Premium
Nucleophile Selectivity of Chorismate‐Utilizing Enzymes
Author(s) -
Kerbarh Olivier,
Ciulli Alessio,
Chirgadze Dimitri Y.,
Blundell Tom L.,
Abell Chris
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700019
Subject(s) - nucleophile , chemistry , stereochemistry , residue (chemistry) , enzyme , isomerase , atp synthase , mutant , selectivity , biochemistry , gene , catalysis
A comparison of the active sites from the crystal structures of the product complexes of salicylate synthase (Irp9) and the TrpE subunit of anthranilate synthase shows that they are identical, apart from residue Lys193 in Irp9, which is Gln262 in TrpE. 1 H NMR spectroscopic analysis of the Irp9 K193Q and TrpE Q262K mutants indicates that both residues have a key role in the initial nucleophilic attack at C2 of the common substrate chorismate.