Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, 1111 Budapest (Hungary); Institute of Enzymology, Research Centre of National Sciences, HAS, 1117 Budapest (Hungary).
Angew Chem Int Ed Engl. 2014 Dec 1;53(49):13471-6. doi: 10.1002/anie.201408246. Epub 2014 Oct 5.
Cation-π interactions to cognate ligands in enzymes have key roles in ligand binding and enzymatic catalysis. We have deciphered the key functional role of both charged and aromatic residues within the choline binding subsite of CTP:phosphocholine cytidylyltransferase and choline kinase from Plasmodium falciparum. Comparison of quaternary ammonium binding site structures revealed a general composite aromatic box pattern of enzyme recognition sites, well distinguished from the aromatic box recognition site of receptors.
阳离子-π 相互作用在酶与同源配体的结合中起着关键作用，对酶的催化作用也有重要影响。我们已经揭示了疟原虫 CTP：磷酸胆碱胞苷转移酶和胆碱激酶的胆碱结合亚基中带电和芳香残基的关键功能作用。四级铵结合位点结构的比较揭示了酶识别位点的一般复合芳香盒模式，与受体的芳香盒识别位点明显区分开来。
