3    Begley, T.P.4    Ealick, S.E.5
  • 51
    • 34250850181 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone biogenesis: Characterization of PqqC and its H84N and H84A active site variants
    • DOI 10.1021/bi700162n
    • Magnusson, O. T., RoseFigura, J. M., Toyama, H., Schwarzenbacher, R., and Klinman, J. P. (2007) Pyrroloquinoline quinone biogenesis: Characterization of PqqC and its H84N and H84A active site variants Biochemistry 46, 7174-7186 (Pubitemid 46973991)
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7174-7186
    • Magnusson, O.Th.1    Rosefigura, J.M.2    Toyama, H.3    Schwarzenbacher, R.4    Klinman, J.P.5
  • 54
    • 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., 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
  • 56
    • 79954499453 scopus 로고    scopus 로고
    • Structural insights into radical generation by the radical SAM superfamily
    • Vey, J. L. and Drennan, C. L. (2011) Structural insights into radical generation by the radical SAM superfamily Chem. Rev. 111, 2487-2506
    • (2011) Chem. Rev. , vol.111 , pp. 2487-2506
    • Vey, J.L.1    Drennan, C.L.2
  • 57
    • 3242882336 scopus 로고    scopus 로고
    • AdoMet radical proteins - From structure to evolution - Alignment of divergent protein sequences reveals strong secondary structure element conservation
    • DOI 10.1093/nar/gkh728
    • Nicolet, Y. and Drennan, C. L. (2004) AdoMet radical proteins - from structure to evolution - alignment of divergent protein sequences reveals strong secondary structure element conservation Nucleic Acids Res. 13, 4015-4025 (Pubitemid 39199093)
    • (2004) Nucleic Acids Research , vol.32 , Issue.13 , pp. 4015-4025
    • Nicolet, Y.1    Drennan, C.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.