Skip to main content

Table 1 Apparent dissociation constants (K d ) of MutY mutants.

From: Insights into the role of Val45 and Gln182 of Escherichia coli MutY in DNA substrate binding and specificity

DNA

WT

V45A

Q182L

V45A/Q182L

A/G

1.3 ± 0.11a

6.1 ± 1.7 (0.21)b

8.9 ± 5.0 (0.15)

15 ± 2 (0.09)

A/GO

0.0048 ± 0.0029

0.45 ± 0.06 (0.01)

0.051 ± 0.009 (0.09)

0.59 ± 0.12 (0.01)

T/G

14 ± 1

0.011 ± 0.004 (1273)

0.043 ± 0.014 (326)

8.4 ± 0.7 (1.7)

T/GO

0.036 ± 0.013

0.024 ± 0.009 (1.5)

0.088 ± 0.061 (0.41)

0.013 ± 0.008 (2.77)

  1. a Kd values (nM) are mean ± standard deviation for more than three experiments using nine protein concentrations.
  2. bThe numbers in parenthesis are the folds of binding affinity relative to wild-type (WT) MutY.
Back to article page

BMC Biochemistry

ISSN: 1471-2091

Contact us