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Composite Aromatic Boxes for Enzymatic Transformations of Quaternary Ammonium Substrates
Author(s) -
Nagy Gergely N.,
Marton Lívia,
Contet Alicia,
Ozohanics Olivér,
Ardelean LauraMihaela,
Révész Ágnes,
Vékey Károly,
Irimie Florin Dan,
Vial Henri,
Cerdan Rachel,
Vértessy Beáta G.
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201408246
Subject(s) - chemistry , enzyme , binding site , stereochemistry , biochemistry , ammonium , ligand (biochemistry) , plasmodium falciparum , choline , combinatorial chemistry , receptor , organic chemistry , biology , malaria , immunology
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.