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A simplified approach to derive Cleland model for enzymatic reactions
Ganesan Saraswathi, ,
Published in
2013
PMID: 23455878
Volume: 35
   
Issue: 5
Pages: 785 - 789
Abstract
Metabolic modeling can suggest which is the key enzyme activity that needs to be controlled or its activity enhanced for the required production of a metabolite in a pathway. It also helps to find possible drug targets (enzymes to be inhibited). In metabolic modeling, knowing the kinetics of the enzymes involved in a pathway is mandatory. Most enzymatic reactions involve multi-substrates and follow an ordered sequential or ping-pong mechanism. The kinetic parameters involved in the model are obtained by fitting experimental data using a model based on the mechanism. The Cleland model has been used for some years. The grouping of parameters, such as dissociation constant and Michaelis-Menten constant, makes the strategy meaningful and hence the Cleland model is still in use. Although other alternate methods, e. g., the King-Altman method, are available, derivation by determinants can be used to derive a rate expression for the sequential or ping-pong mechanism, they are tedious. Hence, a meaningful modification is suggested in this communication for deriving the enzyme mechanism which is based on Thilakavathi et al. (Biotech Lett 28:1889-1894, 2006) to obtain the Cleland model in an easier way. © 2013 Springer Science+Business Media Dordrecht.
About the journal
JournalBiotechnology Letters
ISSN01415492
Open AccessNo
Concepts (21)
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    Dissociation constant
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    ENZYMATIC REACTION
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    Enzymology
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    Experimental datum
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    KING-ALTMAN METHODS
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    MICHAELIS-MENTEN CONSTANT
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    PING-PONG MECHANISM
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    RATE EQUATIONS
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    Dissociation
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    Metabolism
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    Enzymes
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    Enzyme
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    Article
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    Biochemistry
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    Biological model
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    Chemical model
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    Chemistry
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    Kinetics
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    BIOCHEMICAL PROCESSES
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    Models, biological
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    Models, chemical