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Information on EC 2.5.1.104 - N1-aminopropylagmatine synthase
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EC Tree
2.5.1.104 N1-aminopropylagmatine synthaseIUBMB 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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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
acapt, pf0127, taapt, triamine/agmatine aminopropyltransferase, agmatine/cadaverine aminopropyl transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5'-thioadenosine + N1-(3-aminopropyl)agmatine
-
-
-
-
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine
the enzyme is involved in polyamine biosynthesis
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
S-adenosyl 3-(methylthio)propylamine + agmatine
S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + cadaverine
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
S-adenosyl 3-(methylthio)propylamine + homospermidine
S-methyl-5'-thioadenosine + ?
low activity
-
-
?
S-adenosyl 3-(methylthio)propylamine + N,N'-bis(3-aminopropyl)-1,3-propanediamine
S-methyl-5'-thioadenosine + ?
i.e. thermine. Low activity
-
-
?
S-adenosyl 3-(methylthio)propylamine + norspermidine
S-methyl-5'-thioadenosine + N,N'-bis(3-aminopropyl)-1,3-propanediamine
-
i.e. thermine
-
?
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine
5'-S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine
2.9% of the activity compared to cadaverine
-
-
?
S-adenosyl 3-(methylthio)propylamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylthio)propylamine + spermidine
5'-S-methyl-5'-thioadenosine + spermine
0.8% of the activity compared to cadaverine
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
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
i.e. mitsubishine. Low activity. No formation of tetrakis(3-aminopropyl)ammonium
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
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 + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
4.9% of the activity compared to cadaverine
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
the enzyme is involved in polyamine biosynthesis
-
-
?
S-adenosyl 3-(methylthio)propylamine + cadaverine
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + cadaverine
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
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
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
8.7% of the activity compared to cadaverine
-
-
?
S-adenosyl 3-(methylthio)propylamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
-
-
?
additional information
?
-
only faint activities (less than 10% of spermidine) are detected for diaminopropane [NH2(CH2)3NH2], putrescine, spermine, and caldopentamine
-
-
?
additional information
?
-
-
only faint activities (less than 10% of spermidine) are detected for diaminopropane [NH2(CH2)3NH2], putrescine, spermine, and caldopentamine
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine
the enzyme is involved in polyamine biosynthesis
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
S-adenosyl 3-(methylthio)propylamine + cadaverine
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
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 + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
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 + agmatine
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
the enzyme is involved in polyamine biosynthesis
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 103
70°C: about 50% of maximal activity, 103°C: about 50% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SPEE_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
288
0
33447
Swiss-Prot
-
SPEE_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
314
0
36006
Swiss-Prot
-
SPEE_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
281
0
32334
Swiss-Prot
-
A0A5B8RAG8_9ZZZZ
290
0
31656
TrEMBL
other Location (Reliability: 2)
A0A6A7SE05_9ZZZZ
290
0
31656
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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
brenda
Morimoto, N.; Fukuda, W.; Nakajima, N.; Masuda, T.; Terui, Y.; Kanai, T.; Oshima, T.; Imanaka, T.; Fujiwara, S.
Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis
J. Bacteriol.
192
4991-5001
2010
Thermococcus kodakarensis (Q5JFG9)
brenda
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)
brenda
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
brenda
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Release 2023.1 (January 2023)
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