. Author manuscript; available in PMC: 2010 Jun 10.

Published in final edited form as: Biochemistry. 2009 Mar 10;48(9):1850–1861. doi: 10.1021/bi8018898

TABLE 1.

Binding and excision kinetic constants of various lesions by AAG.

	Binding	Glycosylase Activity

Base excised :pairing partner	Δ80AAG	Δ80AAG		Full-length AAG
	K_d±s.d. (nM)	k_obs±s.d. (min⁻¹)^a	Initial excision rate (fmol/min)^b	k_obs±s.d. (min⁻¹)^a	k_obs±s.d. (fmol/min)^c	Initial excision rate (fmol/min)^b
m1G:C	648 ± 154	0.101 ± 0.010	4.46	0.065 ± 0.005		3.68
m1A:T	176 ± 28	N.A.	N.A.	N.A.		N.A.
m3T:A	189 ± 35	N.A.	N.A.	N.A.		N.A.
m3C:G	61 ± 9	N.A.	N.A.	N.A.		N.A.
m3U:G	27 ± 4	N.A.	N.A.	N.A.		N.A.
e3U:G	103 ± 12	N.A.	N.A.	N.A.		N.A.
εA:T	7 ± 1	0.027 ± 0.003	1.98	0.029 ± 0.003		2.12
EA:T	340 ± 129	0.017 ± 0.001	0.47	0.016 ± 0.001		0.51
εC:G	10 ± 1	N.A.	N.A.	N.A.		N.A.
1,N ²-εG:C	928 ± 137	0.079 ± 0.011	0.44	0.074 ± 0.012		0.46
M1G:C	N.B.	N.A.	N.A.	N.A.		N.A.
Hx:T	125 ± 30	0.425 ± 0.070	30.4	0.390 ± 0.061		27.6
U:G	N.B.	N.A.	N.A.		0.062 ± 0.002^c	0.062^c
		k_obs±s.d. (min⁻¹)^a		k_obs±s.d. (min⁻¹)^a
εA (ss)	N.B.	0.030 ± 0.006	1.22	0.043 ± 0.005		1.65
Hx (ss)	N.B.	0.062 ± 0.011	2.01	0.061 ± 0.007		1.90
U (ss)	N.B.	N.A.	N.A.		0.063 ± 0.003^c	0.063^c

Activity rate constants k_obs were determined from one-phase exponential association except for U.

Initial rate is the product of the rate constant k_obs and the maximum saturation cleavage (maximum amount of abasic product formed), except for U where the initial rate is equal to the rate constant obtained from linear regression.

Rate data for U were fitted with linear regression in the form of y=kt.

N.B. or N.A. represents no detectable binding or no activity, < 0.3% or 0.3 fmol, respectively.

Full-length AAG was not observed to bind DNA at all in gel-shift assay.

Δ80 AAG was not observed to bind to single-stranded DNA.