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Information on EC 3.5.3.24 - N1-aminopropylagmatine ureohydrolase and Organism(s) Thermus thermophilus and UniProt Accession Q5SJ85

for references in articles please use BRENDA:EC3.5.3.24
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IUBMB Comments
The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.
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Thermus thermophilus
UNIPROT: Q5SJ85
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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
n1-aminopropylagmatine ureohydrolase, more
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
N1-aminopropylagmatine amidinohydrolase
The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N1-aminopropylagmatine + H2O
spermidine + urea
show the reaction diagram
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
N1-aminopropylagmatine + H2O
spermidine + urea
show the reaction diagram
the enzyme is involved in biosynthesis of spermidine. The conversion of N1-aminopropylagmatine to spermidine is essential for production of long and branched polyamines in Thermus thermophilus
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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a disruption mutant accumulates N1-aminopropylagmatine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32500
x * 32500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32500, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression 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 (Q5SJ85)
Manually annotated by BRENDA team