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Residues in the acetyl CoA binding site of pyruvate carboxylase involved in allosteric regulation
Author(s) -
Choosangtong Kamonman,
Sirithanakorn Chaiyos,
Adina-Zada Abdul,
Wallace John C.,
Jitrapakdee Sarawut,
Attwood Paul V.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.06.034
Subject(s) - allosteric regulation , pyruvate carboxylase , acetyl coa , biochemistry , mutant , activator (genetics) , chemistry , acetyl coa carboxylase , allosteric enzyme , pkm2 , enzyme , enzyme activator , glycolysis , pyruvate kinase , receptor , gene
We have examined the roles of Asp1018, Glu1027, Arg469 and Asp471 in the allosteric domain of Rhizobium etli pyruvate carboxylase. Arg469 and Asp471 interact directly with the allosteric activator acetyl coenzyme A (acetyl CoA) and the R469S and R469K mutants showed increased enzymic activity in the presence and absence of acetyl CoA, whilst the D471A mutant exhibited no acetyl CoA‐activation. E1027A, E1027R and D1018A mutants had increased activity in the absence of acetyl CoA, but not in its presence. These results suggest that most of these residues impose restrictions on the structure and/or dynamics of the enzyme to affect activity.