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Volumn 591, Issue 16, 2017, Pages 2394-2405

The radical-SAM enzyme Viperin catalyzes reductive addition of a 5′-deoxyadenosyl radical to UDP-glucose in vitro

Author keywords

immune system; radical SAM; Viperin

Indexed keywords

5' DEOXYADENOSYL RADICAL; ENZYME; HYDROGEN; RADICAL; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE; VIPERIN; DEOXYADENOSINE DERIVATIVE; FREE RADICAL; FUNGAL PROTEIN;

EID: 85028395690     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1002/1873-3468.12769     Document Type: Article
Times cited : (26)

References (47)
  • 1
    • 84974736098 scopus 로고    scopus 로고
    • Radical S-adenosylmethionine enzymes in human health and disease
    • Landgraf BJ, McCarthy EL and Booker SJ (2016) Radical S-adenosylmethionine enzymes in human health and disease. Annu Rev Biochem 85, 485–514.
    • (2016) Annu Rev Biochem , vol.85 , pp. 485-514
    • Landgraf, B.J.1    McCarthy, E.L.2    Booker, S.J.3
  • 3
    • 36048929198 scopus 로고    scopus 로고
    • Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme
    • Wang SC and Frey PA (2007) Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme. Biochemistry 46, 12889–12895.
    • (2007) Biochemistry , vol.46 , pp. 12889-12895
    • Wang, S.C.1    Frey, P.A.2
  • 4
    • 84948775336 scopus 로고    scopus 로고
    • Radical-mediated ring contraction in the biosynthesis of 7-deazapurines
    • Bandarian V and Drennan CL (2015) Radical-mediated ring contraction in the biosynthesis of 7-deazapurines. Curr Opin Struct Biol 35, 116–124.
    • (2015) Curr Opin Struct Biol , vol.35 , pp. 116-124
    • Bandarian, V.1    Drennan, C.L.2
  • 5
    • 4444346402 scopus 로고    scopus 로고
    • Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
    • Hänzelmann P and Schindelin H (2004) Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proc Natl Acad Sci USA 101, 12870–12875.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12870-12875
    • Hänzelmann, P.1    Schindelin, H.2
  • 6
  • 7
    • 33847635732 scopus 로고    scopus 로고
    • S-adenosylmethionine as an oxidant: the radical SAM superfamily
    • Wang SC and Frey PA (2007) S-adenosylmethionine as an oxidant: the radical SAM superfamily. Trends Biochem Sci 32, 101–110.
    • (2007) Trends Biochem Sci , vol.32 , pp. 101-110
    • Wang, S.C.1    Frey, P.A.2
  • 9
    • 2342631335 scopus 로고    scopus 로고
    • S-adenosylmethionine: nothing goes to waste
    • Fontecave M, Atta M and Mulliez E (2004) S-adenosylmethionine: nothing goes to waste. Trends Biochem Sci 29, 243–249.
    • (2004) Trends Biochem Sci , vol.29 , pp. 243-249
    • Fontecave, M.1    Atta, M.2    Mulliez, E.3
  • 10
    • 85006850795 scopus 로고    scopus 로고
    • Tryptophan lyase (NosL): a cornucopia of 5′-deoxyadenosyl radical mediated transformations
    • Bhandari DM, Fedoseyenko D and Begley TP (2016) Tryptophan lyase (NosL): a cornucopia of 5′-deoxyadenosyl radical mediated transformations. J Am Chem Soc 138, 16184–16187.
    • (2016) J Am Chem Soc , vol.138 , pp. 16184-16187
    • Bhandari, D.M.1    Fedoseyenko, D.2    Begley, T.P.3
  • 11
    • 84886908672 scopus 로고    scopus 로고
    • Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme
    • Mahanta N, Fedoseyenko D, Dairi T and Begley TP (2013) Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme. J Am Chem Soc 135, 15318–15321.
    • (2013) J Am Chem Soc , vol.135 , pp. 15318-15321
    • Mahanta, N.1    Fedoseyenko, D.2    Dairi, T.3    Begley, T.P.4
  • 12
    • 84992065313 scopus 로고    scopus 로고
    • Expanding radical SAM chemistry by using radical addition reactions and SAM analogues
    • Ji X, Li Y, Xie L, Lu H, Ding W and Zhang Q (2016) Expanding radical SAM chemistry by using radical addition reactions and SAM analogues. Angew Chem Int Edit 55, 11845–11848.
    • (2016) Angew Chem Int Edit , vol.55 , pp. 11845-11848
    • Ji, X.1    Li, Y.2    Xie, L.3    Lu, H.4    Ding, W.5    Zhang, Q.6
  • 13
    • 0033766517 scopus 로고    scopus 로고
    • Vesicular stomatitis virus and pseudorabies virus induce a vig1/cig5 homologue in mouse dendritic cells via different pathways
    • Boudinot P, Riffault S, Salhi S, Carrat C, Sedlik C, Mahmoudi N, Charley B and Benmansour A (2000) Vesicular stomatitis virus and pseudorabies virus induce a vig1/cig5 homologue in mouse dendritic cells via different pathways. J Gen Virol 81, 2675–2682.
    • (2000) J Gen Virol , vol.81 , pp. 2675-2682
    • Boudinot, P.1    Riffault, S.2    Salhi, S.3    Carrat, C.4    Sedlik, C.5    Mahmoudi, N.6    Charley, B.7    Benmansour, A.8
  • 14
    • 0035910046 scopus 로고    scopus 로고
    • Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus
    • Chin K-C and Cresswell P (2001) Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proc Natl Acad Sci USA 98, 15125–15130.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15125-15130
    • Chin, K.-C.1    Cresswell, P.2
  • 15
    • 84872300249 scopus 로고    scopus 로고
    • Positive selection drives rapid evolution of certain amino acid residues in an evolutionarily highly conserved interferon-inducible antiviral protein of fishes
    • Padhi A (2013) Positive selection drives rapid evolution of certain amino acid residues in an evolutionarily highly conserved interferon-inducible antiviral protein of fishes. Immunogenetics 65, 75–81.
    • (2013) Immunogenetics , vol.65 , pp. 75-81
    • Padhi, A.1
  • 16
    • 73949157872 scopus 로고    scopus 로고
    • Structural characterization reveals that viperin is a radical S-adenosyl-l-methionine (SAM) enzyme
    • Shaveta G, Shi J, Chow VTK and Song J (2010) Structural characterization reveals that viperin is a radical S-adenosyl-l-methionine (SAM) enzyme. Biochem Biophys Res Commun 391, 1390–1395.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 1390-1395
    • Shaveta, G.1    Shi, J.2    Chow, V.T.K.3    Song, J.4
  • 17
    • 77950368112 scopus 로고    scopus 로고
    • The antiviral protein viperin is a radical SAM enzyme
    • Duschene KS and Broderick JB (2010) The antiviral protein viperin is a radical SAM enzyme. FEBS Lett 584, 1263–1267.
    • (2010) FEBS Lett , vol.584 , pp. 1263-1267
    • Duschene, K.S.1    Broderick, J.B.2
  • 18
    • 83655192651 scopus 로고    scopus 로고
    • Viperin: a multifunctional, interferon-inducible protein that regulates virus replication
    • Seo J-Y, Yaneva R and Cresswell P (2011) Viperin: a multifunctional, interferon-inducible protein that regulates virus replication. Cell Host Microbe 10, 534–539.
    • (2011) Cell Host Microbe , vol.10 , pp. 534-539
    • Seo, J.-Y.1    Yaneva, R.2    Cresswell, P.3
  • 19
    • 84859428525 scopus 로고    scopus 로고
    • Viperin, a key player in the antiviral response
    • Mattijssen S and Pruijn GJ (2012) Viperin, a key player in the antiviral response. Microbes Infect 14, 419–426.
    • (2012) Microbes Infect , vol.14 , pp. 419-426
    • Mattijssen, S.1    Pruijn, G.J.2
  • 23
    • 34547656276 scopus 로고    scopus 로고
    • The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts
    • Wang X, Hinson ER and Cresswell P (2007) The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts. Cell Host Microbe 2, 96–105.
    • (2007) Cell Host Microbe , vol.2 , pp. 96-105
    • Wang, X.1    Hinson, E.R.2    Cresswell, P.3
  • 26
    • 33749129426 scopus 로고    scopus 로고
    • TLR3 ligation activates an antiviral response in human fetal astrocytes: a role for viperin/cig5
    • Rivieccio MA, Suh HS, Zhao Y, Zhao ML, Chin KC, Lee SC and Brosnan CF (2006) TLR3 ligation activates an antiviral response in human fetal astrocytes: a role for viperin/cig5. J Immunol 177, 4735–4741.
    • (2006) J Immunol , vol.177 , pp. 4735-4741
    • Rivieccio, M.A.1    Suh, H.S.2    Zhao, Y.3    Zhao, M.L.4    Chin, K.C.5    Lee, S.C.6    Brosnan, C.F.7
  • 28
    • 84905494783 scopus 로고    scopus 로고
    • Fish viperin exerts a conserved antiviral function through RLR-triggered IFN signaling pathway
    • Wang B, Zhang Y-B, Liu T-K, Shi J, Sun F and Gui J-F (2014) Fish viperin exerts a conserved antiviral function through RLR-triggered IFN signaling pathway. Dev Comp Immunol 47, 140–149.
    • (2014) Dev Comp Immunol , vol.47 , pp. 140-149
    • Wang, B.1    Zhang, Y.-B.2    Liu, T.-K.3    Shi, J.4    Sun, F.5    Gui, J.-F.6
  • 31
    • 84867672506 scopus 로고    scopus 로고
    • The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement
    • Honarmand Ebrahimi K, Bill E, Hagedoorn P-L and Hagen WR (2012) The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement. Nat Chem Biol 8, 941–948.
    • (2012) Nat Chem Biol , vol.8 , pp. 941-948
    • Honarmand Ebrahimi, K.1    Bill, E.2    Hagedoorn, P.-L.3    Hagen, W.R.4
  • 33
    • 63249085868 scopus 로고    scopus 로고
    • The N-terminal amphipathic α-helix of viperin mediates localization to the cytosolic face of the endoplasmic reticulum and inhibits protein secretion
    • Hinson ER and Cresswell P (2009) The N-terminal amphipathic α-helix of viperin mediates localization to the cytosolic face of the endoplasmic reticulum and inhibits protein secretion. J Biol Chem 284, 4705–4712.
    • (2009) J Biol Chem , vol.284 , pp. 4705-4712
    • Hinson, E.R.1    Cresswell, P.2
  • 35
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL and Brown MS (1990) Regulation of the mevalonate pathway. Nature 343, 425.
    • (1990) Nature , vol.343 , pp. 425
    • Goldstein, J.L.1    Brown, M.S.2
  • 36
    • 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 SR, Stoll S, Iavarone AT, Imsand EM, Tran H, Britt RD and Klinman JP (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
  • 39
    • 0028280411 scopus 로고
    • Biotin synthase: purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product
    • Sanyal I, Cohen G and Flint DH (1994) Biotin synthase: purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product. Biochemistry 33, 3625–3631.
    • (1994) Biochemistry , vol.33 , pp. 3625-3631
    • Sanyal, I.1    Cohen, G.2    Flint, D.H.3
  • 40
    • 0034623162 scopus 로고    scopus 로고
    • Regulation of glycogen synthase identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation
    • Pederson BA, Cheng C, Wilson WA and Roach PJ (2000) Regulation of glycogen synthase identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation. J Biol Chem 275, 27753–27761.
    • (2000) J Biol Chem , vol.275 , pp. 27753-27761
    • Pederson, B.A.1    Cheng, C.2    Wilson, W.A.3    Roach, P.J.4
  • 41
    • 69249186404 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of UDP-glucose pyrophosphorylase from sphingomonas chungbukensis DJ77
    • Yoon M-Y, Lee K-J, Park H-C, Park S-H, Kim S-G, Kim S-K and Choi J-D (2009) Cloning, expression, and characterization of UDP-glucose pyrophosphorylase from sphingomonas chungbukensis DJ77. Bull Korean Chem Soc 30, 1360–1364.
    • (2009) Bull Korean Chem Soc , vol.30 , pp. 1360-1364
    • Yoon, M.-Y.1    Lee, K.-J.2    Park, H.-C.3    Park, S.-H.4    Kim, S.-G.5    Kim, S.-K.6    Choi, J.-D.7
  • 42
    • 17644405273 scopus 로고    scopus 로고
    • Characterisation and expression of the pathway from UDP-glucose to UDP-xylose in differentiating tobacco tissue
    • Bindschedler LV, Wheatley E, Gay E, Cole J, Cottage A and Bolwell GP (2005) Characterisation and expression of the pathway from UDP-glucose to UDP-xylose in differentiating tobacco tissue. Plant Mol Biol 57, 285–301.
    • (2005) Plant Mol Biol , vol.57 , pp. 285-301
    • Bindschedler, L.V.1    Wheatley, E.2    Gay, E.3    Cole, J.4    Cottage, A.5    Bolwell, G.P.6
  • 43
    • 84928476077 scopus 로고    scopus 로고
    • New ways to boost molecular dynamics simulations
    • Krieger E and Vriend G (2015) New ways to boost molecular dynamics simulations. J Comput Chem 36, 996–1007.
    • (2015) J Comput Chem , vol.36 , pp. 996-1007
    • Krieger, E.1    Vriend, G.2
  • 45
    • 0000852087 scopus 로고
    • S-adenosyl-L-methionine and S-adenosyl-L-homocysteine, an NMR study
    • Stolowitz ML and Minch MJ (1981) S-adenosyl-L-methionine and S-adenosyl-L-homocysteine, an NMR study. J Am Chem Soc 103, 6015–6019.
    • (1981) J Am Chem Soc , vol.103 , pp. 6015-6019
    • Stolowitz, M.L.1    Minch, M.J.2
  • 46
    • 84977079425 scopus 로고    scopus 로고
    • The vaccinia virus H3 envelope protein, a major target of neutralizing antibodies, exhibits a glycosyltransferase fold and binds UDP-glucose
    • Singh K, Gittis AG, Gitti RK, Ostazeski SA, Su H-P and Garboczi DN (2016) The vaccinia virus H3 envelope protein, a major target of neutralizing antibodies, exhibits a glycosyltransferase fold and binds UDP-glucose. J Virol 90, 5020–5030.
    • (2016) J Virol , vol.90 , pp. 5020-5030
    • Singh, K.1    Gittis, A.G.2    Gitti, R.K.3    Ostazeski, S.A.4    Su, H.-P.5    Garboczi, D.N.6
  • 47
    • 84883424197 scopus 로고    scopus 로고
    • Viperin regulates cellular lipid metabolism during human cytomegalovirus infection
    • Seo J-Y and Cresswell P (2013) Viperin regulates cellular lipid metabolism during human cytomegalovirus infection. PLoS Pathog 9, e1003497.
    • (2013) PLoS Pathog , vol.9
    • Seo, J.-Y.1    Cresswell, P.2


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