1.5.3.16: spermine oxidase
This is an abbreviated version!
For detailed information about spermine oxidase, go to the full flat file.
Word Map on EC 1.5.3.16
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1.5.3.16
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polyamine
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putrescine
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acetylpolyamine
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back-conversion
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n1-acetylspermine
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n1-acetylpolyamine
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3-aminopropanal
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acrolein
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benspm
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medicine
- 1.5.3.16
- polyamine
- putrescine
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acetylpolyamine
-
back-conversion
- n1-acetylspermine
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n1-acetylpolyamine
- 3-aminopropanal
- acrolein
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benspm
- medicine
Reaction
Synonyms
AtPAO1, AtPAO4, AtPAO5, EC 1.5.3.11, Fms1 protein, GhPAO, hSMO, MmSMO, mSMO, mSMOalpha, mSMOmu, PAO, PAO1, PAO4, PAO5, PAO6, PAO7, PAOh1, PAOh1/SMO, SelPAO5, SMO, SMO(PAOh1), SMO/PAOh1, SMO5, SMOX, spermine oxidase, Spm oxidase, thermospermine oxidase
ECTree
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KM Value
KM Value on EC 1.5.3.16 - spermine oxidase
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1.06
N1-(3-[[(thiophen-2-yl)methyl]amino]propyl)octane-1,8-diamine
pH 7.5, 37°C
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0.034
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without benzyladehyde, kinetic value for the unmethylated end, hSMO
0.067
alpha-methylspermine
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without benzyladehyde, kinetic value for the unmethylated end, hSMO
0.47
N1-acetylspermine
pH 8.0, temperature not specified in the publication
0.9
norspermine
pH 8.0, temperature not specified in the publication
0.02
spermine
mutant enzyme deprived of all but two cysteine residues (C263/C429), pH 8.3, 25°C
0.047
spermine
pH 7.5, temperature not specified in the publication
0.09
spermine
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isozyme SMOalpha, pH 8.0, temperature not specified in the publication
0.09
spermine
isozyme SMOalpha, pH 8.0, temperature not specified in the publication
0.12
spermine
pH 8.0, temperature not specified in the publication
0.19
spermine
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isozyme SMO1, pH 8.0, temperature not specified in the publication
0.22
spermine
pH 8.5, mutant mSMOmuDELTA (with a deletion of the nuclear domain A)
0.02
pH 8.0, temperature not specified in the publication
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics, overview
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additional information
additional information
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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
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