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Information on EC 2.5.1.104 - N1-aminopropylagmatine synthase and Organism(s) Thermus thermophilus and UniProt Accession Q5SK28

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IUBMB Comments
The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase.
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q5SK28
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The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
acapt, pf0127, taapt, triamine/agmatine aminopropyltransferase, agmatine/cadaverine aminopropyl transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agmatine aminopropyltransferase
-
triamine/agmatine aminopropyltransferase
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase
The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase.
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 + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + agmatine
S-methyl-5'-thioadenosine + N1-aminopropylagmatine
show the reaction diagram
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + homospermidine
S-methyl-5'-thioadenosine + ?
show the reaction diagram
low activity
-
-
?
S-adenosyl 3-(methylthio)propylamine + N,N'-bis(3-aminopropyl)-1,3-propanediamine
S-methyl-5'-thioadenosine + ?
show the reaction diagram
i.e. thermine. Low activity
-
-
?
S-adenosyl 3-(methylthio)propylamine + norspermidine
S-methyl-5'-thioadenosine + N,N'-bis(3-aminopropyl)-1,3-propanediamine
show the reaction diagram
-
i.e. thermine
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
show the reaction diagram
-
no formation of thermospermine (i.e. 1,12-diamino-4,8-diazadodecane)
-
?
S-adenosyl 3-(methylthio)propylamine + tris(3-aminopropyl)amine
S-methyl-5'-thioadenosine + N4-aminopropylthermine
show the reaction diagram
i.e. mitsubishine. Low activity. No formation of tetrakis(3-aminopropyl)ammonium
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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 + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
show the reaction diagram
the enzyme is involved in polyamine biosynthesis
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.77
agmatine
0.57
norspermidine
pH 9.0, 37°C
1.64
S-adenosyl 3-(methylthio)propylamine
pH 9.0, 37°C
0.00173
spermidine
pH 9.0, 37°C
38.31
tris(3-aminopropyl)amine
pH 9.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37
agmatine
0.53
norspermidine
pH 9.0, 37°C
0.73
S-adenosyl 3-(methylthio)propylamine
pH 9.0, 37°C
0.65
spermidine
pH 9.0, 37°C
0.29
tris(3-aminopropyl)amine
pH 9.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
480
agmatine
920
norspermidine
pH 9.0, 37°C
450
S-adenosyl 3-(methylthio)propylamine
pH 9.0, 37°C
375
spermidine
pH 9.0, 37°C
7.6
tris(3-aminopropyl)amine
pH 9.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4
pH 8.5, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
gel filtration
32500
x * 32500, SDS-PAGE
36006
4 * 36006, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32500, SDS-PAGE
homotetramer
4 * 36006, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
stable around pH 10.0 at room temperature
720250
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ohnuma, M.; Terui, Y.; Tamakoshi, M.; Mitome, H.; Niitsu, M.; Samejima, K.; Kawashima, E.; Oshima, T.
N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus
J. Biol. Chem.
280
30073-30082
2005
Thermus thermophilus (Q5SK28)
Manually annotated by BRENDA team
Ohnuma, M.; Ganbe, T.; Terui, Y.; Niitsu, M.; Sato, T.; Tanaka, N.; Tamakoshi, M.; Samejima, K.; Kumasaka, T.; Oshima, T.
Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus
J. Mol. Biol.
408
971-986
2011
Thermus thermophilus (Q5SK28), Thermus thermophilus
Manually annotated by BRENDA team