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Information on EC 3.5.3.1 - arginase and Organism(s) Mus musculus and UniProt Accession Q61176
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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: Mus musculus
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
additional information
?
-
-
arginase II is constitutively expressed in the airways of normal mice, whereas arginase I is undetectable in normal airways, while its expression is increased in airways of mice exposed to ovalbumin
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
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
additional information
?
-
-
arginase II is constitutively expressed in the airways of normal mice, whereas arginase I is undetectable in normal airways, while its expression is increased in airways of mice exposed to ovalbumin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-3-(2-amino-1H-imidazol-5-yl)propanoic acid
-
2-aminoimidazole amino acid inhibitor in which the 2-aminoimidazole moiety serves as a guanidine mimetic, significantly attenuates airways hyperresponsiveness in a murine model of allergic airways inflammation
L-norvaline
-
blocks arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
Polymyxin B
-
blocks arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
additional information
-
cell treatment with anti-CD14 and anti-toll-like receptor 4 but not anti-toll-like receptor 2 antibody decreases arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
-
additional information
-
DL-norvaline does not block arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
-
additional information
-
testing consequences of inhibiting arginase activity in vivo with NO production, lung inflammation, and lung function in both C57BL/6 and NOS2 knockout mice undergoing ovalbumin-induced airway inflammation, a mouse model of asthma
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dexamethasone
-
augments arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
interleukin-4
-
augments arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
-
lipopolysaccharide
-
lipopolysaccharide from Actinobacillus actinomycetemcomitans or Escherichia coli
low-density lipoprotein
-
ArgI expression is potently induced by both oxidized and acetylated low-density lipoprotein in macrophages, this effect is mediated by peroxisome proliferator-activated receptors
-
additional information
-
interferon-gamma does not augment arginase activity in Actinobacillus actinomycetemcomitans lipopolysaccharide-stimulated cells
-
additional information
-
expression of arginase I strongly correlated with the presence of lung inflammation, as quantified by differential cell counts in lung lavage, suggesting that most, or all, of the arginase I in lungs of mice exposed to ovalbumin is present in the inflammatory cells rather than in the airway epithelium
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20
imidazole-3-lactate
Mus musculus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
method for radiochemical detection of arginie to citrulline conversion, to measure NO production in intact aorta, presence of enzyme may confound assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
macrophage cell, infection with Mycobacterium bovis strain AS-1 lacking an arginine permease. AS-1 infection enhances enzyme activity in resting J774.1 cells. Intracellular growth of AS-1 is enhanced by inhibition of enzyme and of ornithine decarboxylase using L-norvaline and difluoromethylornithine treatment
-
isolated microdissected airway preparations. Arginase II is constitutively expressed in the airways of normal mice, whereas arginase I is undetectable in normal airways, while its expression is increased in airways of mice exposed to ovalbumin
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
arginase inhibition increases hepatic nitric oxide in high fat diet-fed mice and reverses the elevated mRNA expression of hepatic genes in lipid metabolism. The expression of phosphorylated 5' adenosine monophosphate-activated protein kinase alpha is increased by arginase inhibition in the mouse liver. Arginase inhibition prevents diet-induced obesity and reduces liver weight
physiological function
physiological function
-
coinhibitory and costimulatory molecules PD-1 and CTLA-4 on the Gr-1+CD11b+ myeloid-derived suppression cells regulate the activity and expression of arginase I. The blockage and silencing of PD-1, CTLA-4 or both PD-1 and CTLA4 molecules can significantly reduce arginase I activity and expression induced with tumor-associated factor. Similar results are also observed while their ligands B7-H1 and/or CD80 are blocked or silenced. CD80 deficiency also decreases the arginase I expression and activity. Antibody blockade or silencing of PD-1, CTLA-4 or both reduces the suppressive potential of PD-1+CTLA-4+ myeloid-derived suppression cells. Blockade of PD-1, CTLA-4 or both also slows tumor growth and improves the survival rate of tumor-bearing mice
physiological function
-
in arginase I-deficient bone marrow chimeric mice, following transfer of arginase I-deficient bone marrow into irradiated recipient mice, arginase I expression is not required for hematopoietic reconstitution and baseline immunity. Arginase I deficiency in bone marrow-derived cells decreases allergen-induced lung arginase by 85.8%. Arginase II-deficient mice have increased lung arginase activity following allergen challenge to a similar level to wild type mice. Bone-marrow-derived arginase I is not required for allergen-elicited sensitization, recruitment of inflammatory cells in the lung, and proliferation of cells. Allergen-induced airway hyperresponsiveness and collagen deposition are similar in arginase-deficient and wild type mice. Arginase II-deficient mice respond similarly to their control wild type mice with allergen-induced inflammation, airway hyperresponsiveness, proliferation and collagen deposition
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ARGI1_MOUSE
323
0
34808
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
infection of macrophage cell J774.1 with Mycobacterium bovis strain AS-1 lacking an arginine permease. AS-1 infection enhances enzyme activity in resting J774.1 cells. Intracellular growth of AS-1 is enhanced by inhibition of enzyme and of ornithine decarboxylase using L-norvaline and difluoromethylornithine treatment
additional information
additional information
-
OVA/OVA mice, murine models of ovalbumin-induced airway inflammation, ARG1 expression is similar to the sam ples from asthma patients. ARG1 is visibly increased throughout the lungs, and strong-positive staining is observed in infiltrating inflammatory cells, bronchiolar and alveolar macrophages, and the peribronchiolar regions in the OVA/OVA mice
additional information
OVA/OVA mice, murine models of ovalbumin-induced airway inflammation, ARG1 expression is similar to the sam ples from asthma patients. ARG1 is visibly increased throughout the lungs, and strong-positive staining is observed in infiltrating inflammatory cells, bronchiolar and alveolar macrophages, and the peribronchiolar regions in the OVA/OVA mice
additional information
-
OVA/OVA mice, murine models of ovalbumin-induced airway inflammation
additional information
OVA/OVA mice, murine models of ovalbumin-induced airway inflammation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
coinhibitory and costimulatory molecules PD-1 and CTLA-4 on the Gr-1+CD11b+ myeloid-derived suppression cells regulate the activity and expression of arginase I. The blockage and silencing of PD-1, CTLA-4 or both PD-1 and CTLA4 molecules can significantly reduce arginase I activity and expression induced with tumor-associated factor. CD80 deficiency also decreases the arginase I expression and activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
specific detection of NO production in intact mouse tissue, inhibition of enzyme by N-hydroxy-nor-L-arginine to avoid disturbances
medicine
medicine
-
overexpression of arginase in the penis contributes to erectile dysfunction
medicine
-
arginase gene expression in the lung is linked to asthma both in clinical studies of human patients and in the well-studied mouse model of ovalbumin-induced airway inflammation
medicine
-
bone marrow cell derived arginase I is the predominant source of allergen-induced lung arginase but is not required for allergen-induced inflammation, airway hyperresponsiveness or collagen deposition
medicine
-
coinhibitory and costimulatory molecules PD-1 and CTLA-4 on the Gr-1+CD11b+ myeloid-derived suppression cells regulate the activity and expression of arginase I. The blockage and silencing of PD-1, CTLA-4 or both PD-1 and CTLA4 molecules can significantly reduce arginase I activity and expression induced with tumor-associated factor. Similar results are also observed while their ligands B7-H1 and/or CD80 are blocked or silenced. CD80 deficiency also decreases the arginase I expression and activity. Antibody blockade or silencing of PD-1, CTLA-4 or both reduces the suppressive potential of PD-1+CTLA-4+ myeloid-derived suppression cells. Blockade of PD-1, CTLA-4 or both also slows tumor growth and improves the survival rate of tumor-bearing mice
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grody, W.W.; Dizikes, G.J.; Cederbaum, S.D.
Human arginase isozymes
Isozymes Curr. Top. Biol. Med. Res.
13
181-214
1987
Bos taurus, Saccharomyces cerevisiae, Canis lupus familiaris, Gallus gallus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Platyrrhini, Mus musculus, Neurospora crassa, Rattus norvegicus
Kuhn, N.J.; Talbot, J.; Ward, S.
pH-Sensitive control of arginase by Mn(II) ions at submicromolar concentrations
Arch. Biochem. Biophys.
286
217-221
1991
Mus musculus
Hrabak, A.; Bajor, T.; Temesi, A.
Comparison of substrate and inhibitor specificity of arginase and nitric oxide (NO) synthase for arginine analogues and related compounds in murine and rat macrophages
Biochem. Biophys. Res. Commun.
198
206-212
1994
Mus musculus, Rattus norvegicus
Talaue, M.T.; Venketaraman, V.; Hazbon, M.H.; Peteroy-Kelly, M.; Seth, A.; Colangeli, R.; Alland, D.; Connell, N.D.
Arginine homeostasis in J774.1 macrophages in the context of Mycobacterium bovis BCG infection
J. Bacteriol.
188
4830-4840
2006
Mus musculus
Yasuda, N.; Moriwaki, K.; Furuyama, S.
Distribution and properties of arginase in the salivary glands of four species of laboratory mammals
J. Comp. Physiol. B
174
237-242
2004
Mus musculus, Rattus norvegicus
de Bono, J.P.; Warrick, N.; Bendall, J.K.; Channon, K.M.; Alp, N.J.
Radiochemical HPLC detection of arginine metabolism: Measurement of nitric oxide synthesis and arginase activity in vascular tissue
Nitric Oxide
16
1-9
2007
Mus musculus
Bivalacqua, T.J.; Burnett, A.L.; Hellstrom, W.J.; Champion, H.C.
Overexpression of arginase in the aged mouse penis impairs erectile function and decreases eNOS activity: influence of in vivo gene therapy of anti-arginase
Am. J. Physiol. Heart Circ. Physiol.
292
H1340-H1351
2007
Mus musculus, Mus musculus B6/129
Hrabak, A.; Bajor, T.; Meszaros, G.
The inhibitory effect of various indolyl amino acid derivatives on arginase activity in macrophages
Amino Acids
34
293-300
2008
Bos taurus, Mus musculus
Gallardo-Soler, A.; Gomez-Nieto, C.; Campo, M.L.; Marathe, C.; Tontonoz, P.; Castrillo, A.; Corraliza, I.
Arginase I induction by modified lipoproteins in macrophages: a peroxisome proliferator-activated receptor-{gamma}/{delta}-mediated effect that links lipid metabolism and immunity
Mol. Endocrinol.
22
1394-1402
2008
Mus musculus
Sosroseno, W.; Musa, M.; Ravichandran, M.; Fikri Ibrahim, M.; Bird, P.S.; Seymour, G.J.
Arginase activity in a murine macrophage cell line (RAW264.7) stimulated with lipopolysaccharide from Actinobacillus actinomycetemcomitans
Oral Microbiol. Immunol.
21
145-150
2006
Mus musculus
North, M.L.; Khanna, N.; Marsden, P.A.; Grasemann, H.; Scott, J.A.
Functionally Important Role for Arginase 1 in the Airways Hyperresponsiveness of Asthma
Am. J. Physiol. Lung Cell Mol. Physiol.
296
L911-L920
2009
Homo sapiens, Homo sapiens (P05089), Mus musculus, Mus musculus (Q61176)
Kenyon, N.J.; Bratt, J.M.; Linderholm, A.L.; Last, M.S.; Last, J.A.
Arginases I and II in lungs of ovalbumin-sensitized mice exposed to ovalbumin: sources and consequences
Toxicol. Appl. Pharmacol.
230
269-275
2008
Mus musculus
Bratt, J.M.; Franzi, L.M.; Linderholm, A.L.; Last, M.S.; Kenyon, N.J.; Last, J.A.
Arginase enzymes in isolated airways from normal and nitric oxide synthase 2-knockout mice exposed to ovalbumin
Toxicol. Appl. Pharmacol.
234
273-280
2009
Mus musculus
Bera, S.; Wallimann, T.; Ray, S.; Ray, M.
Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells
FEBS J.
275
5899-5909
2008
Mus musculus
Niese, K.; Collier, A.; Hajek, A.; Cederbaum, S.; OBrien, W.; Wills-Karp, M.; Rothenberg, M.; Zimmermann, N.
Bone marrow cell derived arginase I is the major source of allergen-induced lung arginase but is not required for airway hyperresponsiveness, remodeling and lung inflammatory responses in mice
BMC Immunol.
10
33
2009
Mus musculus
Liu, Y.; Yu, Y.; Yang, S.; Zeng, B.; Zhang, Z.; Jiao, G.; Zhang, Y.; Cai, L.; Yang, R.
Regulation of arginase i activity and expression by both PD-1 and CTLA-4 on the myeloid-derived suppressor cells
Cancer Immunol. Immunother.
58
687-697
2009
Mus musculus
Ilies, M.; Di Costanzo, L.; North, M.L.; Scott, J.A.; Christianson, D.W.
2-aminoimidazole amino acids as inhibitors of the binuclear manganese metalloenzyme human arginase I
J. Med. Chem.
53
4266-4276
2010
Mus musculus, Homo sapiens (P05089), Homo sapiens
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