[Kinetics of inhibition by 8-oxy-ATP of the dinucleotide pppApU synthesis catalyzed by Escherichia coli RNA-polymerase on the promoter A1 of phage T7 delta D111 DNA during coupled synthesis of di- and trinucleotides and a limited set of substrates].
A kinetic analysis of inhibition of synthesis of dinucleotide pppApU catalyzed by Escherichia coli RNA-polymerase on A1 promoter of the DNA from T7 delta DIII phage mutant by 8-oxy-ATP under the conditions of the coupled synthesis of pppApU and pppApUpC and in the presence of an incomplete set of substrates, namely ATP, UTP, CTP, has been performed. It was found that 8-oxy-ATP is an unproductive analog of both ATP and CTP. A comparative analysis of the dissociation constants shows that 8-oxy-ATP binds at ATP center 3.3. times and at CTP center 540 times weaker than natural substrates. At the UTP center 8-oxy-ATP does not bind at all.
Kuriavyĭ
V V
VV
Bruskov
V I
VI
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000494:pharmacology; D002384:Catalysis; D004279:DNA, Viral / Q000235:genetics; D012321:DNA-Directed RNA Polymerases / Q000037:antagonists & inhibitors*; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D008954:Models, Biological; D009154:Mutation; D009843:Oligoribonucleotides / Q000096:biosynthesis*; D011401:Promoter Regions, Genetic; D013379:Substrate Specificity; D013604:T-Phages / Q000235:genetics
D004279:DNA, Viral; D009843:Oligoribonucleotides; C045650:adenosine triphosphate uridine monophosphate; C051607:8-hydroxyadenosine 5'-triphosphate; D000255:Adenosine Triphosphate; C052918:adenosine triphosphate-uridine monophosphate cytidine monophosphate; D012321:DNA-Directed RNA Polymerases
Kinetika ingibirovaniia 8-oksi-ATP sinteza dinukleotida pppApU RNK-polimerazoĭ Escherichia coli na promotore A1 DNK faga T7 delta D111 v usloviiakh sopriazhennogo sinteza di- i trinukleotida i ogranichennogo nabora substratov.