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Literature summary extracted from

  • Adachi, M.S.; Juarez, P.R.; Fitzpatrick, P.F.
    Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects (2010), Biochemistry, 49, 386-392.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.16 additional information
-
 additional information 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 Homo sapiens
1.5.3.16 0.19
-
 spermine pH 8.3, 25°C Homo sapiens
1.5.3.16 0.49 2 N1-acetylspermine pH 8.3, 25°C Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.16 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.16 N1-acetylspermine + O2 + H2O
-
 Homo sapiens spermidine + 3-acetamidopropanal + H2O2
-
 ?
1.5.3.16 spermine + O2 + H2O
-
 Homo sapiens spermidine + 3-aminopropanal + H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.3.16 6.6
-
 spermine pH 8.3, 25°C Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.3.16 0.8
-
 N1-acetylspermine pH 8.3, 25°C Homo sapiens
1.5.3.16 37
-
 spermine pH 8.3, 25°C Homo sapiens