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Volumn 76, Issue 7, 2011, Pages 1992-2000

Experimental and kinetic studies of the Escherichia coli glucuronylsynthase: An engineered enzyme for the synthesis of glucuronide conjugates

Author keywords

[No Author keywords available]

Indexed keywords

AGRICULTURAL RESIDUE; AQUEOUS SOLUBILITY; COSOLVENTS; DEHYDROEPIANDROSTERONE; DONOR SUBSTRATES; DRUG TESTING; E. COLI; GLUCURONIDASE; GLUCURONIDES; GLYCOSYNTHASE; IMPROVED METHODS; KINETIC STUDY; OPTIMIZED CONDITIONS; POLAR SUBSTITUENTS; PRODUCT INHIBITION; SINGLE-STEP SYNTHESIS;

EID: 79953188703     PISSN: 00223263     EISSN: 15206904     Source Type: Journal    
DOI: 10.1021/jo101914s     Document Type: Article
Times cited : (17)

References (71)
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    • For reviews on glycosynthases, see
    • For reviews on glycosynthases, see: Rakić, B; Withers, S. G. Aust. J. Chem. 2009, 62, 510-520
    • (2009) Aust. J. Chem. , vol.62 , pp. 510-520
    • Rakić, B.1    Withers, S.G.2
  • 37
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    • Plots of initial rate against substrate concentration are reported in Supporting Information.
    • Plots of initial rate against substrate concentration are reported in Supporting Information.
  • 42
    • 79953197871 scopus 로고    scopus 로고
    • The ORTEP diagram and CIF file for the α- d -glucuronyl fluoride 2 crystal structure (CCDC 793479) is provided in Supporting Information.
    • The ORTEP diagram and CIF file for the α- d -glucuronyl fluoride 2 crystal structure (CCDC 793479) is provided in Supporting Information.
  • 55
    • 0000746575 scopus 로고
    • -1 (50 mM sodium acetate buffer, pH 6.0, 40 °C)
    • -1 (50 mM sodium acetate buffer, pH 6.0, 40 °C) Zhang, Y.; Bommuswamy, J.; Sinnott, M. L. J. Am. Chem. Soc. 1994, 116, 7557-7563
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7557-7563
    • Zhang, Y.1    Bommuswamy, J.2    Sinnott, M.L.3
  • 56
    • 0001439188 scopus 로고
    • -1 (5 mM potassium phosphate buffer, 30 °C);,. The hydrolysis of α- d -glucopyranosyl fluoride is catalyzed by phosphate buffer and is subject to isotope effects
    • -1 (5 mM potassium phosphate buffer, 30 °C) Banait, N. S.; Jencks, W. P. J. Am. Chem. Soc. 1991, 113, 7951-7958. The hydrolysis of α- d -glucopyranosyl fluoride is catalyzed by phosphate buffer and is subject to isotope effects
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7951-7958
    • Banait, N.S.1    Jencks, W.P.2
  • 57
    • 0001407980 scopus 로고
    • We are currently investigating the influence of buffer composition on the hydrolysis of α- d -glucuronyl fluoride 2
    • Banait, N. S.; Jencks, W. P. J. Am. Chem. Soc. 1991, 113, 7958-7963. We are currently investigating the influence of buffer composition on the hydrolysis of α- d -glucuronyl fluoride 2
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7958-7963
    • Banait, N.S.1    Jencks, W.P.2
  • 58
    • 79953171464 scopus 로고    scopus 로고
    • The HPLC reaction yields increased on average 3.1 times from day 4 to day 13 for each temperature regime. The HPLC yield of the reaction held at 37 °C for 13 d was 2.9 times greater than that determined at 4 d. Details are reported in Supporting Information.
    • The HPLC reaction yields increased on average 3.1 times from day 4 to day 13 for each temperature regime. The HPLC yield of the reaction held at 37 °C for 13 d was 2.9 times greater than that determined at 4 d. Details are reported in Supporting Information.
  • 59
    • 79953203148 scopus 로고    scopus 로고
    • A more comprehensive study of wild-type E. coli β-glucuronidase activity and stability in a wide range of cosolvents and detergents is reported in Supporting Information. Similar results are observed for the influence of cosolvent and detergent activity on both the wild-type glucuronidase and the glucuronylsynthase enzymes. For the effects of cosolvents on immobilized E. coli β-glucuronidase activity see ref 20b.
    • A more comprehensive study of wild-type E. coli β-glucuronidase activity and stability in a wide range of cosolvents and detergents is reported in Supporting Information. Similar results are observed for the influence of cosolvent and detergent activity on both the wild-type glucuronidase and the glucuronylsynthase enzymes. For the effects of cosolvents on immobilized E. coli β-glucuronidase activity see ref 20b.
  • 61
    • 79953196817 scopus 로고    scopus 로고
    • Derivatives investigated included: hydrazone, 2-(2-pyridyl)hydrazone, oxime, O -(carboxymethyl)oxime.
    • Derivatives investigated included: hydrazone, 2-(2-pyridyl)hydrazone, oxime, O -(carboxymethyl)oxime.
  • 62
    • 79953209664 scopus 로고    scopus 로고
    • Nonenzymatic hydrolysis of α- d -glucuronyl fluoride was excluded as a significant factor in the incomplete reactions on kinetic grounds. See ref 21.
    • Nonenzymatic hydrolysis of α- d -glucuronyl fluoride was excluded as a significant factor in the incomplete reactions on kinetic grounds. See ref 21.
  • 66
    • 79953174898 scopus 로고    scopus 로고
    • max are reported in Supporting Information.
    • max are reported in Supporting Information.
  • 67
    • 79953184241 scopus 로고    scopus 로고
    • A plot of initial rate against concentration of 2-phenylethyl β- d -glucuronide 12 (0-75 mM) for the glucuronylsynthase reaction of CMO-DHEA 8 and α- d -glucuronyl fluoride 2 is reported in Supporting Information.
    • A plot of initial rate against concentration of 2-phenylethyl β- d -glucuronide 12 (0-75 mM) for the glucuronylsynthase reaction of CMO-DHEA 8 and α- d -glucuronyl fluoride 2 is reported in Supporting Information.
  • 68
    • 79953182639 scopus 로고    scopus 로고
    • The ORTEP diagram and CIF file of the CMO-DHEA 3-β- d -glucuronide 11 crystal structure (CCDC 793480) is provided in Supporting Information.
    • The ORTEP diagram and CIF file of the CMO-DHEA 3-β- d -glucuronide 11 crystal structure (CCDC 793480) is provided in Supporting Information.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.