Abstract
The structure activity relationship on a series of ester and hydroxamate analogues of methionyl and isoleucyl adenylate has been investigated through introducing linkers between the 1'-position of ribose and adenine surrogates as methionyl-tRNA, and isoleucyl-tRNA synthetase inhibitors, respectively. The results indicate that ester analogue 23 was found to be a potent inhibitor of Escherichia coli methionyl-tRNA synthetase, and its interaction with the active site was proposed by a molecular modeling study.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenosine / analogs & derivatives
-
Adenosine / chemical synthesis
-
Adenosine / pharmacology*
-
Adenosine Monophosphate / analogs & derivatives*
-
Adenosine Monophosphate / chemical synthesis
-
Adenosine Monophosphate / pharmacology*
-
Binding Sites / physiology
-
Escherichia coli
-
Esters / chemical synthesis
-
Hydroxamic Acids / chemical synthesis
-
Isoleucine / chemical synthesis
-
Isoleucine-tRNA Ligase / antagonists & inhibitors*
-
Methionine / analogs & derivatives*
-
Methionine / chemical synthesis
-
Methionine / pharmacology*
-
Methionine-tRNA Ligase / antagonists & inhibitors*
-
Models, Molecular
-
Structure-Activity Relationship
Substances
-
Esters
-
Hydroxamic Acids
-
Isoleucine
-
methioninyl adenylate
-
Adenosine Monophosphate
-
Methionine
-
Methionine-tRNA Ligase
-
Isoleucine-tRNA Ligase
-
Adenosine