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Information on EC 3.5.3.1 - arginase and Organism(s) Entamoeba histolytica and UniProt Accession C4LSS0

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.3 In linear amidines
                3.5.3.1 arginase
IUBMB Comments
Also hydrolyses alpha-N-substituted L-arginines and canavanine.
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This record set is specific for:
Entamoeba histolytica
UNIPROT: C4LSS0
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Word Map
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The taxonomic range for the selected organisms is: Entamoeba histolytica
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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L-arginine
+
H2O
=
L-ornithine
+
urea
+
=
+
Synonyms
arginase, arginase-1, arginase i, arginase 1, arginase ii, arginase-2, serum arginase, arginase1, l-arginase, liver-type arginase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
arginine amidinase
-
-
-
-
arginine transamidinase
-
-
-
-
canavanase
-
-
-
-
Kidney-type arginase
-
-
-
-
L-arginase
-
-
-
-
Liver-type arginase
-
-
-
-
Non-hepatic arginase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amidines
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine amidinohydrolase
Also hydrolyses alpha-N-substituted L-arginines and canavanine.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-96-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine + H2O
L-ornithine + 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
L-arginine + H2O
L-ornithine + urea
show the reaction diagram
the enzyme catalyses the catabolism of L-arginine to L-ornithine and urea
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Cd2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Co2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Cu2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Hg2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Mg2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Mn2+
two Mn2+ ions are required for the enzyme to be fully functional
NaCl
the enzyme is optimally active at 100 mM NaCl, but as the salt concentration increase, the activity of the enzyme is reduced to almost half of the maximal activity but the enzyme is still partially active
Ni2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Zn2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
the enzyme is optimally active at 100 mM NaCl, but as the salt concentration increased, the activity of the enzyme was reduced to almost half of the maximal activity but the enzyme was still partially active
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
pH 5.0: about 55% of maximal activity, pH 11.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 70
4°C: about 80% of maximal activity, 70°C: about 95% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyses the catabolism of l-arginine to l-ornithine and urea. First committed step in polyamine biosynthesis. In pathogenic organisms, arginase plays a crucial role in depleting host L-arginine, a substrate for nitric oxide synthase that participates in protective immunity, thereby evading host immune response
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C4LSS0_ENTHI
296
0
32844
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
exists in monomeric and dimeric form in solution
monomer
exists in monomeric and dimeric form in solution
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
urea
8 M urea denatures the enzyme which results in the release of the deeply embedded metal ion too
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli Rosetta (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malik, A.; Singh, H.; Pareek, A.; Tomar, S.
Biochemical and biophysical insights into the metal binding spectrum and bioactivity of arginase of Entamoeba histolytica
Metallomics
10
623-638
2018
Entamoeba histolytica (C4LSS0), Entamoeba histolytica
Manually annotated by BRENDA team