Title : Inhibition of single and double-stranded DNA-dependent ATPase of RecA protein by ATP ribose-modified analogs.

Pub. Date : 1987 Jun 1

PMID : 2956659






2 Functional Relationships(s)
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1 The single-stranded (SS) DNA-dependent ATP hydrolysis at pH 7.5 and 6.2 and the double-stranded (DS) DNA-dependent ATP hydrolysis at pH 6.2 by recA protein (no reaction was detectable at pH 7.5) were found to be inhibited competitively by ribose-modified analogs of ATP, 3"-0-anthraniloyl-ATP (Ant-ATP) and 3"-0-(N-methylanthraniloyl)- ATP (Mant-ATP). Ribose RAD51 recombinase Homo sapiens
2 These observations showed that the ATP analogs which have a bulky substituent in the ribose moiety of ATP had strong hydrophobic interactions with the ATP binding site on the recA protein and also contributed to the cooperative effect of ATP. Ribose RAD51 recombinase Homo sapiens