From Wikipedia, the free encyclopedia
Spermine oxidase (
EC
1.5.3.16 , PAOh1/SMO , AtPAO1 , AtPAO4 , SMO ) is an
enzyme with
systematic name spermidine:oxygen oxidoreductase (spermidine-forming) .
[1]
[2]
[3]
[4] This enzyme
catalyses the following
chemical reaction
spermine + O2 + H2 O
⇌
{\displaystyle \rightleftharpoons }
spermidine + 3-aminopropanal + H2 O2
The enzyme from
Arabidopsis thaliana oxidizes
norspermine to
norspermidine .
References
^ Murray-Stewart T, Wang Y, Goodwin A, Hacker A, Meeker A, Casero RA (Jun 2008).
"Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology" . The FEBS Journal . 275 (11): 2795–806.
doi :
10.1111/j.1742-4658.2008.06419.x .
PMC
3631774 .
PMID
18422650 .
^ Cervelli M, Polticelli F, Federico R, Mariottini P (Feb 2003).
"Heterologous expression and characterization of mouse spermine oxidase" . The Journal of Biological Chemistry . 278 (7): 5271–6.
doi :
10.1074/jbc.M207888200 .
PMID
12458219 .
^ Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R (Aug 2006).
"Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion" . Plant Physiology . 141 (4): 1519–32.
doi :
10.1104/pp.106.080911 .
PMC
1533960 .
PMID
16778015 .
^ Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA (May 2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO". Biochemical and Biophysical Research Communications . 304 (4): 605–11.
doi :
10.1016/S0006-291X(03)00636-3 .
PMID
12727196 .
External links
Activity Regulation Classification Kinetics Types