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Volumn 395, Issue 3, 2010, Pages 412-415

Cysteine-125 is the catalytic residue of Saccharomyces cerevisiae free methionine-R-sulfoxide reductase

Author keywords

Catalytic function; Free methionine R sulfoxide reductase (fRMsr); Glutaredoxin; Thioredoxin

Indexed keywords

CYSTEINE; GLUTAREDOXIN; METHIONINE SULFOXIDE REDUCTASE;

EID: 77951878944     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.04.036     Document Type: Article
Times cited : (9)

References (17)
  • 1
    • 35748932403 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals
    • Kim H.Y., and Gladyshev V.N. Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem. J. 407 (2007) 321-329
    • (2007) Biochem. J. , vol.407 , pp. 321-329
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 3
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • Moskovitz J. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim. Biophys. Acta 1703 (2005) 213-219
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 213-219
    • Moskovitz, J.1
  • 4
    • 44549088533 scopus 로고    scopus 로고
    • The methionine sulfoxide reductases: catalysis and substrate specificities
    • Boschi-Muller S., Gand A., and Branlant G. The methionine sulfoxide reductases: catalysis and substrate specificities. Arch. Biochem. Biophys. 474 (2008) 266-273
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 266-273
    • Boschi-Muller, S.1    Gand, A.2    Branlant, G.3
  • 6
    • 0032815727 scopus 로고    scopus 로고
    • Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase
    • Sharov V.S., Ferrington D.A., Squier T.C., and Schoneich C. Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase. FEBS Lett. 455 (1999) 247-250
    • (1999) FEBS Lett. , vol.455 , pp. 247-250
    • Sharov, V.S.1    Ferrington, D.A.2    Squier, T.C.3    Schoneich, C.4
  • 8
    • 1542313980 scopus 로고    scopus 로고
    • Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases
    • Kim H.Y., and Gladyshev V.N. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol. Biol. Cell 15 (2004) 1055-1064
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1055-1064
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 9
    • 57649119783 scopus 로고    scopus 로고
    • Mammals reduce methionine-S-sulfoxide with MsrA and are unable to reduce methionine-R-sulfoxide, and this function can be restored with a yeast reductase
    • Lee B.C., Le D.T., and Gladyshev V.N. Mammals reduce methionine-S-sulfoxide with MsrA and are unable to reduce methionine-R-sulfoxide, and this function can be restored with a yeast reductase. J. Biol. Chem. 283 (2008) 28361-28369
    • (2008) J. Biol. Chem. , vol.283 , pp. 28361-28369
    • Lee, B.C.1    Le, D.T.2    Gladyshev, V.N.3
  • 10
    • 0029935647 scopus 로고    scopus 로고
    • Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins
    • Moskovitz J., Weissbach H., and Brot N. Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc. Natl. Acad. Sci. USA 93 (1996) 2095-2099
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2095-2099
    • Moskovitz, J.1    Weissbach, H.2    Brot, N.3
  • 11
  • 12
    • 1642457208 scopus 로고    scopus 로고
    • Properties and functions of GAF domains in cyclic nucleotide phosphodiesterases and other proteins
    • Zoraghi R., Corbin J.D., and Francis S.H. Properties and functions of GAF domains in cyclic nucleotide phosphodiesterases and other proteins. Mol. Pharmacol. 65 (2004) 267-278
    • (2004) Mol. Pharmacol. , vol.65 , pp. 267-278
    • Zoraghi, R.1    Corbin, J.D.2    Francis, S.H.3
  • 13
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor
    • Ho Y.S., Burden L.M., and Hurley J.H. Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor. EMBO J. 19 (2000) 5288-5299
    • (2000) EMBO J. , vol.19 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 15
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg D., Muller R., and Funk M. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156 (1995) 119-122
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 16
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov V.V. Rapid and reliable protein extraction from yeast. Yeast 16 (2000) 857-860
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 17
    • 43549109795 scopus 로고    scopus 로고
    • Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine
    • Kim H.Y., and Kim J.R. Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine. Biochem. Biophys. Res. Commun. 371 (2008) 490-494
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 490-494
    • Kim, H.Y.1    Kim, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.