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Angew Chem Int Ed Engl. 2014 Dec 1;53(49):13471-6. doi: 10.1002/anie.201408246. Epub 2014 Oct 5.

Composite aromatic boxes for enzymatic transformations of quaternary ammonium substrates.

Author information

1
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). nagy.gergely@ttk.mta.hu.

Abstract

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.

KEYWORDS:

cation-π interactions; enzyme catalysis; molecular recognition; quaternary ammonium; structural biology

PMID:
25283789
DOI:
10.1002/anie.201408246
[Indexed for MEDLINE]

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