Directly and Indirectly Determinable Rate Constants in Michaelian Enzyme-Catalyzed Reactions

References (46)

1. 1 The Determination of Enzyme Dissociation Constants [DOI]
2. 2 [17] Amylases, α and β [DOI]
3. 3 Application of a Theory of Enzyme Specificity to Protein Synthesis [DOI]
4. 4 Einfluss der Configuration auf die Wirkung der Enzyme [DOI]
5. 5 The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters [DOI]
6. 6 The Original Michaelis Constant: Translation of the 1913 Michaelis–Menten Paper [DOI]
7. 7 A Note on the Kinetics of Enzyme Action [DOI]
8. 8 Application of microbial α-amylase in industry - A review [DOI]
9. 9 The Quasi-Steady-State Assumption: A Case Study in Perturbation [DOI]
10. 10 Dynamic energy landscape view of coupled binding and protein conformational change: Induced-fit versus population-shift mechanisms [DOI]
11. 11 On the validity of the steady state assumption of enzyme kinetics [DOI]
12. 12 Role of substrate unbinding in Michaelis–Menten enzymatic reactions [DOI]
13. 13 The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding [DOI]
14. 14 A guide to the Michaelis–Menten equation: steady state and beyond [DOI]
15. 15 Validity of the Michaelis–Menten equation – steady‐state or reactant stationary assumption: that is the question [DOI]
16. 16 Selected‐fit versus induced‐fit protein binding: Kinetic differences and mutational analysis [DOI]
17. 17 Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection [DOI]
18. 18 New standards for collecting and fitting steady state kinetic data [DOI]
19. 19 Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data [DOI]
20. 20 THE MODE OF ACTION OF UREASE AND OF ENZYMES IN GENERAL [DOI]
21. 21 The total quasi-steady-state approximation is valid for reversible enzyme kinetics [DOI]
22. 22 Reactant Stationary Approximation in Enzyme Kinetics [DOI]
23. 23 Kinetics of Cellobiohydrolase (Cel7A) Variants with Lowered Substrate Affinity [DOI]
24. 24 A Kinetic Model for the Enzymatic Action of Cellulase [DOI]
25. 25 Diffusion modifies the connectivity of kinetic schemes for multisite binding and catalysis [DOI]
26. 26 Robust Nonlinear Regression in Enzyme Kinetic Parameters Estimation [DOI]
27. 27 Two-Parameter Kinetic Model Based on a Time-Dependent Activity Coefficient Accurately Describes Enzymatic Cellulose Digestion [DOI]
28. 28 The Role of Diffusion in Enzyme Kinetics [DOI]
29. 29 Substrate Induced Population Shifts and Stochastic Gating in the PBCV-1 mRNA Capping Enzyme [DOI]
30. 30 Link between a high k on for drug binding and a fast clinical action: to be or not to be? [DOI]
31. 31 Rate constants are determinable outside the original Michaelis–Menten mathematical formalism wherein the substrate concentration range is 1.6 4.8 times enzyme concentration: A pre-steady-state scenario and beyond [DOI]
32. 32 Derivation of steady-state first-order rate constant equations for enzyme-substrate complex dissociation, as well as zero-order rate constant equations in relation to background assumptions [DOI]
33. 33 Stopped‐flow fluorescence and steady‐state kinetic studies of ligand‐binding reactions of glucoamylase from Aspergillus niger [DOI]
34. 34 The Key to Effective Catalytic Action is Pre-catalytic Site Activity Preceding Enzyme-substrate Complex Formation [DOI]
35. 35 Derivation of Kinetic Parameter Dependent Model for the Quantification of the Concentration and Molar Mass of an Enzyme in Aqueous Solution: A Case Study on Aspergillus oryzea α-amylase [DOI]
36. 36 A method for extracting rate constants from initial rates of stopped-flow kinetic data: application to a physiological electron-transfer reaction [DOI]
37. 37 Modeling the activity burst in the initial phase of cellulose hydrolysis by the processive cellobiohydrolase Cel7A [DOI]
38. 38 Enzyme kinetics: the velocity of reactions [DOI]
39. 39 A Two-part Approach to the Determination of Intrinsic Rate Constants of an Alpha-amylase Catalysed Reaction [DOI]
40. 40 Transient‐phase kinetic studies on the nucleotide binding to 3α‐hydroxysteroid dehydrogenase from Pseudomonas sp. B‐0831 using fluorescence stopped‐flow procedures [DOI]
41. 41 THE MODE OF ACTION OF UREASE AND OF ENZYMES IN GENERAL [DOI]
42. 42 Non-equilibrium Binding Energy Determined Using Alpha-amylase Catalysed Amylolysis of Gelatinised Starch as a Probable Generalisable Model and Importance [DOI]
43. 43 Kinetic parameters from linear plot vis-á-vis condition for validity of various quasi steady state approximations [DOI]
44. 44 The State of Proteins not with Standing, Translational Velocity is Vital for their Function [DOI]
45. 45 Journal of Biological Chemistry [DOI]
46. 46 Asian Journal of Physical and Chemical Sciences [DOI]

Cited by 4

Related research

• Effect of Selected Conditions on Spore Populations Outgrowth Dynamics and Time to Single Spore Outgrowth Distribution in Bacillus subtilis and Bacillus cereus Spores Population — shares topic coverage
• Activation of Local Bentonitic Clays for Use as Viscosifiers in Water-based Drilling Fluids — shares topic coverage
• Treatment of Red Mud with Distilled Water to Improve Its Efficiency to Remove Methylene Blue from Aqueous Solution — shares topic coverage
• Isolation of a Latent Polyphenol Oxidase from Edible Yam (Dioscorea cayenensis-rotundata cv. Zrèzrou) Cultivated in Côte D’ivoire — shares topic coverage
• Chemical Activation of Khojakul Phosphorites by Ammonium Salts — shares topic coverage