A generic rate law for surface-active enzymes

FEBS Letters

Volumn 587, Issue 17, 2013, Pages 2882-2890

  Kartal, Önder ^a   Ebenhöh, Oliver ^b,c  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF ABERDEEN   (United Kingdom)

^c GFZ GERMAN RESEARCH CENTRE FOR GEOSCIENCES   (Germany)

Author keywords

Adsorption isotherm; Available area function; Enzyme kinetics; Langmuir isotherm; Random sequential adsorption; Surface biochemistry; Systems biology

Indexed keywords

ADSORPTION KINETICS; ARTICLE; BINDING COMPETITION; CATALYSIS; CONTROLLED STUDY; DISSOCIATION; ENZYME ACTIVATION; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; GENERIC RATE LAW; MATHEMATICAL PHENOMENA; MICHAELIS MENTEN KINETICS; PRIORITY JOURNAL; STEADY STATE; SURFACE PROPERTY;

ADSORPTION ISOTHERM; AVAILABLE AREA FUNCTION; ENZYME KINETICS; LANGMUIR ISOTHERM; RANDOM SEQUENTIAL ADSORPTION; SURFACE BIOCHEMISTRY; SYSTEMS BIOLOGY;

ADSORPTION; ALGORITHMS; ANIMALS; BINDING, COMPETITIVE; BIOCATALYSIS; ENZYMES; HUMANS; KINETICS; MEMBRANE PROTEINS; MODELS, CHEMICAL; MULTIENZYME COMPLEXES; PROTEIN BINDING; SURFACE PROPERTIES;

EID: 84883054120     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.07.026     Document Type: Article

References (62)

1. O.B. Berg, and M.K. Jain Interfacial Enzyme Kinetics 2002 John Wiley & Sons
2. L. Michaelis, and M.L. Menten Die Kinetik der Invertinwirkung Biochem. Z. 49 1913 333 369
3. K. Suga, G.V. Dedem, and M. Moo-Young Enzymatic breakdown of water insoluble substrates Biotechnol. Bioeng. 17 1975 185 201
4. R. Verger Interfacial enzyme kinetics of lipolysis Annu. Rev. Biophys. Bioeng. 5 1976 77 117
5. R.A.J. Burns, M.Y. El-Sayed, and M.F. Roberts Kinetic model for surface-active enzymes based on the Langmuir adsorption isotherm: phospholipase C (Bacillus cereus) activity toward dimyristoyl phosphatidylcholine/detergent micelles Proc. Natl. Acad. Sci. USA 79 1982 4902 4906
6. R.F. Brown, and M.T. Holtzapple A comparison of the Michaelis-Menten and HCH-1 models Biotechnol. Bioeng. 36 11 1990 1151 1154
7. Y.-H.P. Zhang, and L.R. Lynd Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems Biotechnol. Bioeng. 88 2004 797 824
8. S. Nayak, W.-S. Yeo, and M. Mrksich Determination of kinetic parameters for interfacial enzymatic reactions on self-assembled monolayers Langmuir 23 10 2007 5578 5583
9. A.D. McLaren, and L. Packer Some aspects of enzyme reactions in heterogeneous systems Adv. Enzymol. Relat. Areas Mol. Biol. 33 1970 245 308
10. R.A. Deems Interfacial enzyme kinetics at the phospholipid/water interface: practical considerations Anal. Biochem. 287 1 2000 1 16
11. O.A. Gutiérrez, M. Chavez, and E. Lissi A theoretical approach to some analytical properties of heterogeneous enzymatic assays Anal. Chem. 76 9 2004 2664 2668
12. A. Cornish-Bowden Fundamentals of Enzyme Kinetics fourth ed. 2012 Wiley Blackwell
13. D.L. Purich Enzyme Kinetics: Catalysis & Control: A Reference of Theory and Best-practice Methods 2010 Elsevier
14. A.G. Marangoni Enzyme Kinetics: A Modern Approach 2003 Wiley
15. J.M. Rohwer, and J.-H.S. Hofmeyr Kinetic and thermodynamic aspects of enzyme control and regulation J. Phys. Chem. B 114 49 2010 16280 16289
16. R. Heinrich, and S. Schuster The Regulation of Cellular Systems 1996 Chapman & Hall
17. W. Liebermeister, and E. Klipp Bringing metabolic networks to life: convenience rate law and thermodynamic constraints Theor. Biol. Med. Model. 3 2006 41
18. L.W. Lee, L. Yin, X.M. Zhu, and P. Ao Generic enzymatic rate equation under living conditions J. Biol. Syst. 15 04 2007 495 514
19. M. Adamczyk, K. van Eunen, B.M. Bakker, and H.V. Westerhoff Chapter thirteen - enzyme kinetics for systems biology: when, why and how M.V. Daniel Jameson, H.V. Westerhoff, Methods in Systems Biology Methods in Enzymology vol. 500 2011 Academic Press 233 257
20. M.G. Poolman, D.A. Fell, and S. Thomas Modelling photosynthesis and its control J. Exp. Bot. 51 Spec No. 2000 319 328
21. A. Nag, M. Lunacek, P.A. Graf, and C.H. Chang Kinetic modeling and exploratory numerical simulation of chloroplastic starch degradation BMC Syst. Biol. 5 2011 94
22. S.C. Zeeman, J. Kossmann, and A.M. Smith Starch: its metabolism, evolution, and biotechnological modification in plants Annu. Rev. Plant Biol. 61 2010 209 234
23. M. Stitt, and S.C. Zeeman Starch turnover: pathways, regulation and role in growth Curr. Opin. Plant Biol. 15 3 2012 282 292
24. G.E. Briggs, and J.B. Haldane A note on the kinetics of enzyme action Biochem. J. 19 2 1925 338 339
25. J.W. Dingee, and A.B. Anton A new perturbation solution to the Michaelis-Menten problem AIChE J. 54 5 2008 1344 1357
26. S. Cha 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 1968 820 825
27. C.H. Giles, D. Smith, and A. Huitson A general treatment and classification of the solute adsorption isotherm. I. Theoretical J. Colloid Interface Sci. 47 3 1974 755 765
28. J. Talbot, G. Tarjus, P.R.V. Tassel, and P. Viot From car parking to protein adsorption: an overview of sequential adsorption processes Colloids Surf., A 165 1-3 2000 287 324
29. G. Limousin, J.-P. Gaudet, L. Charlet, S. Szenknect, V. Barths, and M. Krimissa Sorption isotherms: a review on physical bases, modeling and measurement Appl. Geochem. 22 2 2007 249 275
30. R.A. Alberty Rapid-equilibrium enzyme kinetics J. Chem. Educ. 85 8 2008 1136
31. G.J. Wegner, A.W. Wark, H.J. Lee, E. Codner, T. Saeki, S. Fang, and R.M. Corn Real-time surface plasmon resonance imaging measurements for the multiplexed determination of protein adsorption/desorption kinetics and surface enzymatic reactions on peptide microarrays Anal. Chem. 76 19 2004 5677 5684 pMID: 1545628
32. C. Clé, C. Martin, R.A. Field, P. Kuzmic̀, and S. Bornemann Detection of enzyme-catalyzed polysaccharide synthesis on surfaces Biocatal. Biotransform. 28 1 2010 64 71
33. J. Medve, J. Karlsson, D. Lee, and F. Tjerneld Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: adsorption, sugar production pattern, and synergism of the enzymes Biotechnol. Bioeng. 59 5 1998 621 634
34. H. Tatsumi, and H. Katano Kinetics of the surface hydrolysis of raw starch by glucoamylase J. Agric. Food Chem. 53 2005 8123 8127
35. I. Langmuir The adsorption of gases on plane surfaces of glass, mica and platinum J. Am. Chem. Soc. 40 9 1918 1361 1403
36. J.J. Ramsden Adsorption kinetics of proteins A.T. Hubbard, Encyclopedia of Surface and Colloid Science vol. 1 2002 Marcel Dekker 240 261
37. A. Rusanov Surface thermodynamics revisited Surf. Sci. Rep. 58 5-8 2005 111 239
38. P. Schaaf, and J. Talbot Kinetics of random sequential adsorption Phys. Rev. Lett. 62 1989 175 178
39. M. Manciu, and E. Ruckenstein Estimation of the available surface and the jamming coverage in the random sequential adsorption of a binary mixture of disks Colloids Surf., A 232 1 2004 1 10
40. I. Damager, S.B. Engelsen, A. Blennow, B.L. Møller, and M.S. Motawia First principles insight into the α-glucan structures of starch: their synthesis, conformation, and hydration Chem. Rev. 110 4 2010 2049 2080
41. N.M. Goldenberg, and B.E. Steinberg Surface charge: a key determinant of protein localization and function Cancer Res. 70 4 2010 1277 1280
42. B.E. Feller, J.T. Kellis, L.G. Casco-Pereira, C.R. Robertson, and C.W. Frank Interfacial biocatalysis on charged and immobilized substrates: the roles of enzyme and substrate surface charge Langmuir 27 1 2011 250 263
43. J.W. Evans Random and cooperative sequential adsorption Rev. Mod. Phys. 65 1993 1281 1330
44. A.B. Boraston, D.N. Bolam, H.J. Gilbert, and G.J. Davies Carbohydrate-binding modules: fine-tuning polysaccharide recognition Biochem. J. 382 Pt 3 2004 769 781
45. A.B. Boraston The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven Biochem. J. 385 Pt 2 2005 479 484
46. R. Mikkelsen, K. Suszkiewicz, and A. Blennow A novel type carbohydrate-binding module identified in α-glucan, water dikinases is specific for regulated plastidial starch metabolism Biochemistry 45 14 2006 4674 4682
47. C. Christiansen, M.A. Hachem, M.A. Glaring, A.V. Nielsen, B.W. Sigurskjold, B. Svensson, and A. Blennow A CBM20 low-affinity starch-binding domain from glucan, water dikinase FEBS Lett. 583 7 2009 1159 1163
48. Y.-S. Liu, Y. Zeng, Y. Luo, Q. Xu, M. Himmel, S. Smith, and S.-Y. Ding Does the cellulose-binding module move on the cellulose surface? Cellulose 16 2009 587 597
49. E.L. King, and C. Altman A schematic method of deriving the rate laws for enzyme-catalyzed reactions J. Phys. Chem. 60 10 1956 1375 1378
50. R.A. Deems, B.R. Eaton, and E.A. Dennis Kinetic analysis of phospholipase A2 activity toward mixed micelles and its implications for the study of lipolytic enzymes J. Biol. Chem. 250 23 1975 9013 9020
51. P.A. Lizotte, C.A. Henson, and S.H. Duke Purification and characterization of pea epicotyl β-amylase Plant Physiol. 92 3 1990 615 621
52. E.J.V. Damme, J. Hu, A. Barre, B. Hause, G. Baggerman, P. Rougé, and W.J. Peumans Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β-amylase from Calystegia sepium (hedge bindweed) rhizomes Eur. J. Biochem. 268 23 2001 6263 6273
53. H. Tatsumi, H. Katano, and T. Ikeda Kinetic analysis of glucoamylase-catalyzed hydrolysis of starch granules from various botanical sources Biosci. Biotechnol. Biochem. 71 4 2007 946 950
54. S.E. Levine, J.M. Fox, H.W. Blanch, and D.S. Clark A mechanistic model of the enzymatic hydrolysis of cellulose Biotechnol. Bioeng. 107 2010 37 51
55. V. Leloup, P. Colonna, and S. Ring α-Amylase adsorption on starch crystallites Biotechnol. Bioeng. 38 1991 127 134
56. G. Ertl Reactions at surfaces: from atoms to complexity (nobel lecture) Angew. Chem. Int. Ed. Engl. 47 19 2008 3524 3535
57. H.S. Taylor Chemical reactions at surfaces Chem. Rev. 9 1 1931 1 46
58. B.T. Houseman, J.H. Huh, S.J. Kron, and M. Mrksich Peptide chips for the quantitative evaluation of protein kinase activity Nat. Biotechnol. 20 3 2002 270 274
59. B.T. Houseman, and M. Mrksich Carbohydrate arrays for the evaluation of protein binding and enzymatic modification Chem. Biol. 9 4 2002 443 454
60. G. Brezesinski, and H. Möhwald Langmuir monolayers to study interactions at model membrane surfaces Adv. Colloid Interface Sci. 100 2003 563 584
61. A. Buléon, P. Colonna, V. Planchot, and S. Ball Starch granules: structure and biosynthesis Int. J. Biol. Macromol. 23 2 1998 85 112
62. W. Stein et al., Sage Mathematics Software (Version 5.2), The Sage Development Team, Available from: (2012).