酵素反応速度
酵素反応速度論
(enzyme kinetics から転送)
出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2023/09/03 21:26 UTC 版)
酵素反応速度論 (こうそはんのうそくどろん) とは酵素によって触媒される化学反応を反応速度の面から研究する学問。酵素の反応速度論を研究することで、酵素反応の機構、代謝における役割、活性調節の仕組み、薬物や毒が酵素をどう阻害するかといったことを明らかにできる。
- ^ Hsieh M, Brenowitz M (August 1997). “Comparison of the DNA association kinetics of the Lac repressor tetramer, its dimeric mutant LacIadi, and the native dimeric Gal repressor”. J. Biol. Chem. 272 (35): 22092–6. doi:10.1074/jbc.272.35.22092. PMID 9268351.
- ^ Ebbing, D.D. General chemistry (4th edition) Houghton Mifflin Co. 1993, ISBN 0-395-63696-5
- ^ Eisenthal R. Danson M.J. (Eds), Enzyme Assays: A Practical Approach. Oxford University Press (2002) ISBN 0-19-963820-9
- ^ Xie XS, Lu HP. Single-molecule enzymology. J Biol Chem. 1999 Jun 4;274(23):15967-70. PMID 10347141
- ^ Lu H (2004). “Single-molecule spectroscopy studies of conformational change dynamics in enzymatic reactions”. Current pharmaceutical biotechnology 5 (3): 261–9. doi:10.2174/1389201043376887. PMID 15180547.
- ^ Schnell J, Dyson H, Wright P (2004). “Structure, dynamics, and catalytic function of dihydrofolate reductase”. Annual review of biophysics and biomolecular structure 33: 119–40. doi:10.1146/annurev.biophys.33.110502.133613. PMID 15139807.
- ^ Gibson Q.H. Rapid mixing: Stopped flow Methods in Enzymology, (1969) 16:187–228
- ^ Duggleby, R.G. Analysis of enzyme progress curves by non-linear regression. Methods in Enzymology, (1995) 249:61–90.
- ^ Michaelis L. and Menten M.L. Kinetik der Invertinwirkung Biochem. Z. 1913; 49:333–369 English translation Accessed 6 April 2007
- ^ Cha S (1968). “A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state”. J. Biol. Chem. 243 (4): 820–5. PMID 5638598.
- ^ Briggs GE, Haldane JB. A Note on the Kinetics of Enzyme Action. Biochem J. 1925;19(2):338-9. PMID 16743508
- ^ Stroppolo ME, Falconi M, Caccuri AM, Desideri A (2001). “Superefficient enzymes”. Cell. Mol. Life Sci. 58 (10): 1451–60. doi:10.1007/PL00000788. PMID 11693526.
- ^ Davis ME, Madura JD, Sines J, Luty BA, Allison SA, McCammon JA (1991). “Diffusion-controlled enzymatic reactions”. Meth. Enzymol. 202: 473–97. PMID 1784185.
- ^ Jones ME (1992). “Analysis of algebraic weighted least-squares estimators for enzyme parameters”. Biochem. J. 288 ( Pt 2): 533–8. PMID 1463456.
- ^ a b Tseng SJ, Hsu JP. A comparison of the parameter estimating procedures for the Michaelis–Menten model. J Theor Biol. 1990 Aug 23;145(4):457–64. PMID 2246896
- ^ Bravo, I.G., Busto, F., De Arriaga, D., Ferrero, M. A., Rodríguez-Aparicio, L. B., Martínez-Blanco H., Reglero, A. A normalised plot as a novel and time-saving tool in complex enzyme kinetic analysis Biochem. J. (2001). 358, 573–583. PMID 11577687
- ^ Almaas E, Kovacs B, Vicsek T, Oltvai ZN, Barabasi AL. Global organization of metabolic fluxes in the bacterium Escherichia coli. Nature. 2004 Feb 26;427(6977):839-43. PMID 14985762
- ^ Reed JL, Vo TD, Schilling CH, Palsson BO. An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR). Genome Biol. 2003;4(9):R54. PMID 12952533
- ^ Dirr H, Reinemer P, Huber R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. Eur J Biochem. 1994 Mar 15;220(3):645-61. PMID 8143720
- ^ Stone SR, Morrison JF. Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates. Biochemistry. 1988 Jul 26;27(15):5493–9. PMID 3052577
- ^ Fisher PA. Enzymologic mechanism of replicative DNA polymerases in higher eukaryotes. Prog Nucleic Acid Res Mol Biol. 1994;47:371-97. PMID 8016325
- ^ Akerman SE, Muller S. 2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum. Mol Biochem Parasitol. 2003 Aug 31;130(2):75-81. PMID 12946843
- ^ Bravo, I.G., Barrallo, S., Ferrero, M. A., Rodríguez-Aparicio, L. B., Martínez-Blanco H., Reglero, A. “Kinetic properties of the Acylneuraminate Cytidylytransferase from Pasteurella haemolytica A2”. Biochem. J. (2001) 358, 585-598. [1]
- ^ Kraut J. Serine proteases: structure and mechanism of catalysis. Annu Rev Biochem. 1977;46:331-58. PMID 332063
- ^ Ricard J, Cornish-Bowden A. Co-operative and allosteric enzymes: 20 years on. Eur J Biochem. 1987 Jul 15;166(2):255-72. PMID 3301336
- ^ Ward WH, Fersht AR., Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activity. Biochemistry. 1988 Jul 26;27(15):5525–30. PMID 3179266
- ^ Helmstaedt K, Krappmann S, Braus GH., Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. Microbiol. Mol. Biol. Rev. 2001 Sep;65(3):404-21 PMID 11528003
- ^ Schirmer T, Evans PR., Structural basis of the allosteric behaviour of phosphofructokinase. Nature. 1990 Jan 11;343(6254):140-5. PMID 2136935
- ^ Hill, A. V. The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves. J. Physiol. (Lond.), 1910 40, iv-vii.
- ^ Bender ML, Begue-Canton ML, Blakeley RL, Brubacher LJ, Feder J, Gunter CR, Kezdy FJ, Killheffer JV Jr, Marshall TH, Miller CG, Roeske RW, Stoops JK. The Determination of the Concentration of Hydrolytic Enzyme Solutions : a-Chymotrypsin, Trypsin, Papain, Elastase, Subtilisin, and Acetylcholinesterase. J Am Chem Soc. 1966 Dec 20;88(24):5890-913. PMID 5980876
- ^ Cleland WW. The use of isotope effects to determine enzyme mechanisms. Arch Biochem Biophys. 2005 Jan 1;433(1):2–12. PMID 15581561
- ^ Northrop D (1981). “The expression of isotope effects on enzyme-catalyzed reactions”. Annu. Rev. Biochem. 50: 103–31. doi:10.1146/annurev.bi.50.070181.000535. PMID 7023356.
- ^ Baillie T, Rettenmeier A (1986). “Drug biotransformation: mechanistic studies with stable isotopes”. Journal of clinical pharmacology 26 (6): 448–51. PMID 3734135.
- ^ Cleland WW. Use of isotope effects to elucidate enzyme mechanisms. CRC Crit Rev Biochem. 1982;13(4):385–428. PMID 6759038
- ^ Christianson DW, Cox JD. Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes. Annu Rev Biochem. 1999;68:33–57. PMID 10872443
- ^ Kraut D, Carroll K, Herschlag D (2003). “Challenges in enzyme mechanism and energetics”. Annu. Rev. Biochem. 72: 517–71. doi:10.1146/annurev.biochem.72.121801.161617. PMID 12704087.
- ^ Leatherbarrow RJ. Using linear and non-linear regression to fit biochemical data. Trends Biochem Sci. 1990 Dec;15(12):455–8. PMID 2077683
- ^ Koshland DE, Application of a Theory of Enzyme Specificity to Protein Synthesis. Proc. Natl. Acad. Sci. U.S.A. 1958 Feb;44(2):98–104. PMID 16590179
- ^ Hammes G (2002). “Multiple conformational changes in enzyme catalysis”. Biochemistry 41 (26): 8221–8. doi:10.1021/bi0260839. PMID 12081470.
- ^ Sutcliffe M, Scrutton N (2002). “A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes”. Eur. J. Biochem. 269 (13): 3096–102. doi:10.1046/j.1432-1033.2002.03020.x. PMID 12084049.
[続きの解説]
「酵素反応速度論」の続きの解説一覧
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