Inhibition of ATPase activity of the recA protein by ATP ribose-modified analogs.

Abstract:

:The single-stranded, DNA-dependent ATPase activity of purified recA protein was found to be inhibited competitively by ribose-modified analogs of ATP, 3'-O-anthraniloyl-ATP (Ant-ATP), and 3'-O-(N-methylanthraniloyl)-ATP (Mant-ATP). The Ki values for Ant-ATP and Mant-ATP were around 7 and 3 microM at pH 7.5, respectively. The inhibitions by these analogs were much stronger than that by ADP, which is also a competitive inhibitor for the ATPase activity of the recA protein. The Ki value for ADP is 76 microM. Ant-ATP and Mant-ATP reduced the Hill coefficient for ATP hydrolysis and thus contributed to the cooperative effect of ATP.

journal_name

Arch Biochem Biophys

authors

Karasaki Y,Higashi K

doi

10.1016/0003-9861(84)90508-3

subject

Has Abstract

pub_date

1984-09-01 00:00:00

pages

796-9

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(84)90508-3

journal_volume

233

pub_type

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