Aminoalkyl adenylate and aminoacyl sulfamate intermediate analogues differing greatly in affinity for their cognate Staphylococcus aureus aminoacyl tRNA synthetases.
Aminoalkyl adenylates and aminoacyl sulfamates derived from arginine, histidine and threonine, have been prepared and tested as inhibitors of their cognate Staphylococcus aureus aminoacyl tRNA synthetases. The arginyl derivatives were both potent nanomolar inhibitors of the Class I arginyl tRNA synthetase whereas for the Class II histidyl and threonyl tRNA synthetases, the acyl sulfamates were potent inhibitors but the adenylates had very little affinity.
Forrest
A K
AK
SmithKline Beecham Pharmaceuticals, Discovery Research, Harlow, Essex, UK.
Jarvest
R L
RL
Mensah
L M
LM
O'Hanlon
P J
PJ
Pope
A J
AJ
Sheppard
R J
RJ
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D000604:Amino Acyl-tRNA Synthetases / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000378:metabolism; D013211:Staphylococcus aureus / Q000201:enzymology*; D013449:Sulfonamides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology
D004791:Enzyme Inhibitors; D013449:Sulfonamides; D000249:Adenosine Monophosphate; D000604:Amino Acyl-tRNA Synthetases