Information on EC 3.5.3.10 - D-arginase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.5.3.10
-
RECOMMENDED NAME
GeneOntology No.
D-arginase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arginine + H2O = D-ornithine + urea
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bond
hydrolysis of linear amidines
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-Arginine and D-ornithine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
D-arginine amidinohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37289-14-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KUJ8602
SwissProt
Manually annotated by BRENDA team
strain KUJ8602
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
toad
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-guanidinopropionate + H2O
3-aminopropanoate + urea
show the reaction diagram
4-Guanidinobutyrate + H2O
4-Aminobutyrate + urea
show the reaction diagram
D-arginine + H2O
?
show the reaction diagram
D-arginine + H2O
D-ornithine + urea
show the reaction diagram
L-arginine + H2O
L-ornithine + urea
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-arginine + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
activation
Zn2+
1 g-atom bound to 1 mol of subunit, dependent on, removal causes loss of activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
inactivation due to removal of bound Zn2+, reversible by Zn2+ and Co2+, and partially by Mn2+
5-Aminovalerate
competitive inhibition
Al3+
-
-
Cu2+
-
-
Hg2+
-
-
L-Lys
-
-
L-Orn
-
-
Mercaptoacetate
strong mixed-type inhibitor
Zn2+
-
-
Zr4+
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.71
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
with substrate 4-guanidinobutyrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
6 * 40000, SDS-PAGE
232000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
20% loss of activity in 24 h due to autolysis
37
-
70% loss of activity in 24 h due to autolysis
55
-
10 min, 50% loss of activity in absence of Mn2+, 10% loss of activity in presence of Mn2+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli