Information on EC 2.5.1.23 - sym-norspermidine synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.5.1.23
-
RECOMMENDED NAME
GeneOntology No.
sym-norspermidine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-thioadenosine + bis(3-aminopropyl)amine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopropyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
polyamine pathway
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:propane-1,3-diamine 3-aminopropyltransferase
The enzyme has been originally characterized from the protist Euglena gracilis [1,2]. The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylthio)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency [3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.22 (spermine synthase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Z, strain 1224-5/25
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine
S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + thermospermine + H+
show the reaction diagram
S-adenosylmethioninamine + propane-1,3-diamine
5'-methylthioadenosine + N-(3-aminopropyl)-1,3-diaminopropane
show the reaction diagram
S-adenosylmethioninamine + propane-1,3-diamine
5'-S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine
show the reaction diagram
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
S-adenosylmethioninamine + spermidine
5'-S-methyl-5'-thioadenosine + spermine
show the reaction diagram
S-adenosylmethioninamine + sym-norspermidine
5'-S-methyl-5'-thioadenosine + ?
show the reaction diagram
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
S-adenosylmethioninamine + propane-1,3-diamine
5'-methylthioadenosine + N-(3-aminopropyl)-1,3-diaminopropane
show the reaction diagram
-
-
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-isobutylthioadenosine
-
-
5'-methylthiotubercidin
-
-
5'-S-ethyl-5'-thioadenosine
-
-
5'-S-methyl-5'-thioadenosine
-
powerful competitive inhibitor
n-propylthioadenosine
-
-
-
S-adenosyl(5')-3-thiopropylamine
-
-
S-adenosyl-3-thio-1,8-diaminooctane
-
-
S-adenosyl-3-thiopropylamine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.675
propane-1,3-diamine
-
pH 7.5, 78C
3.85
putrescine
-
pH 7.5, 78C
0.0079
S-adenosylmethioninamine
-
pH 7.5, 78C
1.539
spermidine
-
pH 7.5, 78C
0.954
sym-norspermidine
-
pH 7.5, 78C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037
5'-S-methyl-5'-thioadenosine
-
pH 7.5, 78C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
5'-isobutylthioadenosine
Sulfolobus solfataricus
-
pH 7.5, 78C
0.1
5'-S-ethyl-5'-thioadenosine
Sulfolobus solfataricus
-
pH 7.5, 78C
0.014
5'-S-methyl-5'-thioadenosine
Sulfolobus solfataricus
-
pH 7.5, 78C
0.1
A9154C
Sulfolobus solfataricus
-
pH 7.5, 78C
0.12
n-propylthioadenosine
Sulfolobus solfataricus
-
pH 7.5, 78C
-
0.021
S-adenosyl-3-thio-1,8-diaminooctane
Sulfolobus solfataricus
-
pH 7.5, 78C
0.016
S-adenosyl-3-thiopropylamine
Sulfolobus solfataricus
-
pH 7.5, 78C
0.1
sinefungin
Sulfolobus solfataricus
-
pH 7.5, 78C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
pH 7.5, 95C, substrate: spermidine
0.038
pH 7.5, 95C, substrate: propane-1,3-diamine
2.059
-
pH 7.5, 78C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
pH 6: about 50% of maximal activity, pH 9.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 110
-
50C: about 40% of maximal activity, 110C: about 45% of maximal activity, 120C: about 20% of maximal activity
60 - 120
-
less than 5% of maximal activity up to 45C. 60C: about 15% of maximal activity, 75C: about 50% of maximal activity, 120C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
112000
-
ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 85
-
protein retains its quarternary structure between 25C and 28C. A highly reversible subtle conformational transition is detected by numerous structure-dependent techniques over 40-45C, with a midpoint centered at 45C
87
-
the mechanism by which the protein achieves thermal stabilization is driven by a conformational equilibrium between two forms of different stability. The stability of each form towards denaturation is characterized by a specific temperature dependence. The low temperature form (form A), is stable over 12-89C. Its stability maximum is 36.8 kJ/mol at 50C. Form B, which is populated at higher temperature, spans the interval 28-146C. Its stability maximum is 71.6 kJ/mol at 87C
90
-
rapidly looses activity above 90C and can no longer be considered native
100
-
1 h, completely stable
120
-
no protection by substrate against thermal inactivation at 120C is observed by incubating the enzyme in the presence of polyamines
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, pH 7.5, stable for 1 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli with an N-terminal 6* His sequence
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
no difference in its activity between the cells harvested during the logarithmic or the stationary phase of growth. Propylamine transferase is not induced by the addition of either 1 mM 1,3-diaminopropane or sym-norspermidine or spermidine to the standard culture medium