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Information on EC 2.5.1.104 - N1-aminopropylagmatine synthase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U4G1

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EC Tree
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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Pyrococcus furiosus
UNIPROT: Q8U4G1
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
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/cadaverine aminopropyl transferase
-
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 + cadaverine
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
show the reaction diagram
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine
5'-S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine
show the reaction diagram
2.9% of the activity compared to cadaverine
-
-
?
S-adenosyl 3-(methylthio)propylamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
8.7% of the activity compared to cadaverine
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
5'-S-methyl-5'-thioadenosine + spermine
show the reaction diagram
0.8% of the activity compared to cadaverine
-
-
?
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
agmatine is the physiological substrate in the constitutive synthesis of spermidine, while cadaverine acts as an aminopropyl acceptor under stress conditions when an active and rapid synthesis of N-(3-aminopropyl)cadaverine could be required
-
-
?
S-adenosyl 3-(methylthio)propylamine + cadaverine
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
show the reaction diagram
agmatine is the physiological substrate in the constitutive synthesis of spermidine, while cadaverine acts as an aminopropyl acceptor under stress conditions when an active and rapid synthesis of N-(3-aminopropyl)cadaverine could be required
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0076
agmatine
pH 7.4, 70°C
3.77
cadaverine
pH 7.4, 70°C
1.88
propane-1,3-diamine
pH 7.4, 70°C
7.7
putrescine
pH 7.4, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
agmatine
pH 7.4, 70°C
2.09
cadaverine
pH 7.4, 70°C
0.06
propane-1,3-diamine
pH 7.4, 70°C
0.18
putrescine
pH 7.4, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.4
agmatine
pH 7.4, 70°C
0.55
cadaverine
pH 7.4, 70°C
0.032
propane-1,3-diamine
pH 7.4, 70°C
0.023
putrescine
pH 7.4, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 103
70°C: about 50% of maximal activity, 103°C: about 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32334
2 * 32334, calculated from sequence
32600
2 * 32600, SDS-PAGE
65000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, 1.8 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
108
transition temperature
112
transition temperature in presence of 5 mM cadaverine
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
Cacciapuoti, G.; Porcelli, M.; Moretti, M.A.; Sorrentino, F.; Concilio, L.; Zappia, V.; Liu, Z.J.; Tempel, W.; Schubot, F.; Rose, J.P.; Wang, B.C.; Brereton, P.S.; Jenney, F.E.; Adams, M.W.
The first agmatine/cadaverine aminopropyl transferase: biochemical and structural characterization of an enzyme involved in polyamine biosynthesis in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
189
6057-6067
2007
Pyrococcus furiosus (Q8U4G1), Pyrococcus furiosus
Manually annotated by BRENDA team