[Gamma-anilides of nucleoside-5'triphosphates as substrates of DNA-dependent RNA-polymerase of Escherichia coli].
Characteristics of NTP gamma-anilidates (AnpppN) as substrates of E. coli RNA-polymerase have been studied. Michaelis constants for AnpppN are about an order of magnitude greater than those for the usual substrates, whereas the maximum rates differ but unsignificantly. AnpppA is almost completely transformed to polyA and Anppi when synthesis of polyA takes place with AnpppA as the only substrate with denatured DNA as template (reiteration system). The AnpppA-residue is present at the 5'-terminus of RNA synthesized from AnpppA, CTP, UTP and GTP on T7 DNA template by the holo-enzyme.
D000813:Anilides; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D009711:Nucleotides; D011061:Poly A; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D000813:Anilides; D009711:Nucleotides; C025882:nucleoside triphosphate-gamma-anilide; D011061:Poly A; D012321:DNA-Directed RNA Polymerases
Gamma-anilicy nukleozid-5'-trifosfatov kak substraty DNK-zavisimoĭ RNK polimerazy Escherichia coli.