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. Author manuscript; available in PMC: 2013 Oct 30.
Published in final edited form as: Biochemistry. 2012 Oct 15;51(43):8690–8697. doi: 10.1021/bi3011434

Table 2.

Steady-State Kinetic Parameters for Wild-type Fmsl and the N195A and D94N Enzymesa

substrate kinetic parameter Fms1d N195A D94N
N1-acetylspermineb kcat (s-1)c 15.1 ± 0.4 8.1 ± 0.2 9.7 ± 0.2
kcat/Kamine (mM-1 s-1)c 1400 ± 200 78 ± 13 320 ± 50
Kamine (μM)c 10.9 ± 1.8 104 ± 14 30 ± 5
kcat/KO2 (mM-1 s-1)e 358 ± 20 405 ± 72 100 ± 14
KO2 (μM)e 43.6 ± 2.3 20 ± 3 97 ± 14
sperminef kcat (s-1)c 39.0 ± 1.5 4.9 ± 0.2 2.0 ± 0.3
kcat/Kamine (mM-1 s-1)c 330 ± 60 38.5 ± 8.3 4.1 ± 1.0
Kamine (μM)c 118 ± 25 127 ± 27 320 ± 88
kcat/KO2 (mM-1 s-1)g 428 ± 77 327 ± 67 104 ± 36
KO2 (μM)g 91 ± 16 15 ± 3 192 ± 60
a

Conditions: 25 °C.

b

Determined at pH 9.0.

c

Determined by varying the concentration of the amine at 1.2 mM oxygen.

d

From ref. (13).

e

Determined by varying the concentration of oxygen at 20 mM N1-acetylspermine.

f

Determined at pH 9.35.

g

Determined by varying the concentration of oxygen at 20 mM spermine.