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Volumn 329, Issue 2, 2004, Pages 345-347

Escherichia coli methionine aminopeptidase with Tyr168 to alanine substitution can improve the N-terminal processing of recombinant proteins with valine at the penultimate position

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; RECOMBINANT PROTEINS;

EID: 2542417350     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.03.031     Document Type: Article
Times cited : (2)

References (6)
  • 1
    • 0040911108 scopus 로고    scopus 로고
    • Co-expression of glutathione S-transferase with methionine aminopeptidase: A system of producing enriched N-terminal processed proteins in Escherichia coli
    • Hwang D.D., Liu L.F., Kuan I.C., Lin L.Y., Tam T.C., Tam M.F. Co-expression of glutathione S-transferase with methionine aminopeptidase: a system of producing enriched N-terminal processed proteins in Escherichia coli. Biochem. J. 338:1999;335-342
    • (1999) Biochem. J. , vol.338 , pp. 335-342
    • Hwang, D.D.1    Liu, L.F.2    Kuan, I.C.3    Lin, L.Y.4    Tam, T.C.5    Tam, M.F.6
  • 2
    • 0034615568 scopus 로고    scopus 로고
    • Structure and function of the methionine aminopeptidases
    • Lowther W., Matthews B. Structure and function of the methionine aminopeptidases. Biochim. Biophys. Acta. 1477:2000;157-167
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 157-167
    • Lowther, W.1    Matthews, B.2
  • 3
    • 0027436258 scopus 로고
    • Reversible modification of rat liver glutathione S-transferase 3-3 with 1-chloro-2,4-dinitrobenzene: Specific labelling of Tyr-115
    • Liu L.F., Hong J.L., Tsai S.P., Hsieh J.C., Tam M.F. Reversible modification of rat liver glutathione S-transferase 3-3 with 1-chloro-2, 4-dinitrobenzene: specific labelling of Tyr-115. Biochem. J. 296:1993;189-197
    • (1993) Biochem. J. , vol.296 , pp. 189-197
    • Liu, L.F.1    Hong, J.L.2    Tsai, S.P.3    Hsieh, J.C.4    Tam, M.F.5
  • 4
    • 0033564306 scopus 로고    scopus 로고
    • Escherichia coli methionine aminopeptidase: Implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis
    • Lowther W., Orville A., Madden D., Lim S., Rich D., Matthews B. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry. 38:1999;7678-7688
    • (1999) Biochemistry , vol.38 , pp. 7678-7688
    • Lowther, W.1    Orville, A.2    Madden, D.3    Lim, S.4    Rich, D.5    Matthews, B.6
  • 5
    • 0033532182 scopus 로고    scopus 로고
    • Yeast methionine aminopeptidase I. Alternation of substrate specificity by site-directed mutagenesis
    • Walker K.W., Bradshaw R.A. Yeast methionine aminopeptidase I. Alternation of substrate specificity by site-directed mutagenesis. J. Biol. Chem. 274:1999;13403-13409
    • (1999) J. Biol. Chem. , vol.274 , pp. 13403-13409
    • Walker, K.W.1    Bradshaw, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.