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Volumn 405, Issue 3, 2011, Pages 388-392

What is the true enzyme kinetics in the biological system? An investigation of macromolecular crowding effect upon enzyme kinetics of glucose-6-phosphate dehydrogenase

Author keywords

Enzyme kinetics; Glucose 6 phosphate dehydrogenase; Macromolecular crowding; Metabolic network; Modelling; Systems biology

Indexed keywords

BOVINE SERUM ALBUMIN; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; MACROGOL;

EID: 79951575052     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.01.037     Document Type: Article
Times cited : (78)

References (19)
  • 1
    • 0032167971 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for signal transduction and metabolite channelling
    • Rohwer J.M., Postma P.W., Kholodenko B.N., Westerhoff H.V. Implications of macromolecular crowding for signal transduction and metabolite channelling. Proc. Natl. Acad. Sci. USA 1998, 95:10547-10552.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10547-10552
    • Rohwer, J.M.1    Postma, P.W.2    Kholodenko, B.N.3    Westerhoff, H.V.4
  • 2
    • 4544252011 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    • Munishkina L.A., Cooper E.M., Uversky V.N., Fink A.L. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit. 2004, 17:456-464.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 456-464
    • Munishkina, L.A.1    Cooper, E.M.2    Uversky, V.N.3    Fink, A.L.4
  • 3
    • 27744475701 scopus 로고    scopus 로고
    • Anomalous diffusion of proteins due to molecular crowding
    • Banks D.S., Fradin C. Anomalous diffusion of proteins due to molecular crowding. Biophys. J. 2005, 89:2960-2971.
    • (2005) Biophys. J. , vol.89 , pp. 2960-2971
    • Banks, D.S.1    Fradin, C.2
  • 4
    • 33746868886 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry to measureenzyme kinetics and activity in complex solutions
    • Olsen S.N. Applications of isothermal titration calorimetry to measureenzyme kinetics and activity in complex solutions. Thermochim. Acta 2006, 448:12-18.
    • (2006) Thermochim. Acta , vol.448 , pp. 12-18
    • Olsen, S.N.1
  • 5
    • 33846569091 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase
    • Jiang M., Guo Z. Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase. J. Am. Chem. Soc. 2007, 129:730-731.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 730-731
    • Jiang, M.1    Guo, Z.2
  • 7
    • 39049105287 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on glycoprotein processing enzymes
    • Totani K., Ihara Y., Matsuo I., Ito Y. Effects of macromolecular crowding on glycoprotein processing enzymes. J. Am. Chem. Soc. 2008, 130:2101-2107.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2101-2107
    • Totani, K.1    Ihara, Y.2    Matsuo, I.3    Ito, Y.4
  • 8
    • 0019883893 scopus 로고
    • Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase
    • Minton A.P., Wilf J. Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 1981, 20:4821-4826.
    • (1981) Biochemistry , vol.20 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 9
    • 33845218867 scopus 로고    scopus 로고
    • Effect of crowding by dextrans and Ficolls on the rate of alkaline phosphatase-catalyzed hydrolysis: a size-dependent investigation
    • Homchaudhuri L., Sarma N., Swaminathan R. Effect of crowding by dextrans and Ficolls on the rate of alkaline phosphatase-catalyzed hydrolysis: a size-dependent investigation. Biopolymers 2006, 83:477-486.
    • (2006) Biopolymers , vol.83 , pp. 477-486
    • Homchaudhuri, L.1    Sarma, N.2    Swaminathan, R.3
  • 10
    • 76849096284 scopus 로고    scopus 로고
    • Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase
    • Pozdnyakova I., Wittung-Stafshede P. Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase. Biochim. Biophys. Acta 2010, 1804:740-744.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 740-744
    • Pozdnyakova, I.1    Wittung-Stafshede, P.2
  • 12
    • 37649016316 scopus 로고    scopus 로고
    • Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin
    • Stagg L., Zhang S.Q., Cheung M.S., Wittung-Stafshede P. Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin. Proc. Natl. Acad. Sci. USA 2007, 104:18976-18981.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18976-18981
    • Stagg, L.1    Zhang, S.Q.2    Cheung, M.S.3    Wittung-Stafshede, P.4
  • 13
    • 47649097660 scopus 로고    scopus 로고
    • Macromolecular crowding enhances thermal stability of rabbit muscle creatine kinase
    • Zhua J., Hea H., Lib S. Macromolecular crowding enhances thermal stability of rabbit muscle creatine kinase. Tsingh. Sci & Tech. 2008, 13:454-459.
    • (2008) Tsingh. Sci & Tech. , vol.13 , pp. 454-459
    • Zhua, J.1    Hea, H.2    Lib, S.3
  • 14
    • 33746813983 scopus 로고    scopus 로고
    • How can biochemical reactions within cells differ from those in test tubes?
    • Minton A.P. How can biochemical reactions within cells differ from those in test tubes?. J. Cell. Sci. 2006, 119:2863-2869.
    • (2006) J. Cell. Sci. , vol.119 , pp. 2863-2869
    • Minton, A.P.1
  • 15
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences
    • Zhou H.X., Rivas G., Minton A.P. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys. 2008, 37:375-397.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 16
    • 33847350336 scopus 로고    scopus 로고
    • New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability
    • Hasmann F.A., Gurpilhares D.B., Roberto I.C., Converti A., Pessoa A. New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability. Enzymol. Microbiol. Tech. 2007, 40:849-858.
    • (2007) Enzymol. Microbiol. Tech. , vol.40 , pp. 849-858
    • Hasmann, F.A.1    Gurpilhares, D.B.2    Roberto, I.C.3    Converti, A.4    Pessoa, A.5
  • 17
    • 33847404319 scopus 로고    scopus 로고
    • Stabilisation mechanism of glucose-6-phosphate dehydrogenase
    • Zaitseva E.A., Chukhrai E.S., Poltorak O.M. Stabilisation mechanism of glucose-6-phosphate dehydrogenase. Khimiya 2000, 41:127-129.
    • (2000) Khimiya , vol.41 , pp. 127-129
    • Zaitseva, E.A.1    Chukhrai, E.S.2    Poltorak, O.M.3
  • 19
    • 0001925266 scopus 로고
    • Purification and properties of D-glucose-6-phosphate dehydrogenase
    • Glaser L., Brown D.H. Purification and properties of D-glucose-6-phosphate dehydrogenase. J. Biol. Chem. 1955, 216:67-79.
    • (1955) J. Biol. Chem. , vol.216 , pp. 67-79
    • Glaser, L.1    Brown, D.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.