Table 4

Steady-state kinetic constants for hydrolysis of penicillins by wild-type L1 and L1 mutants.


pencilin G
ampicillin
Enzyme
Km (μM)
kcat (s-1)
kcat/Km × 107
Km (μM)
kcat (s-1)
kcat/Km × 107

w.t.
38 ± 12
600 ± 100
1.6
55 ± 5
520 ± 10
0.95
S224A
70 ± 20
580 ± 100
0.83
125 ± 13
339 ± 1
0.27
S224K
44 ± 8
124 ± 12
0.28
25 ± 3
152 ± 2
0.61
S224D
1600 ± 200
42 ± 9
0.0026
1100 ± 240
10 ± 1
0.00091
I164A
60 ± 5
698 ± 100
1.2
43 ± 3
524 ± 100
1.2
F158A
50 ± 5
138 ± 10
0.28
165 ± 20
270 ± 30
0.16
Y228A
410 ± 60
609 ± 64
0.15
710 ± 74
443 ± 10
0.062
Y228F
140 ± 14
630 ± 30
0.45
271 ± 40
243 ± 30
0.090
N233L
33 ± 9
184 ± 35
0.56
90 ± 20
508 ± 40
0.56
N233D
60 ± 2
440 ± 86
0.73
117 ± 18
621 ± 31
0.53

Carenbauer et al. BMC Biochemistry 2002 3:4   doi:10.1186/1471-2091-3-4