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Volumn 52, Issue 17, 2013, Pages 2874-2887

Further characterization of Cys-type and Ser-type anaerobic sulfatase maturating enzymes suggests a commonality in the mechanism of catalysis

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM PERFRINGENS; INSOLUBLE PROTEINS; MONOMERIC PROTEINS; OXIDIZABLE AMINO ACIDS; REDUCTIVE CLEAVAGE; S-ADENOSYLMETHIONINE; SITE DIRECTED MUTAGENESIS; TWO-ELECTRON OXIDATION;

EID: 84877062815     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400136u     Document Type: Article
Times cited : (49)

References (59)
  • 1
    • 49649128470 scopus 로고    scopus 로고
    • Anaerobic sulfatase-maturating enzymes: First dual substrate radical S -adenosylmethionine enzymes
    • Benjdia, A., Subramanian, S., Leprince, J., Vaudry, H., Johnson, M. K., and Berteau, O. (2008) Anaerobic sulfatase-maturating enzymes: First dual substrate radical S -adenosylmethionine enzymes J. Biol. Chem. 283, 17815-17826
    • (2008) J. Biol. Chem. , vol.283 , pp. 17815-17826
    • Benjdia, A.1    Subramanian, S.2    Leprince, J.3    Vaudry, H.4    Johnson, M.K.5    Berteau, O.6
  • 2
    • 47349101467 scopus 로고    scopus 로고
    • In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters
    • Grove, T. L., Lee, K. H., St Clair, J., Krebs, C., and Booker, S. J. (2008) In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters Biochemistry 47, 7523-7538
    • (2008) Biochemistry , vol.47 , pp. 7523-7538
    • Grove, T.L.1    Lee, K.H.2    St Clair, J.3    Krebs, C.4    Booker, S.J.5
  • 3
    • 37049024768 scopus 로고    scopus 로고
    • Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin
    • Yokoyama, K., Numakura, M., Kudo, F., Ohmori, D., and Eguchi, T. (2007) Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin J. Am. Chem. Soc. 129, 15147-15155
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15147-15155
    • Yokoyama, K.1    Numakura, M.2    Kudo, F.3    Ohmori, D.4    Eguchi, T.5
  • 4
    • 33947655766 scopus 로고    scopus 로고
    • Anaerobic sulfatase-maturating enzymes: Radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification
    • Benjdia, A., Leprince, J., Guillot, A., Vaudry, H., Rabot, S., and Berteau, O. (2007) Anaerobic sulfatase-maturating enzymes: Radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification J. Am. Chem. Soc. 129, 3462
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3462
    • Benjdia, A.1    Leprince, J.2    Guillot, A.3    Vaudry, H.4    Rabot, S.5    Berteau, O.6
  • 5
    • 77950463535 scopus 로고    scopus 로고
    • Anaerobic sulfatase-maturating enzyme: A mechanistic link with glycyl radical-activating enzymes?
    • Benjdia, A., Subramanian, S., Leprince, J., Vaudry, H., Johnson, M. K., and Berteau, O. (2010) Anaerobic sulfatase-maturating enzyme: A mechanistic link with glycyl radical-activating enzymes? FEBS J. 277, 1906-1920
    • (2010) FEBS J. , vol.277 , pp. 1906-1920
    • Benjdia, A.1    Subramanian, S.2    Leprince, J.3    Vaudry, H.4    Johnson, M.K.5    Berteau, O.6
  • 6
    • 77955076779 scopus 로고    scopus 로고
    • Mechanistic and functional versatility of radical SAM enzymes
    • Booker, S. J. and Grove, T. L. (2010) Mechanistic and functional versatility of radical SAM enzymes F1000 Biol. Rep. 2, 52
    • (2010) F1000 Biol. Rep. , vol.2 , pp. 52
    • Booker, S.J.1    Grove, T.L.2
  • 7
    • 84866011930 scopus 로고    scopus 로고
    • Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes
    • Lanz, N. D. and Booker, S. J. (2012) Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes Biochim. Biophys. Acta 1824, 1196-1212
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1196-1212
    • Lanz, N.D.1    Booker, S.J.2
  • 8
    • 50149113479 scopus 로고    scopus 로고
    • Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy
    • Yokoyama, K., Ohmori, D., Kudo, F., and Eguchi, T. (2008) Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy Biochemistry 47, 8950-8960
    • (2008) Biochemistry , vol.47 , pp. 8950-8960
    • Yokoyama, K.1    Ohmori, D.2    Kudo, F.3    Eguchi, T.4
  • 9
    • 13844275460 scopus 로고    scopus 로고
    • Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "radical-SAM" protein superfamily
    • Walsby, C. J., Ortillo, D., Yang, J., Nnyepi, M. R., Broderick, W. E., Hoffman, B. M., and Broderick, J. B. (2005) Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "radical-SAM" protein superfamily Inorg. Chem. 44, 727-741
    • (2005) Inorg. Chem. , vol.44 , pp. 727-741
    • Walsby, C.J.1    Ortillo, D.2    Yang, J.3    Nnyepi, M.R.4    Broderick, W.E.5    Hoffman, B.M.6    Broderick, J.B.7
  • 10
    • 84866021687 scopus 로고    scopus 로고
    • Structural diversity in the AdoMet radical enzyme superfamily
    • Dowling, D. P., Vey, J. L., Croft, A. K., and Drennan, C. L. (2012) Structural diversity in the AdoMet radical enzyme superfamily Biochim. Biophys. Acta 1824, 1178-1195
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1178-1195
    • Dowling, D.P.1    Vey, J.L.2    Croft, A.K.3    Drennan, C.L.4
  • 11
    • 65249142024 scopus 로고    scopus 로고
    • Anaerobic functionalization of unactivated C-H bonds
    • Booker, S. J. (2009) Anaerobic functionalization of unactivated C-H bonds Curr. Opin. Chem. Biol. 13, 58-73
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 58-73
    • Booker, S.J.1
  • 13
    • 0038575234 scopus 로고    scopus 로고
    • S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin?
    • Frey, P. A. and Magnusson, O. T. (2003) S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin? Chem. Rev. 103, 2129-2148
    • (2003) Chem. Rev. , vol.103 , pp. 2129-2148
    • Frey, P.A.1    Magnusson, O.T.2
  • 14
    • 84856367380 scopus 로고    scopus 로고
    • Radical S -adenosylmethionine enzymes: Mechanism, control and function
    • Challand, M. R., Driesener, R. C., and Roach, P. L. (2011) Radical S -adenosylmethionine enzymes: Mechanism, control and function Nat. Prod. Rep. 28, 1696-1721
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1696-1721
    • Challand, M.R.1    Driesener, R.C.2    Roach, P.L.3
  • 15
    • 84866046539 scopus 로고    scopus 로고
    • Enzyme catalyzed formation of radicals from S -adenosylmethionine and inhibition of enzyme activity by the cleavage products
    • Hiscox, M. J., Driesener, R. C., and Roach, P. L. (2012) Enzyme catalyzed formation of radicals from S -adenosylmethionine and inhibition of enzyme activity by the cleavage products Biochim. Biophys. Acta 1824, 1165-1177
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1165-1177
    • Hiscox, M.J.1    Driesener, R.C.2    Roach, P.L.3
  • 16
    • 33747330135 scopus 로고    scopus 로고
    • A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes
    • Berteau, O., Guillot, A., Benjdia, A., and Rabot, S. (2006) A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes J. Biol. Chem. 281, 22464-22470
    • (2006) J. Biol. Chem. , vol.281 , pp. 22464-22470
    • Berteau, O.1    Guillot, A.2    Benjdia, A.3    Rabot, S.4
  • 17
    • 2442499333 scopus 로고    scopus 로고
    • Post-translational formylglycine modification of bacterial sulfatases by the radical S -adenosylmethionine protein AtsB
    • Fang, Q., Peng, J., and Dierks, T. (2004) Post-translational formylglycine modification of bacterial sulfatases by the radical S -adenosylmethionine protein AtsB J. Biol. Chem. 279, 14570-14578
    • (2004) J. Biol. Chem. , vol.279 , pp. 14570-14578
    • Fang, Q.1    Peng, J.2    Dierks, T.3
  • 18
    • 8844275956 scopus 로고    scopus 로고
    • Sulfatases: Structure, mechanism, biological activity, inhibition, and synthetic utility
    • Hanson, S. R., Best, M. D., and Wong, C.-H. (2004) Sulfatases: Structure, mechanism, biological activity, inhibition, and synthetic utility Angew. Chem., Int. Ed. 43, 5736-5763
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 5736-5763
    • Hanson, S.R.1    Best, M.D.2    Wong, C.-H.3
  • 20
    • 0032145321 scopus 로고    scopus 로고
    • Computational analysis of bacterial sulfatases and their modifying enzymes
    • Schirmer, A. and Kolter, R. (1998) Computational analysis of bacterial sulfatases and their modifying enzymes Chem. Biol. 5, R181-R186
    • (1998) Chem. Biol. , vol.5
    • Schirmer, A.1    Kolter, R.2
  • 21
    • 0032104543 scopus 로고    scopus 로고
    • A novel protein modification generating an aldehyde group in sulfatases: Its role in catalysis and disease
    • von Figura, K., Schmidt, B., Selmer, T., and Dierks, T. (1998) A novel protein modification generating an aldehyde group in sulfatases: Its role in catalysis and disease BioEssays 20, 505-510
    • (1998) BioEssays , vol.20 , pp. 505-510
    • Von Figura, K.1    Schmidt, B.2    Selmer, T.3    Dierks, T.4
  • 22
    • 0034987576 scopus 로고    scopus 로고
    • 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family
    • Boltes, I., Czapinska, H., Kahnert, A., von Bülow, R., Dierks, T., Schmidt, B., von Figura, K., Kertesz, M. A., and Usón, I. (2001) 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family Structure 9, 483-491
    • (2001) Structure , vol.9 , pp. 483-491
    • Boltes, I.1    Czapinska, H.2    Kahnert, A.3    Von Bülow, R.4    Dierks, T.5    Schmidt, B.6    Von Figura, K.7    Kertesz, M.A.8    Usón, I.9
  • 23
    • 0032539976 scopus 로고    scopus 로고
    • Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis
    • Lukatela, G., Krauss, N., Theis, K., Selmer, T., Gieselmann, V., von Figura, K., and Saenger, W. (1998) Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis Biochemistry 37, 3654-3664
    • (1998) Biochemistry , vol.37 , pp. 3654-3664
    • Lukatela, G.1    Krauss, N.2    Theis, K.3    Selmer, T.4    Gieselmann, V.5    Von Figura, K.6    Saenger, W.7
  • 24
    • 0032513051 scopus 로고    scopus 로고
    • Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine
    • Recksiek, M., Selmer, T., Dierks, T., Schmidt, B., and von Figura, K. (1998) Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine J. Biol. Chem. 273, 6096-6103
    • (1998) J. Biol. Chem. , vol.273 , pp. 6096-6103
    • Recksiek, M.1    Selmer, T.2    Dierks, T.3    Schmidt, B.4    Von Figura, K.5
  • 25
    • 0037509873 scopus 로고    scopus 로고
    • The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases
    • Cosma, M. P., Pepe, S., Annunziata, I., Newbold, R. F., Grompe, M., Parenti, G., and Ballabio, A. (2003) The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases Cell 113, 445-456
    • (2003) Cell , vol.113 , pp. 445-456
    • Cosma, M.P.1    Pepe, S.2    Annunziata, I.3    Newbold, R.F.4    Grompe, M.5    Parenti, G.6    Ballabio, A.7
  • 26
    • 19344367884 scopus 로고    scopus 로고
    • Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme
    • Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., von Figura, K., Ficner, R., and Rudolph, M. G. (2005) Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme Cell 121, 541-552
    • (2005) Cell , vol.121 , pp. 541-552
    • Dierks, T.1    Dickmanns, A.2    Preusser-Kunze, A.3    Schmidt, B.4    Mariappan, M.5    Von Figura, K.6    Ficner, R.7    Rudolph, M.G.8
  • 29
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt, B., Selmer, T., Ingendoh, A., and von Figura, K. (1995) A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency Cell 82, 271-278
    • (1995) Cell , vol.82 , pp. 271-278
    • Schmidt, B.1    Selmer, T.2    Ingendoh, A.3    Von Figura, K.4
  • 30
    • 33847107131 scopus 로고    scopus 로고
    • First evidences for a third sulfatase maturation system in prokaryotes from E. coli aslB and ydeM deletion mutants
    • Benjdia, A., Deho, G., Rabot, S., and Berteau, O. (2007) First evidences for a third sulfatase maturation system in prokaryotes from E. coli aslB and ydeM deletion mutants FEBS Lett. 581, 1009-1014
    • (2007) FEBS Lett. , vol.581 , pp. 1009-1014
    • Benjdia, A.1    Deho, G.2    Rabot, S.3    Berteau, O.4
  • 31
    • 77951930923 scopus 로고    scopus 로고
    • A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
    • Grove, T. L., Ahlum, J. H., Sharma, P., Krebs, C., and Booker, S. J. (2010) A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters Biochemistry 49, 3783-3785
    • (2010) Biochemistry , vol.49 , pp. 3783-3785
    • Grove, T.L.1    Ahlum, J.H.2    Sharma, P.3    Krebs, C.4    Booker, S.J.5
  • 32
    • 6344256785 scopus 로고    scopus 로고
    • Insight into the polar reactivity of the onium chalcogen analogues of S -adenosyl- l -methionine
    • Iwig, D. F. and Booker, S. J. (2004) Insight into the polar reactivity of the onium chalcogen analogues of S -adenosyl- l -methionine Biochemistry 43, 13496-13509
    • (2004) Biochemistry , vol.43 , pp. 13496-13509
    • Iwig, D.F.1    Booker, S.J.2
  • 33
  • 34
    • 84866996636 scopus 로고    scopus 로고
    • RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins
    • Lanz, N. D., Grove, T. L., Gogonea, C. B., Lee, K. H., Krebs, C., and Booker, S. J. (2012) RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins Methods Enzymol. 516, 125-152
    • (2012) Methods Enzymol. , vol.516 , pp. 125-152
    • Lanz, N.D.1    Grove, T.L.2    Gogonea, C.B.3    Lee, K.H.4    Krebs, C.5    Booker, S.J.6
  • 35
    • 0018065357 scopus 로고
    • Micro methods for the quantitative determination of iron and copper in biological material
    • Beinert, H. (1978) Micro methods for the quantitative determination of iron and copper in biological material Methods Enzymol. 54, 435-445
    • (1978) Methods Enzymol. , vol.54 , pp. 435-445
    • Beinert, H.1
  • 36
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • Beinert, H. (1983) Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins Anal. Biochem. 131, 373-378
    • (1983) Anal. Biochem. , vol.131 , pp. 373-378
    • Beinert, H.1
  • 37
    • 0021686102 scopus 로고
    • Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase
    • Kennedy, M. C., Kent, T. A., Emptage, M., Merkle, H., Beinert, H., and Münck, E. (1984) Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase J. Biol. Chem. 259, 14463-14471
    • (1984) J. Biol. Chem. , vol.259 , pp. 14463-14471
    • Kennedy, M.C.1    Kent, T.A.2    Emptage, M.3    Merkle, H.4    Beinert, H.5    Münck, E.6
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 39
  • 41
    • 0032574756 scopus 로고    scopus 로고
    • NADPH-flavodoxin redutase and flavodoxin from Escherichia coli: Characteristics as a soluble microsomal P450 reductase
    • Jenkins, C. M. and Waterman, M. R. (1998) NADPH-flavodoxin redutase 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
  • 42
    • 33846041078 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt)
    • The-UniProt-Consortium
    • The-UniProt-Consortium. (2007) The Universal Protein Resource (UniProt) Nucleic Acids Res. 35, D193-D197
    • (2007) Nucleic Acids Res. , vol.35
  • 43
    • 33750445986 scopus 로고    scopus 로고
    • Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii
    • Johnson, D. C., Unciuleac, M. C., and Dean, D. R. (2006) Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii J. Bacteriol. 188, 7551-7561
    • (2006) J. Bacteriol. , vol.188 , pp. 7551-7561
    • Johnson, D.C.1    Unciuleac, M.C.2    Dean, D.R.3
  • 44
    • 0000440349 scopus 로고
    • Synthetic analogues of the active sites of iron-sulfur proteins
    • In (Lovenberg, W. Ed.) Academic Press, New York.
    • Holm, R. H. and Ibers, J. A. (1977) Synthetic analogues of the active sites of iron-sulfur proteins. In Iron-Sulfur Proteins (Lovenberg, W., Ed.) Academic Press, New York.
    • (1977) Iron-Sulfur Proteins
    • Holm, R.H.1    Ibers, J.A.2
  • 46
    • 0034694686 scopus 로고    scopus 로고
    • Conversion of 3Fe-4S to 4Fe-4S clusters in native pyruvate formate-lyase activating enzyme: Mössbauer characterization and implications for mechanism
    • Krebs, C., Henshaw, T. F., Cheek, J., Huynh, B. H., and Broderick, J. B. (2000) Conversion of 3Fe-4S to 4Fe-4S clusters in native pyruvate formate-lyase activating enzyme: Mössbauer characterization and implications for mechanism J. Am. Chem. Soc. 122, 12497-12506
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12497-12506
    • Krebs, C.1    Henshaw, T.F.2    Cheek, J.3    Huynh, B.H.4    Broderick, J.B.5
  • 47
    • 34447618279 scopus 로고    scopus 로고
    • Human sulfatases: A structural perspective to catalysis
    • Ghosh, D. (2007) Human sulfatases: A structural perspective to catalysis Cell. Mol. Life Sci. 64, 2013-2022
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2013-2022
    • Ghosh, D.1
  • 48
    • 0033561117 scopus 로고    scopus 로고
    • Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases
    • Dierks, T., Lecca, M. R., Schlotterhose, P., Schmidt, B., and von Figura, K. (1999) Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases EMBO J. 18, 2084-2091
    • (1999) EMBO J. , vol.18 , pp. 2084-2091
    • Dierks, T.1    Lecca, M.R.2    Schlotterhose, P.3    Schmidt, B.4    Von Figura, K.5
  • 49
    • 0034719099 scopus 로고    scopus 로고
    • Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase
    • Cosper, N. J., Booker, S. J., Ruzicka, F., Frey, P. A., and Scott, R. A. (2000) Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase Biochemistry 39, 15668-15673
    • (2000) Biochemistry , vol.39 , pp. 15668-15673
    • Cosper, N.J.1    Booker, S.J.2    Ruzicka, F.3    Frey, P.A.4    Scott, R.A.5
  • 51
    • 14844301641 scopus 로고    scopus 로고
    • Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase
    • Shokes, J. E., Duin, E. C., Bauer, C., Jaun, B. H. R., Koch, J., and Scott, R. A. (2005) Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase FEBS Lett. 579, 1741-1744
    • (2005) FEBS Lett. , vol.579 , pp. 1741-1744
    • Shokes, J.E.1    Duin, E.C.2    Bauer, C.3    Jaun, B.H.R.4    Koch, J.5    Scott, R.A.6
  • 52
    • 77749285730 scopus 로고    scopus 로고
    • Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII
    • Ruszczycky, M. W., Choi, S. H., and Liu, H. W. (2010) Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII J. Am. Chem. Soc. 132, 2359-2369
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2359-2369
    • Ruszczycky, M.W.1    Choi, S.H.2    Liu, H.W.3
  • 54
    • 0017886452 scopus 로고
    • - from equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase
    • - from equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase Eur. J. Biochem. 85, 535-547
    • (1978) Eur. J. Biochem. , vol.85 , pp. 535-547
    • Mayhew, S.G.1
  • 55
    • 79952075857 scopus 로고    scopus 로고
    • Radical SAM activation of the B12-independent glycerol dehydratase results in formation of 5′-deoxy-5′-(methylthio)adenosine and not 5′-deoxyadenosine
    • Demick, J. M. and Lanzilotta, W. N. (2011) Radical SAM activation of the B12-independent glycerol dehydratase results in formation of 5′-deoxy-5′-(methylthio)adenosine and not 5′-deoxyadenosine Biochemistry 50, 440-442
    • (2011) Biochemistry , vol.50 , pp. 440-442
    • Demick, J.M.1    Lanzilotta, W.N.2
  • 56
    • 33747127816 scopus 로고    scopus 로고
    • 4-Hydroxyphenylacetate decarboxylases: Properties of a novel subclass of glycyl radical enzymes systems
    • Yu, L., Blaser, M., Andrei, P. I., Pierik, A. J., and Selmer, T. (2006) 4-Hydroxyphenylacetate decarboxylases: Properties of a novel subclass of glycyl radical enzymes systems Biochemistry 45, 9584-9592
    • (2006) Biochemistry , vol.45 , pp. 9584-9592
    • Yu, L.1    Blaser, M.2    Andrei, P.I.3    Pierik, A.J.4    Selmer, T.5
  • 58
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.