Composite aromatic boxes for enzymatic transformations of quaternary ammonium substrates

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 Plasmod...

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Elmentve itt :
Bibliográfiai részletek
Szerzők: Nagy Gergell N.
Marton Lívia
Contet Alicia
Ozohanics Olivér
Ardelean Laura-Mihaela
Rokobné Révész Ágnes
Vékey Károly
Irimie Florin Dan
Vial Henri
Cerdan Rachel
Vértessy Beáta G.
Dokumentumtípus: Cikk
Megjelent: 2014-12-01
Sorozat:Angewandte Chemie (International ed. in English) 53 No. 49
doi:10.1002/anie.201408246

mtmt:2737826
Online Access:http://publicatio.bibl.u-szeged.hu/7707
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520 3 |a 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. 
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700 0 1 |a Contet Alicia  |e aut 
700 0 1 |a Ozohanics Olivér  |e aut 
700 0 1 |a Ardelean Laura-Mihaela  |e aut 
700 0 2 |a Rokobné Révész Ágnes  |e aut 
700 0 2 |a Vékey Károly  |e aut 
700 0 2 |a Irimie Florin Dan  |e aut 
700 0 2 |a Vial Henri  |e aut 
700 0 2 |a Cerdan Rachel  |e aut 
700 0 2 |a Vértessy Beáta G.  |e aut 
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