Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.3.24 - N1-aminopropylagmatine ureohydrolase and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JI38

for references in articles please use BRENDA:EC3.5.3.24
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JI38
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
n1-aminopropylagmatine ureohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
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
agmatine + H2O
putrescine + urea
show the reaction diagram
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
-
-
?
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
in Pyrococcus kodakaraensis spermidine is synthesized mainly from agmatine. The enzyme is involved in the biosynthesis of spermidine from agmatine
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.486
agmatine
pH 7.5, 70°C
0.00642
N1-aminopropylagmatine
pH 7.5, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00186
agmatine
pH 7.5, 70°C
0.001
N1-aminopropylagmatine
pH 7.5, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00387
agmatine
pH 7.5, 70°C
0.165
N1-aminopropylagmatine
pH 7.5, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
enzyme is not fully unfolded
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
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 (Q5JI38), Thermococcus kodakarensis
Manually annotated by BRENDA team