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Volumn 131, Issue 33, 2009, Pages 11900-11908

Structural flexibility enhances the reactivity of the bioremediator glycerophosphodiesterase by fine-tuning its mechanism of hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINUCLEAR CENTER; CATALYTIC TURNOVER; CONCENTRATION OF; COORDINATION SPHERE; ENTEROBACTER AEROGENES; FLUORESCENCE MEASUREMENTS; H-BOND NETWORK; HYDROGEN BOND NETWORKS; INDUCED FIT; MAXIMUM VALUES; PARAMAGNETIC PROPERTIES; STOPPED FLOW; STRUCTURAL CHANGE; STRUCTURAL FLEXIBILITIES; STRUCTURAL REARRANGEMENT; SUBSTRATE BINDING; THREE PHASIS;

EID: 69049087726     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja903534f     Document Type: Article
Times cited : (53)

References (45)
  • 4
    • 0001431264 scopus 로고    scopus 로고
    • Wilcox, D. E. Chem. Rev. 1996, 96, 2435-2458.
    • (1996) Chem. Rev , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 29
    • 0002662180 scopus 로고
    • W. H. Freeman: New York; San Francisco, Chapter 4, pp
    • Fersht, A. In Enzyme Structure and Mechanism; W. H. Freeman: New York; San Francisco, 1977; Chapter 4, pp 103-133.
    • (1977) Enzyme Structure and Mechanism , pp. 103-133
    • Fersht, A.1
  • 32
    • 69049083101 scopus 로고    scopus 로고
    • obs(i) (i ) 1, 2, 3) on the concentration of the monoester substrate pNPP is shown in Figure S4. The overall behavior of the three transients are identical to that observed for bpNPP.
    • obs(i) (i ) 1, 2, 3) on the concentration of the monoester substrate pNPP is shown in Figure S4. The overall behavior of the three transients are identical to that observed for bpNPP.
  • 34
    • 69049096758 scopus 로고    scopus 로고
    • 4.
    • 4.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.