Table S1.
Catalytic constants of the investigated enzyme/substrate combinations. Values
of IMP-1 and
OH-0
are taken from Oelschlaeger
et al.
(2005)
Protein Sci
14, 765-774.
For
OH-2
and
OH-X
, substrate inhibition was observed, and, as in Simm
et al.
(2001)
FEBS Lett
509
,
350-354, the apparent productive binding constant
K
app
was used rather
than
K
M
. The inhibition constants were 155 ± 50
μ
M for
OH-2
/NIT and 70 ± 8
μ
M for
OH-X
/NIT.
Enzyme
Substrate
Kinetic constant
IMP-1
OH-2
OH-X
OH-0
k
cat
(s
-1
)
229 ± 11
205 ± 19
439 ± 24
233 ± 11
K
M/app
(
μ
M
-1
)
9.7 ± 0.8
1.9 ± 0.4
10.8 ± 2.0
10.7 ± 1.8
NIT
k
cat
/
K
M
(s
-1
μ
M
-1
)
23.8 ± 1.0
108 ± 13
41.4 ± 7.2
22.2 ± 2.8
k
cat
(s
-1
)
64.5 ± 5.7
41.5 ± 0.5
41.0 ± 1.7
45.7 ± 1.0
K
M
(
μ
M
-1
)
7.4 ± 1.3
1.2 ± 0.2
2.6 ± 0.4
5.2 ± 0.5
CEF
k
cat
/
K
M
(s
-1
μ
M
-1
)
8.8 ± 0.7
35.0 ± 4.3
15.7 ± 1.5
8.9 ± 0.8
k
cat
(s
-1
)
19.0 ± 4.1
7.8 ± 0.2
18.2 ± 0.2
24.4 ± 2.6
K
M
(
μ
M
-1
)
6.9 ± 3.1
1.3 ± 0.3
3.2 ± 0.3
7.6 ± 1.1
CTX
K
cat
/
K
M
(s
-1
μ
M
-1
)
2.9 ± 0.6
6.0 ± 1.5
5.8 ± 0.4
3.2 ± 0.2
k
cat
(s
-1
)
713 ± 3
920 ± 102
576 ± 37
1060 ± 130
K
M
(
μ
M
-1
)
445 ± 16
255 ± 61
357 ± 40
1230 ± 190
PEN
k
cat
/
K
M
(s
-1
μ
M
-1
)
1.6 ± 0.06
3.7 ± 0.5
1.62 ± 0.08
0.87 ± 0.05
k
cat
(s
-1
)
154 ± 18
74 ± 3
93 ± 6
80 ± 9
K
M
(
μ
M
-1
)
223 ± 44
60.5 ± 0.3
140 ± 16
157 ± 26
AMP
k
cat
/
K
M
(s
-1
μ
M
-1
)
0.70 ± 0.07
1.22 ± 0.44
0.66 ± 0.04
0.52 ± 0.08
k
cat
(s
-1
)
77 ± 4
56 ± 5
35.7 ± 0.6
43.8 ± 2.7
K
M
(
μ
M
-1
)
25 ± 2
12.8 ± 3.0
21.7 ± 1.2
22.7 ± 3.1
IMP
k
cat
/
K
M
(s
-1
μ
M
-1
)
3.1 ± 0.1
4.5 ± 0.7
1.65 ± 0.08
1.95 ± 0.17
k
cat
(s
-1
)
12.2 ± 2.0
8.4 ± 0.5
8.6 ± 1.4
19.7 ± 2.7
K
M
(
μ
M
-1
)
44 ± 13
13.7 ± 1.1
40 ± 11
95 ± 17
CAZ
k
cat
/
K
M
(s
-1
μ
M
-1
)
0.28 ± 0.04
0.62 ± 0.03
0.22 ± 0.02
0.21 ± 0.01