| تعداد نشریات | 24 |
| تعداد شمارهها | 851 |
| تعداد مقالات | 7,575 |
| تعداد مشاهده مقاله | 13,413,758 |
| تعداد دریافت فایل اصل مقاله | 11,580,454 |
The Kinetics of Enzyme Mixtures | ||
| Molecular Biology Research Communications | ||
| مقاله 3، دوره 3، شماره 1، خرداد 2014، صفحه 21-32 اصل مقاله (143.64 K) | ||
| نوع مقاله: Original article | ||
| شناسه دیجیتال (DOI): 10.22099/mbrc.2014.1890 | ||
| نویسندگان | ||
| Simon Brown* 1؛ Noorzaid Muhamad2؛ Kevin C Pedley3؛ David C Simcock4 | ||
| 1Deviot Institute and University of Tasmania | ||
| 2Royal College of Medicine Perak, Universiti Kuala Lumpur | ||
| 3Massey University | ||
| 4James Cook Univesity | ||
| چکیده | ||
| Even purified enzyme preparations are often heterogeneous. For example, preparations of aspartate aminotransferase or cytochrome oxidase can consist of several different forms of the enzyme. For this reason we consider how different the kinetics of the reactions catalysed by a mixture of forms of an enzyme must be to provide some indication of the characteristics of the species present. Based on the standard Michaelis-Menten model, we show that if the Michaelis constants (Km) of two isoforms differ by a factor of at least 20 the steady-state kinetics can be used to characterise the mixture. However, even if heterogeneity is reflected in the kinetic data, the proportions of the different forms of the enzyme cannot be estimated from the kinetic data alone. Consequently, the heterogeneity of enzyme preparations is rarely reflected in measurements of their steady-state kinetics unless the species present have significantly different kinetic properties. This has two implications: (1) it is difficult, but not impossible, to detect molecular heterogeneity using kinetic data and (2) even when it is possible, a considerable quantity of high quality data is required. | ||
| کلیدواژهها | ||
| Aspartate aminotransferase؛ enzyme kinetics؛ heterogeneity؛ isozyme | ||
| مراجع | ||
|
1. Yewdell JW. Not such a dismal science: the economics of protein synthesis, folding, degradation and antigen processing. Trends Cell Biol 2001;11:294-297.
2. Nisselbaum JS, Bodansky O. Kinetics and electrophoretic properties of the isozymes of aspartate aminotransferase from pig heart. J Biol Chem 1966;241:2661-2664.
3. Brown S. Estimating the distribution of forms of cytochrome oxidase from the kinetics of cyanide binding. ICFAI J Biotech 2008;2:51-60.
4. Beinert H, Kennedy MC, Stout CD. Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein. Chem Rev 1996;96:2335-2373.
5. Brzóska K, Meczynska S, Kruszewski M. Iron-sulfur cluster proteins: electron transfer and beyond. Acta Biochim Polon 2006;53:685-691.
6. Hafkenscheid JCM, Dijt CCM. Determination of serum aminotransferases: activation by pyridoxal-5'-phosphate in relation to substrate concentration. Clin Chem 1979;25:55-59.
7. Newman J, Gutteridge S. The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2Å resolution. J Biol Chem 1993;268:25876-25886.
8. Moody AJ, Mitchell JR, Brown S, Rich PR. 1993. The role of CuB in ligand binding by protonmotive terminal oxidases. In International Workshop on Structure-Function of Ion-Translocating Complexes (ed. Drews G), pp. 162-165. Gesellschaft für Biologische Chemie, Freiburg.
9. Vik SB, Georgevich G, Capaldi RA. Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase. Proc Natl Acad Sci USA 1981;7:1456-1460.
10. Menon MP, Hunter FR, Miller S. Kinetic studies on human lactate dehydrogenase isoenzyme-catalyzed lactate-to-pyruvate reaction. J Protein Chem 1987;6:413-429.
11. Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 2001; 43:175-185.
12. Minton AP, Wilf J. Effect of macromolecular crowing upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 1981;20:4821-4826.
13. Farquhar GD. Models describing the kinetics of ribulose bisphosphate carboxylase-oxygenase. Arch Biochem Biophys 1979;193:456-468.
14. Lee W, Shin S, Cho SS, Park J. Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum. J Cell Biochem 1999;76:244-253.
15. Rajas F, Gire V, Rousse B. Involvement of a membrane-bound form of glutamate dehydrogenase in the association of lysosomes to microtubules. J Biol Chem 1996; 271:29882-29890.
16. Preiss T, Sang AE, Chrzanowska-Lightowlers ZMA, Lightowlers RN. The mRNA-binding protein COLBP is glutamate dehydrogenase. FEBS Lett 1995;367:291-296.
17. Fahien LA, MacDonald MJ, Teller JK, Fibich B, Fahien CM. Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the a-ketoglutarate dehydrogenase complex. J Biol Chem 1989;264:12393-12312.
18. Paiva AL, Balcão VM, Malcata FX. Kinetics and mechanisms of reactions catalyzed by immobilized lipases. Enzyme Microb Technol 2000;27:187-204.
19. Michaelis L, Menten ML. Die Kinetik der Invertinwirkung. Biochem Z 1913;49: 333-369.
20. Briggs GE, Haldane JBS. A note on the kinetics of enzyme action. Biochem J 1925; 19:338-339.
21. Keleti T. Two rules of enzyme kinetics for reversible Michaelis-Menten mechanisms. FEBS Lett 1986;208:109-112.
22. Hill CM, Waight RD, Bardsley WG. Does any enzyme follow the Michaelis-Menten equation? Mol Cell Biochem 1977;15:173-178.
23. Bardsley WG, Leff P, Kavanagh J, Waight RD. Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, ß-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase. Biochem J 1980;187:739-765.
24. Alberty RA, Hammes GG. Application of the theory of diffusion-controlled reactions to enzyme kinetics. J Phys Chem 1958;62:154-159.
25. Zhou G-Q, Zhong W-Z. Diffusion-controlled reactions of enzymes. A comparison between Chou's model and Alberty-Hammes-Eigen's model. Eur J Biochem 1982; 128:383-387.
26. Brown S. Developing the enzyme-machine analogy: a non-mathematical approach to teaching Michaelis-Menten kinetics. Orbital 2010;2:92-100.
27. Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R. The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters. Biochemistry 2011;50:4402-4410.
28. Scheer M, Grote A, Chang A, Schomburg I, Munaretto C, Rother M, Söhngen C, Stelzer M, Thiele J, Schomburg D. BRENDA, the enzyme information system in 2011. Nucleic Acids Res 2011;39:D670-D676.
29. Brown S, Simcock DC. Confidence bands for rational rate equations. Int J Emerging Sci 2013;3:15-27.
30. Martinez-Carrion M, Turano C, Chiacone E, Bossa F, Giartosio A, Riva A, Fasella P. Isolation and characterization of multiple forms of glutamate-aspartate aminotransferase from pig heart. J Biol Chem 1967;242:2397-2409.
31. Braunstein AE. Amino group transfer. In The enzymes, vol. 9 (ed. Boyer PD), pp. 379-481.
32. Huynh QK, Sakakibara R, Watanabe T, Wada H. Glutamic oxaloacetic transaminase isozymes from rat liver. Purification and physicochemical characterization. J Biochem 1980;88:231-239.
33. Kuramitsu S, Inoue K, Kondo K, Aki K, Kagamiyama H. Aspartate aminotransferase isozymes from rabbit liver. Purification and properties. J Biochem 1985;97:1337-1345.
34. Titterington DM, Smith AFM, Makov UE, Statistical analysis of finite mixture distributions, John Wiley and Sons Ltd, Chichester. 1985.
35. Haldane JBS, Enzymes, Longmans, Green and Co., London. 1930, p. 43.
36. Errede B, Kamen MD. Comparative kinetic studies of cytochromes c in reactions with mitochondrial cytochrome c oxidase and reductase. Biochemistry 1978;17: 1015-1027.
37. Myers D, Palmer G. The kinetic mechanism(s) of cytochrome oxidase. Techniques for their analysis and criteria for their validation. Ann N Y Acad Sci 1988;550:85-97. | ||
|
آمار تعداد مشاهده مقاله: 5,480 تعداد دریافت فایل اصل مقاله: 2,263 |
||