Isotherm and Catalysis of Allosteric Enzymes
While most enzymes are single-sited for binding key ligands (or substrate) for which Michaelis-Menten equation is adequate, there exist multiple binding-site enzymes. Multiple binding sites can appear either for simple enzymes or for conformal complex structure of enzyme molecules.
The multi-site behavior of enzymes (or enzyme complexes) leads to the concepts of coorperativity, allostery or allosteric enzymes. Substrate binding isotherm and catalytic rate expressions have been derived for multi-site enzymes without differentiating the different structural confirmations.
The simple kinetic expressions can explain some of the simple allosteric interactions.
Keywords: ALLOSTERIC ENZYME; BINDING ISOTHERM; ENZYME CONFORMAL STRUCTURE COMPLEX; KINETIC; MULTI-SITE ENZYME; REGULATION
Document Type: Research Article
Publication date: 01 December 2014
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