Information on EC 1.5.3.15 - N8-acetylspermidine oxidase (propane-1,3-diamine-forming)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Acanthamoeba culbertsoni

EC NUMBER
COMMENTARY hide
1.5.3.15
-
RECOMMENDED NAME
GeneOntology No.
N8-acetylspermidine oxidase (propane-1,3-diamine-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N8-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)
Also active with N1-acetylspermine, weak activity with N1,N12-diacetylspermine. No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. Absence of monoamine oxidase (EC 1.4.3.4) activity. Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N1,N12-diacetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
show the reaction diagram
-
15% of the activity with N8-acetylspermidine
-
-
?
N1-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
show the reaction diagram
-
40% of the activity with N8-acetylspermidine
-
-
?
N8-acetylspermidine + O2 + H2O
1,3-diaminopropanal + H2O2 + ?
show the reaction diagram
-
the enzyme could be involved in the biosynthesis of diaminopropane which is present inlarge quantities in this amoeba
-
-
?
N8-acetylspermidine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. Absence of monoamine oxidase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N8-acetylspermidine + O2 + H2O
1,3-diaminopropanal + H2O2 + ?
show the reaction diagram
-
the enzyme could be involved in the biosynthesis of diaminopropane which is present inlarge quantities in this amoeba
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
-
1-10 mM, stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM, slight inhibition
8-hydroxyquinoline
-
1 mM, slight inhibition
AgNO3
-
0.1-1 mM
CuSO4
-
0.1-1 mM
diphenyldithiocarbazone
-
0.001 mM, 58% inhibition
EDTA
-
1 mM, slight inhibition
HgCl2
-
0.1-1 mM
hydroxylamine
-
0.1 mM, 69% inhibition
MDL 72527
-
0.001 mM, 61.5% inhibition; 0.01 mM, 99% inhibition
phenylhydrazine
-
0.1 mM, 95% inhibition
ZnSO4
-
0.1-1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
spermidine
-
1 mM, stimulation
spermine
-
1 mM, stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.338
N1-acetylspermine
-
37°C, pH 8
0.105
N8-Acetylspermidine
-
37°C, pH 8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
Tris-HCl buffer
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
-
gel filtration
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
polyamines (spermine, spermidine) at 1-5 mM or Mg2+ at 10 mM confer partial stability on the polyamine oxidase while glycerol or DMSO at 15% concentration confer much higher stability. A combination of glycerol or DMSO together with spermine yielded very good protection on the enzyme with 90% recovery of activity after 30 days
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 7 days, about 20% loss of activity, crude enzyme
-
4°C, 24 h, 90% loss of activity, crude enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE