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Volumn 53, Issue 16, 2008, Pages 2454-2461

Biosynthesis of selenosubtilisin: A novel way to target selenium into the active site of subtilisin

Author keywords

Cysteine auxotrophic expression system; Glutathione peroxidase; Selenium; Selenocysteine; Selenosubtilisin

Indexed keywords


EID: 49749087910     PISSN: 10016538     EISSN: 18619541     Source Type: Journal    
DOI: 10.1007/s11434-008-0349-7     Document Type: Article
Times cited : (9)

References (26)
  • 1
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. I. Gluthathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidase breakdown
    • Mills G C. Hemoglobin catabolism. I. Gluthathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidase breakdown. J Biol Chem, 1957, 229: 189-197
    • (1957) J Biol Chem , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 2
    • 0026590163 scopus 로고
    • Alpha-(phenylselenenyl) acetophenone derivatives with glutathione peroxidase-like activity. a comparison with ebselen
    • Cotgreave I A, Moldeus P, Brattsand R, et al. Alpha-(phenylselenenyl) acetophenone derivatives with glutathione peroxidase-like activity. A comparison with ebselen. Biochem Pharmacol, 1992, 43: 793-802
    • (1992) Biochem Pharmacol , vol.43 , pp. 793-802
    • Cotgreave, I.A.1    Moldeus, P.2    Brattsand, R.3
  • 5
    • 0021660653 scopus 로고
    • Selenium-Glutathione peroxidase: Properties and synthesis
    • Tappel A L. Selenium-Glutathione peroxidase: Properties and synthesis. Curr Top Cell Regul, 1984, 24: 87-97
    • (1984) Curr Top Cell Regul , vol.24 , pp. 87-97
    • Tappel, A.L.1
  • 6
    • 0035989963 scopus 로고    scopus 로고
    • A semisynthetic glutathione peroxidase with high catalytic efficiency: Selenoglutathione transferase
    • Ren X J, Jemth P, Board P G, et al. A semisynthetic glutathione peroxidase with high catalytic efficiency: Selenoglutathione transferase. Chem Biol, 2002, 9: 789-794
    • (2002) Chem Biol , vol.9 , pp. 789-794
    • Ren, X.J.1    Jemth, P.2    Board, P.G.3
  • 7
    • 0024992830 scopus 로고
    • Selenosubtilisin as a glutathione peroxidase mimic
    • Wu Z P, Hilvert D. Selenosubtilisin as a glutathione peroxidase mimic. J Am Chem Soc, 1990, 112: 5647-5648
    • (1990) J Am Chem Soc , vol.112 , pp. 5647-5648
    • Wu, Z.P.1    Hilvert, D.2
  • 8
    • 0028335568 scopus 로고
    • Generation of selenium-containing abzyme by using chemical mutation
    • Luo G M, Zhu Z Q, Ding L, et al. Generation of selenium-containing abzyme by using chemical mutation. Biochem Biophys Res Commun, 1994, 198: 1240-1247
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 1240-1247
    • Luo, G.M.1    Zhu, Z.Q.2    Ding, L.3
  • 9
    • 0031842248 scopus 로고    scopus 로고
    • Conversion of trypsin into a selenium-containing enzyme by using chemical mutation
    • Liu J, Jiang M S, Luo G M, et al. Conversion of trypsin into a selenium-containing enzyme by using chemical mutation. Biochem Lett, 1998, 20: 693-696
    • (1998) Biochem Lett , vol.20 , pp. 693-696
    • Liu, J.1    Jiang, M.S.2    Luo, G.M.3
  • 10
    • 0037007179 scopus 로고    scopus 로고
    • A novel cyclodextrin-Derived tellurium compound with glutathione peroxidase activity
    • Ren X J, Xue Y, Liu J Q, et al. A novel cyclodextrin-Derived tellurium compound with glutathione peroxidase activity. Chem Bio Chem, 2002, 3: 356-363
    • (2002) Chem Bio Chem , vol.3 , pp. 356-363
    • Ren, X.J.1    Xue, Y.2    Liu, J.Q.3
  • 12
    • 0034727069 scopus 로고    scopus 로고
    • The twenty-first aminoacid
    • Atkins J F, Gesteland R F. The twenty-first aminoacid. Nature, 2000, 407: 463-465
    • (2000) Nature , vol.407 , pp. 463-465
    • Atkins, J.F.1    Gesteland, R.F.2
  • 13
    • 27144469008 scopus 로고    scopus 로고
    • Selenocysteine in proteins-properties and biotechnological use
    • Johanssona L, Gafvelinb G, Arnér E S. Selenocysteine in proteins-properties and biotechnological use. Biochim Biophys Acta, 2005, 1726: 1-13
    • (2005) Biochim Biophys Acta , vol.1726 , pp. 1-13
    • Johanssona, L.1    Gafvelinb, G.2    Arnér, E.S.3
  • 14
    • 0034666169 scopus 로고    scopus 로고
    • Substituting selenocysteine for catalytic cysteine 41 enhances enzymatic activity of plant phospholipid hydroperoxide glutathione peroxidase expressed in Escherichia coli
    • Hazebrouck S, Camoin L, Faltin Z, et al. Substituting selenocysteine for catalytic cysteine 41 enhances enzymatic activity of plant phospholipid hydroperoxide glutathione peroxidase expressed in Escherichia coli. J Biol Chem, 2000, 275: 28715-28721
    • (2000) J Biol Chem , vol.275 , pp. 28715-28721
    • Hazebrouck, S.1    Camoin, L.2    Faltin, Z.3
  • 15
    • 0034921026 scopus 로고    scopus 로고
    • Identification of selenocysteine insertion sequence (SECIS) element in eukaryotic selenoproteins by RNA draw program
    • Xu H B, Huang K X, Qu X H, et al. Identification of selenocysteine insertion sequence (SECIS) element in eukaryotic selenoproteins by RNA draw program. Chin Sci Bull, 2001, 46: 1159-1161
    • (2001) Chin Sci Bull , vol.46 , pp. 1159-1161
    • Xu, H.B.1    Huang, K.X.2    Qu, X.H.3
  • 17
    • 0031760530 scopus 로고    scopus 로고
    • Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity
    • Boschi-Muller S, Muller S, Dorsselaer A V, et al. Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity. FEBS Lett, 1998, 439: 241-245
    • (1998) FEBS Lett , vol.439 , pp. 241-245
    • Boschi-Muller, S.1    Muller, S.2    Dorsselaer, A.V.3
  • 18
    • 15744394832 scopus 로고    scopus 로고
    • Engineering glutathione transferase to a novel glutathione peroxidase mimic with high catalytic efficiency. Incorporation of selenocysteine into a glutathione-binding scaffold using an auxotrophic expression system
    • Yu H J, Liu J Q, Böck A, et al. Engineering glutathione transferase to a novel glutathione peroxidase mimic with high catalytic efficiency. Incorporation of selenocysteine into a glutathione-binding scaffold using an auxotrophic expression system. J Biol Chem, 2005, 280: 11930-11935
    • (2005) J Biol Chem , vol.280 , pp. 11930-11935
    • Yu, H.J.1    Liu, J.Q.2    Böck, A.3
  • 19
    • 0034662681 scopus 로고    scopus 로고
    • Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis
    • Sawano A, Miyawaki A. Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis. Nucl Acids Res, 2000, 28: E78
    • (2000) Nucl Acids Res , vol.28 , pp. 78
    • Sawano, A.1    Miyawaki, A.2
  • 20
    • 0028067179 scopus 로고
    • Autoprocessing of prothiolsubtilisin e in which active-site serine 221 is altered to cysteine
    • Li Y, Inouye M. Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine. J Biol Chem, 1994, 269: 4169-4174
    • (1994) J Biol Chem , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 21
    • 23944485446 scopus 로고    scopus 로고
    • Semisynthetic tellurosubtilisin with glutathione peroxidase activity
    • Mao S Z, Dong Z Y, Liu J Q, et al. Semisynthetic tellurosubtilisin with glutathione peroxidase activity. J Am Chem Soc, 2005, 127: 11588-11589
    • (2005) J Am Chem Soc , vol.127 , pp. 11588-11589
    • Mao, S.Z.1    Dong, Z.Y.2    Liu, J.Q.3
  • 22
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Propeptide release modulates activation precision of pro-subtilisin
    • Yabuta Y, Takagi H, Inouye M, et al. Folding pathway mediated by an intramolecular chaperone: Propeptide release modulates activation precision of pro-subtilisin. J Biol Chem, 2001, 276: 44427-44434
    • (2001) J Biol Chem , vol.276 , pp. 44427-44434
    • Yabuta, Y.1    Takagi, H.2    Inouye, M.3
  • 23
    • 0029026787 scopus 로고
    • Nonessential active site residues modulate Selenosubtilisin's kinetic mechanism
    • Peterson E B, Hilvert D. Nonessential active site residues modulate Selenosubtilisin's kinetic mechanism. Biochemistry, 1995, 34: 6616-6620
    • (1995) Biochemistry , vol.34 , pp. 6616-6620
    • Peterson, E.B.1    Hilvert, D.2
  • 25
    • 0034541151 scopus 로고    scopus 로고
    • The excluding effects of sucrose on a protein chemical degradation pathway: Methionine oxidation in subtilisin
    • DePaz R A, Barnett C C, Dale D A, et al. The excluding effects of sucrose on a protein chemical degradation pathway: Methionine oxidation in subtilisin. Arch Biochem Biophys, 2000, 384: 123-132
    • (2000) Arch Biochem Biophys , vol.384 , pp. 123-132
    • Depaz, R.A.1    Barnett, C.C.2    Dale, D.A.3
  • 26
    • 0021830125 scopus 로고
    • Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation
    • Estell D A, Graycar T P, Wells J A. Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. J Biol Chem, 1985, 260: 6518-6521
    • (1985) J Biol Chem , vol.260 , pp. 6518-6521
    • Estell, D.A.1    Graycar, T.P.2    Wells, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.