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Information on EC 3.5.3.1 - arginase and Organism(s) Helicobacter pylori and UniProt Accession O25949
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3.5.3.1 arginaseIUBMB Comments
Also hydrolyses alpha-N-substituted L-arginines and canavanine.
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Word Map
- 3.5.3.1
- endothelial
- tnf
- polyamines
-
myeloid-derived
- necrosis
- myeloid
- monocyte
- arterial
- lps
- lipopolysaccharide
- peritoneal
- l-ornithine
-
mdscs
- pulmonary
- microglia
- ammonia
- t-cells
- argininosuccinate
- airway
- leishmania
- hypertension
- asthma
- putrescine
-
immunotherapy
-
marrow-derived
-
tumor-associated
- leishmaniasis
-
transcarbamylase
-
vasodilation
-
neuroinflammation
- l-citrulline
- dimethylarginine
- interleukin-10
-
tregs
-
l-name
-
endothelium-dependent
- urease
- agmatine
-
m2-like
- hyperammonemia
-
no-dependent
- amazonensis
-
erectile
- no-synthase
- medicine
-
dimethylaminohydrolase
- ng-monomethyl-l-arginine
-
bmdms
- carbamoylphosphate
-
il-4-induced
- analysis
- synthesis
- pharmacology
- food industry
- drug development
- nutrition
- phosphodiesterase-5
The taxonomic range for the selected organisms is: Helicobacter pylori
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
arginase, arginase-1, arginase i, arginase 1, arginase ii, arginase-2, serum arginase, arginase1, l-arginase, liver-type arginase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
arginine amidinase
-
-
-
-
arginine transamidinase
-
-
-
-
canavanase
-
-
-
-
Kidney-type arginase
-
-
-
-
L-arginase
-
-
-
-
Liver-type arginase
-
-
-
-
Non-hepatic arginase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of linear amidines
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine amidinohydrolase
Also hydrolyses alpha-N-substituted L-arginines and canavanine.
CAS REGISTRY NUMBER
COMMENTARY
9000-96-8
-
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
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
enzyme is involved in acid resistance and inhibits host nitric oxide production
-
-
?
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
L-arginine + H2O
L-ornithine + urea
-
enzyme is involved in acid resistance and inhibits host nitric oxide production
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
Mn2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
Ni2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
Co2+
Mn2+
Ni2+
additional information
-
metalloenzyme, a metal ion is absolutely required for activity, no activation with Zn2+, Cu2+, Fe2+, Ca2+, and Mg2+
Co2+
-
the Co2+- and Mn2+-reconstituted enzymes exhibit cooperative mechanism of arginine hydrolysis, and undergo self-association and activation with increasing concentrations. Co2+ ions play a more important role in the local tertiary structure of the protein than Mn2+
Mn2+
-
the Co2+- and Mn2+-reconstituted enzymes exhibit cooperative mechanism of arginine hydrolysis, and undergo self-association and activation with increasing concentrations. Co2+ ions play a more important role in the local tertiary structure of the protein than Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
enzyme depleted of metal and reconstituted with Co2+, complete loss of activiy. Enzyme reconstitued with Mn2+, 20% loss of activity. Loss of catalytic activity in the wild-type protein with dithiothreitol is due to the interaction with Co2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
L-arginine
-
mutant S89G, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 2.1
4.4
L-arginine
-
mutant H91A, Co2+-activated, pH 5.0, 37°C, Hill coefficient 2.3
5.2
L-arginine
-
mutant A92S, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 1.6
5.9
L-arginine
-
mutant A92S, Co2+-activated, pH 5.0, 37°C, Hill coefficient 1.9
5.9
L-arginine
-
mutant S89G, Co2+-activated, pH 5.0, 37°C, Hill coefficient 2.2
6.3
L-arginine
-
mutant S88G, Co2+-activated, pH 5.0, 37°C, Hill coefficient 2.0
6.4
L-arginine
-
mutant E90A, Co2+-activated, pH 5.0, 37°C, Hill coefficient 1.7
6.7
L-arginine
-
mutant S88G/A92S, Co2+-activated, pH 5.0, 37°C, Hill coefficient 2.0
6.7
L-arginine
-
pH 5.0, 37°C, Mn2+-activited enzyme, K0.5 value, Hill-coefficient 1.6
6.7
L-arginine
-
wild-type, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 1.6
8.4
L-arginine
-
pH 5.0, 37°C, Co2+-activited enzyme, K0.5 value, Hill-coefficient 2.1
8.4
L-arginine
-
wild-type, Co2+-activated, pH 5.0, 37°C, Hill coefficient 2.1
8.7
L-arginine
-
mutant S88G, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 2.4
9.2
L-arginine
-
mutant S88G/A92S, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 2.2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
assay requires heat activation of enzyme in presence of metal cofactor at 50-55°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the disulfide bond is important for the overall stability and folding of the protein. Mutant proteins lacking the disulfide bond start to unfold at lower temperature than the wild-type. In the mutant proteins, the Tm of the holoenzyme is 4°C higher than that of the apoenzyme indicating that in the absence of the disulfide bond the metal ions have relatively larger role in the stability of the mutant proteins compared to the wild-type
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
monomer and dimer with monomer being the major form, but the dimer is associated with higher catalytic activity, analytical gel filtration. The proportion of dimer decreases with increasing salt concentrations
monomer
-
monomer and dimer with monomer being the major form, but the dimer is associated with higher catalytic activity, analytical gel filtration. The proportion of dimer decreases with increasing salt concentrations
?
-
x * 37800-40000, about, His-tagged enzyme, sequence calculation and SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling based on Bacillus caldovelox crystal structure. Residues D116, D120, D234, D236 and H91, H118, H133 contribute to catalysis and stability of binuclear metal center of arginase and have an important role in binding and catalytic activity in the active site
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A92S
-
mutation of A92 to its analogous residues in other arginases individually enhances the catalytic activity
C66A
-
residue involved in disulfide bond. Catalytic turnover and the catalytic efficiency for the mutant proteins similar to the wild-type
C73A
-
residue involved in disulfide bond. Catalytic turnover and the catalytic efficiency for the mutant proteins similar to the wild-type
E90A
-
residue E90 is important for catalytic activity and plays a crucial role in retaining the metal ion at the active site
H91A
-
residue E90 is important for catalytic activity and plays a crucial role in retaining the metal ion at the active site
S88G
-
mutation of Ser88 to its analogous residues in other arginases individually enhances the catalytic activity
S88G/A92S
-
mutation of S88 and A92 to its analogous residues in other arginases individually enhances the catalytic activity
additional information
-
enzyme disruption mutant. Helicobacter pylori extracts and intact Helicobacter pylori of wild-type, but not of enzyme deficient mutant, induce a decreased expression of CD3zeta-chain of the TCR in Jurkat cells and reduce proliferation of freshly isolated human normal T-lymphocytes
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
69
71
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis results in in loss of over 90% activity, highly unstable enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, His-tagged recombinant protein, 1:2 dilution with 100% glycerol, 4 months, 45-65% loss of activity
-
-20°C, purified recombinant enzyme, 1:2 with glycerol, loss of 45-65% activity after 4 months, and of over 90% after 6 months
-
4°C, His-tagged recombinant protein, 1:2 dilution with 100% glycerol, 1 week, 90% loss of activity
-
4°C, purified recombinant enzyme, 1:2 with glycerol, over 90% loss of activity within 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rocF, functional expression in Escherichia coli DH5alpha as His-tagged enzyme
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation of heat- or urea-denatured enzyme by chaperone thioredoxin Trx1 from Helicobacter pylori extracts
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme is involved in T-cell function during infection. Helicobacter pylori extracts and intact Helicobacter pylori of wild-type, but not of enzyme deficient mutant, induce a decreased expression of CD3zeta-chain of the TCR in Jurkat cells and reduce proliferation of freshly isolated human normal T-lymphocytes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mendz, G.L.; Holmes, E.M.; Ferrero, R.L.
In situ characterization of Helicobacter pylori arginase
Biochim. Biophys. Acta
1388
465-477
1998
Helicobacter pylori
McGee, D.J.; Zabaleta, J.; Viator, R.J.; Testerman, T.L.; Ochoa, A.C.; Mendz, G.L.
Purification and characterization of Helicobacter pylori arginase, RocF: unique features among the arginase superfamily
Eur. J. Biochem.
271
1952-1962
2004
Helicobacter pylori, Helicobacter pylori ATCC 43504
McGee, D.J.; Kumar, S.; Viator, R.J.; Bolland, J.R.; Ruiz, J.; Spadafora, D.; Testerman, T.L.; Kelly, D.J.; Pannell, L.K.; Windle, H.J.
Helicobacter pylori thioredoxin is an arginase chaperone and guardian against oxidative and nitrosative stresses
J. Biol. Chem.
281
3290-3296
2006
Helicobacter pylori
Zabaleta, J.; McGee, D.J.; Zea, A.H.; Hernandez, C.P.; Rodriguez, P.C.; Sierra, R.A.; Correa, P.; Ochoa, A.C.
Helicobacter pylori arginase inhibits T cell proliferation and reduces the expression of the TCR zeta-chain (CD3zeta)
J. Immunol.
173
586-593
2004
Helicobacter pylori
Viator, R.J.; Rest, R.F.; Hildebrandt, E.; McGee, D.J.
Characterization of Bacillus anthracis arginase: effects of pH, temperature, and cell viability on metal preference
BMC Biochem.
9
15
2008
Bacillus anthracis, Helicobacter pylori, Bacillus anthracis 7702
Srivastava, A.; Dwivedi, N.; Sau, A.K.
Role of a disulphide bond in Helicobacter pylori arginase
Biochem. Biophys. Res. Commun.
395
348-351
2010
Helicobacter pylori
Azizian, H.; Bahrami, H.; Pasalar, P.; Amanlou, M.
Molecular modeling of Helicobacter pylori arginase and the inhibitor coordination interactions
J. Mol. Graph. Model.
28
626-635
2010
Helicobacter pylori
Srivastava, A.; Sau, A.K.
Biochemical studies on Helicobacter pylori arginase: insight into the difference in activity compared to other arginases
IUBMB Life
62
906-915
2010
Helicobacter pylori
Srivastava, A.; Dwivedi, N.; Samanta, U.; Sau, A.K.
Insight into the role of a unique SSEHA motif in the activity and stability of Helicobacter pylori arginase
IUBMB Life
63
1027-1036
2011
Helicobacter pylori
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