Information on EC 2.5.1.126 - norspermine synthase

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: Pyrobaculum aerophilum

EC NUMBER
COMMENTARY hide
2.5.1.126
-
RECOMMENDED NAME
GeneOntology No.
norspermine synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
polyamine pathway
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:norspermidine 3-aminopropyltransferase
The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.127, caldopentamine synthase, this enzyme does not accept norspermine as a substrate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
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
2 S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldoheptamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldohexamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + norspermidine
S-methyl-5'-thioadenosine + norspermine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + norspermine
S-methyl-5'-thioadenosine + caldopentamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine
S-methyl-5'-thioadenosine + norspermidine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + thermospermine + H+
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
2 S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldoheptamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + caldopentamine
S-methyl-5'-thioadenosine + caldohexamine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + norspermidine
S-methyl-5'-thioadenosine + norspermine
show the reaction diagram
Q8ZXM4
the long-chain polyamines stabilize double-stranded DNA at high temperatures
-
-
?
S-adenosyl 3-(methylthio)propylamine + norspermine
S-methyl-5'-thioadenosine + caldopentamine
show the reaction diagram
Q8ZXM4
the long-chain polyamines stabilize double-stranded DNA at high temperatures
-
-
?
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine
S-methyl-5'-thioadenosine + norspermidine
show the reaction diagram
Q8ZXM4
the long-chain polyamines stabilize double-stranded DNA at high temperatures
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + thermospermine + H+
show the reaction diagram
Q8ZXM4
spermidine is not the most preferred substrate for any enzyme. Nevertheless, in vivo the enzyme can be responsible for the synthesis of thermospermine, if spermidine is present in a high concentration in competition to other accepted polyamines
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.005
pH 7.5, 95°C, substrate: norspermine
0.052
pH 7.5, 95°C, substrate: spermidine
0.09
pH 7.5, 95°C, substrate: propane-1,3-diamine
0.14
pH 7.5, 95°C, substrate: norspermidine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32800
x * 32800, calculation from sequence
37000
x * 37000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli with an N-terminal 6His sequence