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. Author manuscript; available in PMC: 2008 Aug 15.
Published in final edited form as: Anal Biochem. 2007 Apr 20;367(2):247–258. doi: 10.1016/j.ab.2007.04.021

Table 1.

Inhibition of RecA activities by nucleotide analogs as measured in microplate assays.

Filament Assembly
Nucleotide Entry % Inhibition (at 100 μM) Kdapp (μM)
1 89 ± 5 60 ± 30
2 82 ± 2 44 ± 6
3 75 ± 7 50 ± 30
4 65 ± 2 100 ± 40
5 55 ± 4 340 ± 190
6 32 ± 3 ≥ 500

ATPase Activity
Nucleotide Entry % Inhibition (at 100 μM) Kic (μM)

6 98 ± 2 0.8 ± 0.1
2 34 ± 4 63 ± 7
1 11 ± 1 140 ± 50
3 7 ± 2 160 ± 20
5 6 ± 3 ≥ 500
4 2 ± 2 ≥ 500

Apparent dissociation constants (Kdapp) were assessed by measuring the extent of filament assembly in the FP assay over an inhibitor concentration range of 0 to 1000 μM (see Materials & Methods and Fig. 3D). ATP-competitive inhibition constants (Kic) were assessed by measuring the apparent S0.5 for ATP in the ATPase assay over an inhibitor concentration range of 0 - 1000 μM (see Materials & Methods and Fig. 5B). The identity of each nucleotide analog represented in the table is indicated by a specific numeral in the “Nucleotide Entry” column: (1) TTP (CAS# 18423-43-3); (2) N6-(1-naphthyl)ADP (see reference [15]); (3) 5-Me-UTP (CAS# 1463-10-11); (4) O6-Me-GTP (CAS# 99404-63-4); (5) 2′-O-Me-ATP (CAS# 2140-79-6); and (6) 2′-(or 3′)-O-(N-methylanthraniloyl)ATP (MANT-ATP, CAS# 85287-56-5).