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When used to model enzyme rates in vivo , for example, to model a metabolic pathway, this representation is inadequate because under these conditions product is present. As a result, when building computer models of metabolism [1] or other enzymatic processes, it is better to use the reversible form of the Michaelis–Menten equation.
Molecular biology; Cell biology ... to the lock and key model: since enzymes are rather ... a different enzyme. Several enzymes can work together in a ...
The model is used in a variety of biochemical situations other than enzyme-substrate interaction, including antigen–antibody binding, DNA–DNA hybridization, and protein–protein interaction. [ 17 ] [ 18 ] It can be used to characterize a generic biochemical reaction, in the same way that the Langmuir equation can be used to model generic ...
The induced fit model is a development of the lock-and-key model and assumes that an active site is flexible and changes shape until the substrate is completely bound. This model is similar to a person wearing a glove: the glove changes shape to fit the hand. The enzyme initially has a conformation that attracts its substrate.
The study of enzyme kinetics is important for two basic reasons. Firstly, it helps explain how enzymes work, and secondly, it helps predict how enzymes behave in living organisms. The kinetic constants defined above, K M and V max, are critical to attempts to understand how enzymes work together to control metabolism.
To address such a paradox, Kuo-Chen Chou and his co-workers proposed a model by taking into account the spatial factor and force field factor between the enzyme and its substrate and found that the upper limit could reach 10 10 M −1 s −1, [6] [7] [8] and can be used to explain some surprisingly high reaction rates in molecular biology. [5 ...
Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Most enzymes are proteins, and most such processes are chemical reactions.
Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.