Title : Molecular Interactions between an Enzyme and Its Inhibitor for Selective Detection of Limonene.

Pub. Date : 2022 May 31

PMID : 35543317






6 Functional Relationships(s)
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1 In these simulations, limonene was found to be captured at specific binding sites of AChE by modifying the binding site of acetylcholine (ACh), which induced inhibition of the catalytic activity of AChE toward ACh hydrolysis. Acetylcholine acetylcholinesterase (Cartwright blood group) Homo sapiens
2 In these simulations, limonene was found to be captured at specific binding sites of AChE by modifying the binding site of acetylcholine (ACh), which induced inhibition of the catalytic activity of AChE toward ACh hydrolysis. Acetylcholine acetylcholinesterase (Cartwright blood group) Homo sapiens
3 In these simulations, limonene was found to be captured at specific binding sites of AChE by modifying the binding site of acetylcholine (ACh), which induced inhibition of the catalytic activity of AChE toward ACh hydrolysis. Acetylcholine acetylcholinesterase (Cartwright blood group) Homo sapiens
4 In these simulations, limonene was found to be captured at specific binding sites of AChE by modifying the binding site of acetylcholine (ACh), which induced inhibition of the catalytic activity of AChE toward ACh hydrolysis. Acetylcholine acetylcholinesterase (Cartwright blood group) Homo sapiens
5 In these simulations, limonene was found to be captured at specific binding sites of AChE by modifying the binding site of acetylcholine (ACh), which induced inhibition of the catalytic activity of AChE toward ACh hydrolysis. Acetylcholine acetylcholinesterase (Cartwright blood group) Homo sapiens
6 In these simulations, limonene was found to be captured at specific binding sites of AChE by modifying the binding site of acetylcholine (ACh), which induced inhibition of the catalytic activity of AChE toward ACh hydrolysis. Acetylcholine acetylcholinesterase (Cartwright blood group) Homo sapiens