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Volumn 42, Issue 6, 2017, Pages 457-469

Flavins as Covalent Catalysts: New Mechanisms Emerge

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; ENTEROCIN; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; FLAVOPROTEIN; HISTONE DEMETHYLASE; MUTASE; NATURAL PRODUCT; OXIDOREDUCTASE; PARGYLINE; RASAGILINE; RIBOFLAVIN; THYMIDYLATE SYNTHASE; TRANYLCYPROMINE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GALACTOPYRANOSE MUTASE; RIBOFLAVIN DERIVATIVE;

EID: 85014390371     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2017.02.005     Document Type: Review
Times cited : (108)

References (81)
  • 1
    • 0021759003 scopus 로고
    • Reinvestigation of the structure of oxidized and reduced flavin: carbon-13 and nitrogen-15 nuclear magnetic resonance study
    • Moonen, C.T., et al. Reinvestigation of the structure of oxidized and reduced flavin: carbon-13 and nitrogen-15 nuclear magnetic resonance study. Biochemistry 23 (1984), 4859–4867.
    • (1984) Biochemistry , vol.23 , pp. 4859-4867
    • Moonen, C.T.1
  • 2
    • 84903294538 scopus 로고    scopus 로고
    • Flavins
    • G.C.K. Roberts Springer
    • Gadda, G., Flavins. Roberts, G.C.K., (eds.) Encyclopedia of Biophysics, 2013, Springer, 771–775.
    • (2013) Encyclopedia of Biophysics , pp. 771-775
    • Gadda, G.1
  • 3
    • 84870925950 scopus 로고    scopus 로고
    • Flavoenzymes: versatile catalysts in biosynthetic pathways
    • Walsh, C.T., Wencewicz, T.A., Flavoenzymes: versatile catalysts in biosynthetic pathways. Nat. Prod. Rep. 30 (2013), 175–200.
    • (2013) Nat. Prod. Rep. , vol.30 , pp. 175-200
    • Walsh, C.T.1    Wencewicz, T.A.2
  • 4
    • 0005948684 scopus 로고
    • Isolierung eines neuen gelben Ferments
    • Haas, E., Isolierung eines neuen gelben Ferments. Biochem. Z. 298 (1938), 378–390.
    • (1938) Biochem. Z. , vol.298 , pp. 378-390
    • Haas, E.1
  • 5
    • 0011365375 scopus 로고
    • Action mechanism of the old yellow enzyme
    • Nakamura, T., et al. Action mechanism of the old yellow enzyme. J. Biochem. 57 (1965), 554–564.
    • (1965) J. Biochem. , vol.57 , pp. 554-564
    • Nakamura, T.1
  • 6
    • 0017831143 scopus 로고
    • Chemical approaches to the study of enzymes catalyzing redox transformations
    • Walsh, C., Chemical approaches to the study of enzymes catalyzing redox transformations. Annu. Rev. Biochem. 47 (1978), 881–931.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 881-931
    • Walsh, C.1
  • 7
    • 0036919327 scopus 로고    scopus 로고
    • Flavoenzymes that catalyse reactions with no net redox change
    • Bornemann, S., Flavoenzymes that catalyse reactions with no net redox change. Nat. Prod. Rep. 19 (2002), 761–772.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 761-772
    • Bornemann, S.1
  • 8
    • 0035987236 scopus 로고    scopus 로고
    • ‘New uses for an old enzyme’ – the old yellow enzyme family of flavoenzymes
    • Williams, R.E., Bruce, N.C., ‘New uses for an old enzyme’ – the old yellow enzyme family of flavoenzymes. Microbiology 148 (2002), 1607–1614.
    • (2002) Microbiology , vol.148 , pp. 1607-1614
    • Williams, R.E.1    Bruce, N.C.2
  • 9
    • 16244383493 scopus 로고    scopus 로고
    • Predicting enzyme function from protein sequence
    • Minshull, J., et al. Predicting enzyme function from protein sequence. Curr. Opin. Chem. Biol. 9 (2005), 202–209.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 202-209
    • Minshull, J.1
  • 10
    • 79960570256 scopus 로고    scopus 로고
    • Flavogenomics–a genomic and structural view of flavin-dependent proteins
    • Macheroux, P., et al. Flavogenomics–a genomic and structural view of flavin-dependent proteins. FEBS J. 278 (2011), 2625–2634.
    • (2011) FEBS J. , vol.278 , pp. 2625-2634
    • Macheroux, P.1
  • 12
    • 84921436886 scopus 로고    scopus 로고
    • Flavins and flavoproteins: applications in medicine
    • Jortzik, E., et al. Flavins and flavoproteins: applications in medicine. Methods Mol. Biol. 1146 (2014), 113–157.
    • (2014) Methods Mol. Biol. , vol.1146 , pp. 113-157
    • Jortzik, E.1
  • 13
    • 0029038909 scopus 로고
    • Introduction: flavoprotein structure and mechanism
    • Massey, V., Introduction: flavoprotein structure and mechanism. FASEB J. 9 (1995), 473–475.
    • (1995) FASEB J. , vol.9 , pp. 473-475
    • Massey, V.1
  • 14
    • 68149166459 scopus 로고    scopus 로고
    • Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain
    • Stuehr, D.J., et al. Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain. FEBS J. 276 (2009), 3959–3974.
    • (2009) FEBS J. , vol.276 , pp. 3959-3974
    • Stuehr, D.J.1
  • 15
    • 84962556232 scopus 로고    scopus 로고
    • Electron bifurcation
    • Peters, J.W., et al. Electron bifurcation. Curr. Opin. Chem. Biol. 31 (2016), 146–152.
    • (2016) Curr. Opin. Chem. Biol. , vol.31 , pp. 146-152
    • Peters, J.W.1
  • 16
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: diverse catalysts with recurrent features
    • Fraaije, M., Mattevi, A., Flavoenzymes: diverse catalysts with recurrent features. Trends Biochem. Sci. 25 (2000), 126–132.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.1    Mattevi, A.2
  • 17
    • 34047180214 scopus 로고    scopus 로고
    • New frontiers in structural flavoenzymology
    • De Colibus, L., Mattevi, A., New frontiers in structural flavoenzymology. Curr. Opin. Struc. Biol. 16 (2006), 722–728.
    • (2006) Curr. Opin. Struc. Biol. , vol.16 , pp. 722-728
    • De Colibus, L.1    Mattevi, A.2
  • 18
    • 0017879559 scopus 로고
    • The structure of the flavoenzyme glutathione reductase
    • Schulz, G.E., et al. The structure of the flavoenzyme glutathione reductase. Nature 273 (1978), 120–124.
    • (1978) Nature , vol.273 , pp. 120-124
    • Schulz, G.E.1
  • 19
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R.K., et al. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187 (1986), 101–107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1
  • 20
    • 84857807074 scopus 로고    scopus 로고
    • Blending Baeyer-Villiger monooxygenases: using a robust BVMO as a scaffold for creating chimeric enzymes with novel catalytic properties
    • van Beek, H.L., et al. Blending Baeyer-Villiger monooxygenases: using a robust BVMO as a scaffold for creating chimeric enzymes with novel catalytic properties. Chem. Commun. 48 (2012), 3288–3290.
    • (2012) Chem. Commun. , vol.48 , pp. 3288-3290
    • van Beek, H.L.1
  • 21
    • 84870713545 scopus 로고    scopus 로고
    • Noncanonical reactions of flavoenzymes
    • Sobrado, P., Noncanonical reactions of flavoenzymes. Int. J. Mol. Sci. 13 (2012), 16751–16768.
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 16751-16768
    • Sobrado, P.1
  • 22
    • 84954567664 scopus 로고    scopus 로고
    • Unusual flavoenzyme catalysis in marine bacteria
    • Teufel, R., et al. Unusual flavoenzyme catalysis in marine bacteria. Curr. Opin. Chem. Biol. 31 (2016), 31–39.
    • (2016) Curr. Opin. Chem. Biol. , vol.31 , pp. 31-39
    • Teufel, R.1
  • 23
    • 0014200553 scopus 로고
    • Reduktive photoalkylierung des flavinkerns und flavinkatalysierte photodecarboxylierung von phenylacetat studien in der flavinreihe
    • Walker, W.H., et al. Reduktive photoalkylierung des flavinkerns und flavinkatalysierte photodecarboxylierung von phenylacetat studien in der flavinreihe. Helv. Chim. Acta 50 (1967), 2269–2279.
    • (1967) Helv. Chim. Acta , vol.50 , pp. 2269-2279
    • Walker, W.H.1
  • 24
    • 0015785951 scopus 로고
    • Direct evidence for carbanions and covalent n5-flavin-carbanion adducts as catalytic intermediates in the oxidation of nitroethane by D-amino acid oxidase
    • Porter, D.J.T., et al. Direct evidence for carbanions and covalent n5-flavin-carbanion adducts as catalytic intermediates in the oxidation of nitroethane by D-amino acid oxidase. J. Biol. Chem. 248 (1973), 4400–4416.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4400-4416
    • Porter, D.J.T.1
  • 25
    • 0015926842 scopus 로고
    • Reaction of sulfite with isoalloxazines
    • Hevesi, L., Bruice, T.C., Reaction of sulfite with isoalloxazines. Biochemistry 12 (1973), 290–297.
    • (1973) Biochemistry , vol.12 , pp. 290-297
    • Hevesi, L.1    Bruice, T.C.2
  • 26
    • 0014669771 scopus 로고
    • Studies on milk xanthine oxidase: some spectral and kinetic properties
    • Massey, V., et al. Studies on milk xanthine oxidase: some spectral and kinetic properties. J. Biol. Chem. 244 (1969), 1682–1691.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1682-1691
    • Massey, V.1
  • 27
    • 0032619605 scopus 로고    scopus 로고
    • UV-visible spectroscopy as a tool to study flavoproteins
    • Macheroux, P., UV-visible spectroscopy as a tool to study flavoproteins. Methods Mol. Biol. 131 (1999), 1–7.
    • (1999) Methods Mol. Biol. , vol.131 , pp. 1-7
    • Macheroux, P.1
  • 28
    • 0242696227 scopus 로고    scopus 로고
    • Plant adenosine 5′-phosphosulfate reductase is a novel iron-sulfur protein
    • Kopriva, S., et al. Plant adenosine 5′-phosphosulfate reductase is a novel iron-sulfur protein. J. Biol. Chem. 276 (2001), 42881–42886.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42881-42886
    • Kopriva, S.1
  • 29
    • 33644670560 scopus 로고    scopus 로고
    • Reaction mechanism of the iron-sulfur flavoenzyme adenosine-5′-phosphosulfate reductase based on the structural characterization of different enzymatic states
    • Schiffer, A., et al. Reaction mechanism of the iron-sulfur flavoenzyme adenosine-5′-phosphosulfate reductase based on the structural characterization of different enzymatic states. Biochemistry 45 (2006), 2960–2967.
    • (2006) Biochemistry , vol.45 , pp. 2960-2967
    • Schiffer, A.1
  • 30
    • 0022863121 scopus 로고
    • Identifications of the true carbon-13 nuclear magnetic resonance spectrum of the stable intermediate II in bacterial luciferase
    • Vervoort, J., et al. Identifications of the true carbon-13 nuclear magnetic resonance spectrum of the stable intermediate II in bacterial luciferase. Biochemistry 25 (1986), 8062–8067.
    • (1986) Biochemistry , vol.25 , pp. 8062-8067
    • Vervoort, J.1
  • 31
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A., To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem. Sci. 31 (2006), 276–283.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 32
    • 84865435786 scopus 로고    scopus 로고
    • The enigmatic reaction of flavins with oxygen
    • Chaiyen, P., et al. The enigmatic reaction of flavins with oxygen. Trends Biochem. Sci. 37 (2012), 373–380.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 373-380
    • Chaiyen, P.1
  • 33
    • 84957582098 scopus 로고    scopus 로고
    • Handbook of Flavoproteins
    • De Gruyter
    • Hille, R., et al. Handbook of Flavoproteins. 2012, De Gruyter.
    • (2012)
    • Hille, R.1
  • 34
    • 4344593011 scopus 로고    scopus 로고
    • Identification of inhibitors for UDP-galactopyranose mutase
    • Soltero-Higgin, M., Identification of inhibitors for UDP-galactopyranose mutase. J. Am. Chem. Soc. 34 (2004), 10532–11263.
    • (2004) J. Am. Chem. Soc. , vol.34 , pp. 10532-11263
    • Soltero-Higgin, M.1
  • 35
    • 84944743977 scopus 로고    scopus 로고
    • Virtual screening for UDP-galactopyranose mutase ligands identifies a new class of antimycobacterial agents
    • Kincaid, V.A., et al. Virtual screening for UDP-galactopyranose mutase ligands identifies a new class of antimycobacterial agents. ACS Chem. Biol. 10 (2015), 2209–2218.
    • (2015) ACS Chem. Biol. , vol.10 , pp. 2209-2218
    • Kincaid, V.A.1
  • 36
    • 70449674082 scopus 로고    scopus 로고
    • Structural basis of substrate binding to UDP-galactopyranose mutase: crystal structures in the reduced and oxidized state complexed with UDP-galactopyranose and UDP
    • Partha, S.K., et al. Structural basis of substrate binding to UDP-galactopyranose mutase: crystal structures in the reduced and oxidized state complexed with UDP-galactopyranose and UDP. J. Mol. Biol. 394 (2009), 864–877.
    • (2009) J. Mol. Biol. , vol.394 , pp. 864-877
    • Partha, S.K.1
  • 37
    • 84868674867 scopus 로고    scopus 로고
    • Reversible and efficient inhibition of UDP-galactopyranose mutase by electrophilic, constrained and unsaturated UDP-galactitol analogues
    • Ansiaux, C., et al. Reversible and efficient inhibition of UDP-galactopyranose mutase by electrophilic, constrained and unsaturated UDP-galactitol analogues. Chem. Eur. J. 18 (2012), 14860–14866.
    • (2012) Chem. Eur. J. , vol.18 , pp. 14860-14866
    • Ansiaux, C.1
  • 38
    • 84893714579 scopus 로고    scopus 로고
    • Structure, mechanism, and dynamics of UDP-galactopyranose mutase
    • Tanner, J.J., et al. Structure, mechanism, and dynamics of UDP-galactopyranose mutase. Arch. Biochem. Biophys. 544 (2014), 128–141.
    • (2014) Arch. Biochem. Biophys. , vol.544 , pp. 128-141
    • Tanner, J.J.1
  • 39
    • 0034833650 scopus 로고    scopus 로고
    • Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes
    • Zhang, Q., Liu, H.-W., Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes. J. Am. Chem. Soc. 123 (2001), 6756–6766.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6756-6766
    • Zhang, Q.1    Liu, H.-W.2
  • 40
    • 84858635325 scopus 로고    scopus 로고
    • Chemical mechanism of UDP-galactopyranose mutase from Trypanosoma cruzi: a potential drug target against Chagas’ disease
    • Oppenheimer, M., et al. Chemical mechanism of UDP-galactopyranose mutase from Trypanosoma cruzi: a potential drug target against Chagas’ disease. PLoS One, 7, 2012, e32918.
    • (2012) PLoS One , vol.7 , pp. e32918
    • Oppenheimer, M.1
  • 41
    • 84958730031 scopus 로고    scopus 로고
    • In crystallo capture of a covalent intermediate in the UDP-galactopyranose mutase reaction
    • Mehra-Chaudhary, R., In crystallo capture of a covalent intermediate in the UDP-galactopyranose mutase reaction. Biochemistry 55 (2016), 833–836.
    • (2016) Biochemistry , vol.55 , pp. 833-836
    • Mehra-Chaudhary, R.1
  • 42
    • 84883819129 scopus 로고    scopus 로고
    • Ether lipid generating enzyme AGPS alters the balance of structural and signaling lipids to fuel cancer pathogenicity
    • Benjamin, D.I., et al. Ether lipid generating enzyme AGPS alters the balance of structural and signaling lipids to fuel cancer pathogenicity. Proc. Natl. Acad. Sci. U. S. A. 110 (2013), 14912–14917.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 14912-14917
    • Benjamin, D.I.1
  • 43
    • 84947909618 scopus 로고    scopus 로고
    • Discovery of inhibitors for the ether lipid-generating enzyme AGPS as Anti-cancer agents
    • Piano, V., et al. Discovery of inhibitors for the ether lipid-generating enzyme AGPS as Anti-cancer agents. ACS Chem. Biol. 10 (2015), 2589–2597.
    • (2015) ACS Chem. Biol. , vol.10 , pp. 2589-2597
    • Piano, V.1
  • 44
    • 34249898356 scopus 로고    scopus 로고
    • The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder
    • Razeto, A., et al. The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder. Structure 15 (2007), 683–692.
    • (2007) Structure , vol.15 , pp. 683-692
    • Razeto, A.1
  • 45
    • 84869210790 scopus 로고    scopus 로고
    • Precursor of ether phospholipids is synthesized by a flavoenzyme through covalent catalysis
    • Nenci, S., et al. Precursor of ether phospholipids is synthesized by a flavoenzyme through covalent catalysis. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 18791–18796.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 18791-18796
    • Nenci, S.1
  • 46
    • 44549085227 scopus 로고    scopus 로고
    • The growing VAO flavoprotein family
    • Leferink, N.G., et al. The growing VAO flavoprotein family. Arch. Biochem. Biophys. 474 (2008), 292–301.
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 292-301
    • Leferink, N.G.1
  • 47
    • 22844445708 scopus 로고    scopus 로고
    • Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria–evolutionary implications
    • Urbonavicius, J., et al. Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria–evolutionary implications. Nucleic Acids Res. 33 (2005), 3955–3964.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3955-3964
    • Urbonavicius, J.1
  • 48
    • 0037025191 scopus 로고    scopus 로고
    • An alternative flavin-dependent mechanism for thymidylate synthesis
    • Myllykallio, H., et al. An alternative flavin-dependent mechanism for thymidylate synthesis. Science 297 (2002), 105–107.
    • (2002) Science , vol.297 , pp. 105-107
    • Myllykallio, H.1
  • 49
    • 0004107159 scopus 로고
    • Metabolism of Nucleotides, Nucleosides and Nucleobases in Microorganisms
    • Academic Press
    • Munch-Petersen, A., Metabolism of Nucleotides, Nucleosides and Nucleobases in Microorganisms. 1983, Academic Press.
    • (1983)
    • Munch-Petersen, A.1
  • 50
    • 66349097175 scopus 로고    scopus 로고
    • Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase
    • Nishimasu, H., et al. Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 8180–8185.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8180-8185
    • Nishimasu, H.1
  • 51
    • 84866860266 scopus 로고    scopus 로고
    • Folate binding site of flavin-dependent thymidylate synthase
    • Koehn, E.M., et al. Folate binding site of flavin-dependent thymidylate synthase. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 15722–15727.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 15722-15727
    • Koehn, E.M.1
  • 52
    • 80054714992 scopus 로고    scopus 로고
    • Insights into folate/FAD-dependent tRNA methyltransferase mechanism: role of two highly conserved cysteines in catalysis
    • Hamdane, D., et al. Insights into folate/FAD-dependent tRNA methyltransferase mechanism: role of two highly conserved cysteines in catalysis. J. Biol. Chem. 286 (2011), 36268–36280.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36268-36280
    • Hamdane, D.1
  • 53
    • 84870665611 scopus 로고    scopus 로고
    • FAD/Folate-dependent tRNA methyltransferase: flavin as a new methyl-transfer agent
    • Hamdane, D., et al. FAD/Folate-dependent tRNA methyltransferase: flavin as a new methyl-transfer agent. J. Am. Chem. Soc. 134 (2012), 19739–19745.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 19739-19745
    • Hamdane, D.1
  • 54
    • 84890544860 scopus 로고    scopus 로고
    • Activation of a unique flavin-dependent tRNA-methylating agent
    • Hamdane, D., et al. Activation of a unique flavin-dependent tRNA-methylating agent. Biochemistry 52 (2013), 8949–8956.
    • (2013) Biochemistry , vol.52 , pp. 8949-8956
    • Hamdane, D.1
  • 55
    • 84975060712 scopus 로고    scopus 로고
    • Deprotonations in the reaction of flavin-dependent thymidylate synthase
    • Stull, F.W., et al. Deprotonations in the reaction of flavin-dependent thymidylate synthase. Biochemistry 55 (2016), 3261–3269.
    • (2016) Biochemistry , vol.55 , pp. 3261-3269
    • Stull, F.W.1
  • 56
    • 84906222459 scopus 로고    scopus 로고
    • Detection of intermediates in the oxidative half-reaction of the FAD-dependent thymidylate synthase from Thermotoga maritima: carbon transfer without covalent pyrimidine activation
    • Conrad, J.A., et al. Detection of intermediates in the oxidative half-reaction of the FAD-dependent thymidylate synthase from Thermotoga maritima: carbon transfer without covalent pyrimidine activation. Biochemistry 53 (2014), 5199–5207.
    • (2014) Biochemistry , vol.53 , pp. 5199-5207
    • Conrad, J.A.1
  • 57
    • 84956629678 scopus 로고    scopus 로고
    • An unprecedented mechanism of nucleotide methylation in organisms containing thyX
    • Mishanina, T.V., et al. An unprecedented mechanism of nucleotide methylation in organisms containing thyX. Science 351 (2016), 507–510.
    • (2016) Science , vol.351 , pp. 507-510
    • Mishanina, T.V.1
  • 58
    • 84958983372 scopus 로고    scopus 로고
    • Biosynthesis of coenzyme Q in eukaryotes
    • Kawamukai, M., Biosynthesis of coenzyme Q in eukaryotes. Biosci. Biotechnol. Biochem. 80 (2015), 23–33.
    • (2015) Biosci. Biotechnol. Biochem. , vol.80 , pp. 23-33
    • Kawamukai, M.1
  • 59
    • 84933073520 scopus 로고    scopus 로고
    • New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition
    • Payne, K.A., et al. New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Nature 522 (2015), 497–501.
    • (2015) Nature , vol.522 , pp. 497-501
    • Payne, K.A.1
  • 60
    • 85015310184 scopus 로고    scopus 로고
    • Oxidative maturation and structural characterization of prenylated-FMN binding by UbiD, a decarboxylase involved in bacterial ubiquinone biosynthesis. Published online January 5.
    • Marshall, S.A. et al. (2017) Oxidative maturation and structural characterization of prenylated-FMN binding by UbiD, a decarboxylase involved in bacterial ubiquinone biosynthesis. J. Biol. Chem. Published online January 5, 2017. http://dx.doi.org/jbc.M116.762732.
    • (2017) J. Biol. Chem.
    • Marshall, S.A.1
  • 61
    • 84933056649 scopus 로고    scopus 로고
    • UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis
    • White, M.D., et al. UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature 522 (2015), 502–506.
    • (2015) Nature , vol.522 , pp. 502-506
    • White, M.D.1
  • 63
    • 84973154405 scopus 로고    scopus 로고
    • Sweating the assets of flavin cofactors: new insight of chemical versatility from knowledge of structure and mechanism
    • Leys, D., Scrutton, N.S., Sweating the assets of flavin cofactors: new insight of chemical versatility from knowledge of structure and mechanism. Curr. Opin. Struc. Biol. 41 (2016), 19–26.
    • (2016) Curr. Opin. Struc. Biol. , vol.41 , pp. 19-26
    • Leys, D.1    Scrutton, N.S.2
  • 64
    • 84893737023 scopus 로고    scopus 로고
    • Flavin dependent monooxygenases
    • Huijbers, M.M., et al. Flavin dependent monooxygenases. Arch. Biochem. Biophys. 544 (2014), 2–17.
    • (2014) Arch. Biochem. Biophys. , vol.544 , pp. 2-17
    • Huijbers, M.M.1
  • 65
    • 0037149649 scopus 로고    scopus 로고
    • Mutational analysis of the enterocin Favorskii biosynthetic rearrangement
    • Xiang, L.K., et al. Mutational analysis of the enterocin Favorskii biosynthetic rearrangement. Org. Lett. 4 (2002), 957–960.
    • (2002) Org. Lett. , vol.4 , pp. 957-960
    • Xiang, L.K.1
  • 66
    • 8144227951 scopus 로고    scopus 로고
    • EncM, a versatile enterocin biosynthetic enzyme involved in Favorskii oxidative rearrangement, aldol condensation, and heterocycle-forming reactions
    • Xiang, L., et al. EncM, a versatile enterocin biosynthetic enzyme involved in Favorskii oxidative rearrangement, aldol condensation, and heterocycle-forming reactions. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 15609–15614.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15609-15614
    • Xiang, L.1
  • 67
    • 84888645117 scopus 로고    scopus 로고
    • Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement
    • Teufel, R., et al. Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature 503 (2013), 552–556.
    • (2013) Nature , vol.503 , pp. 552-556
    • Teufel, R.1
  • 68
    • 84935041606 scopus 로고    scopus 로고
    • Biochemical establishment and characterization of EncM's flavin-N5-oxide cofactor
    • Teufel, R., et al. Biochemical establishment and characterization of EncM's flavin-N5-oxide cofactor. J. Am. Chem. Soc. 137 (2015), 8078–8085.
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 8078-8085
    • Teufel, R.1
  • 69
    • 84971542390 scopus 로고    scopus 로고
    • Dibenzothiophene catabolism proceeds via a flavin-N5-oxide intermediate
    • Adak, S., Begley, T.P., Dibenzothiophene catabolism proceeds via a flavin-N5-oxide intermediate. J. Am. Chem. Soc. 138 (2016), 6424–6426.
    • (2016) J. Am. Chem. Soc. , vol.138 , pp. 6424-6426
    • Adak, S.1    Begley, T.P.2
  • 70
    • 84893737023 scopus 로고    scopus 로고
    • Flavin dependent monooxygenases
    • Huijbers, M.M., et al. Flavin dependent monooxygenases. Arch. Biochem. Biophys. 544 (2014), 2–17.
    • (2014) Arch. Biochem. Biophys. , vol.544 , pp. 2-17
    • Huijbers, M.M.1
  • 71
    • 66149173641 scopus 로고    scopus 로고
    • Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases
    • Edmondson, D.E., et al. Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases. Biochemistry 48 (2009), 4220–4230.
    • (2009) Biochemistry , vol.48 , pp. 4220-4230
    • Edmondson, D.E.1
  • 72
    • 0011669498 scopus 로고
    • A new approach to the analysis of the interaction between monoamineoxidase and its substrates and inhibitors
    • Zeller, E.A., A new approach to the analysis of the interaction between monoamineoxidase and its substrates and inhibitors. Annu. N. Y. Acad. Sci. 107 (1963), 811–821.
    • (1963) Annu. N. Y. Acad. Sci. , vol.107 , pp. 811-821
    • Zeller, E.A.1
  • 73
    • 0017228490 scopus 로고
    • Structure of flavin adducts with acetylenic substrates: chemistry of monoamine oxidase and lactate oxidase inhibition
    • Gärtner, B., et al. Structure of flavin adducts with acetylenic substrates: chemistry of monoamine oxidase and lactate oxidase inhibition. Eur. J. Biochem. 63 (1976), 211–221.
    • (1976) Eur. J. Biochem. , vol.63 , pp. 211-221
    • Gärtner, B.1
  • 74
    • 12144289182 scopus 로고    scopus 로고
    • Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class
    • Binda, C., et al. Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J. Med. Chem. 47 (2004), 1767–1774.
    • (2004) J. Med. Chem. , vol.47 , pp. 1767-1774
    • Binda, C.1
  • 75
    • 12144287240 scopus 로고    scopus 로고
    • Inactivation of purified human recombinant monoamine oxidases A and B by rasagiline and its analogues
    • Hubálek, F., et al. Inactivation of purified human recombinant monoamine oxidases A and B by rasagiline and its analogues. J. Med. Chem. 47 (2004), 1760–1766.
    • (2004) J. Med. Chem. , vol.47 , pp. 1760-1766
    • Hubálek, F.1
  • 76
    • 84961644830 scopus 로고    scopus 로고
    • LSD1 inhibitors: a patent review (2010–2015)
    • Stazi, G., et al. LSD1 inhibitors: a patent review (2010–2015). Expert. Opin. Ther. Pat. 26 (2016), 565–580.
    • (2016) Expert. Opin. Ther. Pat. , vol.26 , pp. 565-580
    • Stazi, G.1
  • 77
    • 84975687645 scopus 로고    scopus 로고
    • Irreversible LSD1 inhibitors: application of tranylcypromine and its derivatives in cancer treatment
    • Zheng, Y.C., et al. Irreversible LSD1 inhibitors: application of tranylcypromine and its derivatives in cancer treatment. Curr. Top. Med. Chem. 16 (2016), 2179–2188.
    • (2016) Curr. Top. Med. Chem. , vol.16 , pp. 2179-2188
    • Zheng, Y.C.1
  • 78
    • 77952355653 scopus 로고    scopus 로고
    • Biochemical, structural, and biological evaluation of tranylcypromine derivatives as inhibitors of histone demethylases LSD1 and LSD2
    • Binda, C., et al. Biochemical, structural, and biological evaluation of tranylcypromine derivatives as inhibitors of histone demethylases LSD1 and LSD2. J. Am. Chem. Soc. 132 (2010), 6827–6833.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6827-6833
    • Binda, C.1
  • 79
    • 84896135274 scopus 로고    scopus 로고
    • Flavin-dependent thymidylate synthase as a drug target for deadly microbes: mutational study and a strategy for inhibitor design
    • Mathews, I.I., Flavin-dependent thymidylate synthase as a drug target for deadly microbes: mutational study and a strategy for inhibitor design. J. Bioterror. Biodef., 12, 2013, 004.
    • (2013) J. Bioterror. Biodef. , vol.12 , pp. 004
    • Mathews, I.I.1
  • 80
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A.E., Cravatt, B.F., Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11 (2004), 535–546.
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 81
    • 84863672926 scopus 로고    scopus 로고
    • Activity-based probes for studying the activity of flavin-dependent oxidases and for the protein target profiling of monoamine oxidase inhibitors
    • Krysiak, J.M., et al. Activity-based probes for studying the activity of flavin-dependent oxidases and for the protein target profiling of monoamine oxidase inhibitors. Angew. Chem. Int. Ed. 51 (2012), 7035–7040.
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 7035-7040
    • Krysiak, J.M.1


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