    2.3.3.21 | isoleucine |
end product feedback inhibition, competitive inhibition of the binding of pyruvate and acetyl-CoA; inhibits in a concentration-dependent manner. High selectivity of CMS for isoleucine over leucine is primarily dictated by the residues, Tyr430, Leu451, Tyr454, Ile458 and Val468, that form a hydrophobic pocket to accommodate the side chain of the inhibitor. Binding of isoleucine affects the binding of the substrate and coenzyme at the active site, possibly via conformational change of the dimer interface of the regulatory domain, leading to inhibition of the catalytic reaction, in a typical pattern of K-type inhibition |
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| 2.3.3.21 | more |
mutant I458A is not inhibited by isoleucine, leucine does not inhibit the wild-type and the mutants H400A/H408A, Y430L, L451V, I458A, D431A, T464A, P493A, and Q495A |
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