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EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
1.5.3.16
-999
-
more
Michaelis-Menten kinetics
725625
1.5.3.16
-999
-
more
Michaelis-Menten kinetics, overview
724499
1.5.3.16
-999
-
more
steady-state kinetic pattern is ping-pong. Reduction of SMO by spermine in the absence of oxygen is biphasic. The rate constant for the rapid phase varies with the substrate concentration, with a limiting value k3 of 49 s-1 and an apparent Kd value of 48 microM at pH 8.3. The rate constant for the slow step is independent of the spermine concentration. The kinetics of the oxidative half-reaction depend on the aging time after the spermine and enzyme are mixed in a double-mixing experiment. The results establish the existence of more than one pathway for the reaction of the reduced flavin intermediate with oxygen. The active form of spermine has three charged nitrogens
711241
1.5.3.16
0.0005
-
spermine
splice variant SMO5
692298
1.5.3.16
0.0006
-
spermine
SMO/PAOh1
692298
1.5.3.16
0.00158
-
N1-acetylspermine
pH 9.0, 20°C
654433
1.5.3.16
0.00163
-
spermine
37°C, pH 8.0
654435
1.5.3.16
0.0046
-
O2
pH 7.5, 25°C, cosubstrate: N1-acetylspermine
742993
1.5.3.16
0.0051
-
O2
pH 7.5, 25°C, cosubstrate: thermospermine
742993
1.5.3.16
0.01
-
N1-[(thiophen-2-yl)methyl]spermine
pH 7.5, 37°C
765150
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