Any feedback?
Information on EC 3.5.3.1 - arginase and Organism(s) Rattus norvegicus and UniProt Accession O08701
for references in articles please use BRENDA:EC3.5.3.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.3.1 arginaseIUBMB Comments
Also hydrolyses alpha-N-substituted L-arginines and canavanine.
Specify your search results
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: Rattus norvegicus
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
arginase
arginase I
arginine amidinase
-
-
-
-
arginine transamidinase
-
-
-
-
canavanase
-
-
-
-
Kidney-type arginase
-
-
-
-
L-arginase
-
-
-
-
Liver-type arginase
-
-
-
-
Non-hepatic arginase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arginine + H2O = L-ornithine + urea
Asn130 and Ser137 are involved in substrate binding and catalysis
-
L-arginine + H2O = L-ornithine + urea
H141 serves as an acid/base catalyst, deprotonating the metal-bridging water molecule to generate the metal-bridging hydroxide nucleophile, and by protonating the amino group of the product to facilitate its departure
-
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
1-nitro-3-guanidinobenzene + H2O
3-nitrobenzenamine + urea
-
synthetic chromophoric substrate, low activity
-
-
?
4-guanidino-2-nitrophenylacetic acid + H2O
4-amino-2-nitrophenylacetate + urea
-
-
-
-
?
4-guanidino-3-nitrobenzoic acid + H2O
4-amino-3-nitrobenzoate + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
arginase competes with nitric oxide synthases for L-arginine as the common substrate
-
-
?
additional information
?
-
-
mitochondrial isoform arginase II negatively regulates NO synthase 1 activity by limiting substrate availability in its microdomain
-
-
?
additional information
?
-
-
model cluster used to simulate the active site of arginase is built starting from the 1.7 A X-ray structure of rat liver arginase complexed with the inhibitor 2(S)-amino-6-boronohexanoic acid (ABH)
-
-
?
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
?
-
-
mitochondrial isoform arginase II negatively regulates NO synthase 1 activity by limiting substrate availability in its microdomain
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
arginase competes with nitric oxide synthases for L-arginine as the common substrate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
-
dependent on, manganese-metalloenzyme, activates isozyme I, slightly, and isozyme II
Mn2+
-
dependent on, manganese-metalloenzyme, wild-type enzyme contains 1.97 mol Mn2+ per mol of subunit, mutants R308A and R308E contain 2.1 mol, and mutant R308K 1.25 mol per mol of subunit
Mn2+
-
arginase is a better biological catalyst for arginine hydrolysis when both cations are retained and a hydroxide ion is present in the active site bridging the two Mn metal centers
Mn2+
manganese metalloenzyme, Mn2+-Mn2+ cluster in the active site of each monomer
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epicatechin
-
(-)-epicatechin leads to a decreased arginase-2 mRNA expression after 24 h of incubation, in contrast a weak basal arginase-1 mRNA expression is not affected
caffeic acid
-
inhibiting arginase activity by caffeic acid and chlorogenic acid might be a possible mechanism by which they exert their cardio-protective effect
chlorogenic acid
-
inhibiting arginase activity by caffeic acid and chlorogenic acid might be a possible mechanism by which they exert their cardio-protective effect
diethyl dicarbonate
-
second-order rate constant of 113 per M and s for inactivation process. L-ornithine partially protects, L-ornithine plus borate completely protect
flavanol-rich cocoa
-
cocoa flavanols lower arginase-2 mRNA expression and activity
-
fluoride
-
substrate inhibition of liver enzyme at concentration above 4 mM, the kidney enzyme is more sensitive and is inhibited uncompetitively, at narrow L-arginie concentration, at 1 mM, preincubation with F- does not affect the enzymes
Nomega-nitro-L-arginine methyl ester
-
i.e. L-NAME, inhibition of enzyme from liver and colon cancer cells in vitro and in vivo
S-(2-boronomethyl)-L-cysteine
i.e. BMC, 50% inhibition at 3.8 mM, pH 7.4, or at 7.5 mM, pH 9.0
S-(2-boronomethyl)-L-homocysteine
i.e. BMHC, 50% inhibition at 0.35 mM, pH 7.4, or above 1 mM, pH 9.0
Cd2+
-
mixed competitive inhibitor. Kidney enzyme is more sensitive to inhibition than liver enzyme. Cd2+ enhances substrate activation of kidney enzyme while still being inhibitory. Cd2+ is also inhibitory to kidney enzyme in presence of Mn2+
Cu2+
-
56% inhibition of isozyme I, 69% inhibition of isozyme II, non-linear allosteric inhibition for isozymes I and II, inhibition is increased with isozyme I by preincubation with the metal ions, not with isozyme II
Hg2+
-
80% inhibition of isozyme I, 96% inhibition of isozyme II, non-linear allosteric inhibition for isozymes I and II, inhibition is increased with isozyme I by preincubation with the metal ions, not with isozyme II
S-(2-boronoethyl)-L-cysteine
i.e. BEC, 50% inhibition at 0.005 mM, pH 7.4, or at 0.020 mM, pH 9.0
S-(2-boronoethyl)-L-cysteine
-
inhibition results in augmented Ca2+-dependent NO synthase activity and NO production in isolated myocytes
additional information
-
effect of preincubation of the isozymes with metal ions, overview
-
additional information
-
isothiourea homologues undergo rapid non-enzymic rearrangement to probably give inhibitory compouds, overview
-
additional information
-
ebselen does not inhibit arginase, apocynin does not affect the stability of arginase I mRNA but accelerates the decline of arginase activity when protein synthesis is inhibited by cycloheximide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydralazine
-
treatment with 20 mg/kg/day hydralazine for 5 weeks causes increased arginase activity in hypertensive rats
L-arginine
-
strong substrate activation of the kidney enzyme at concentrations above 4 mM
lipopolysaccharide
-
0.001 mg/ml cause a 2fold increase in arginase activity and a marked increase in mRNA encoding arginase I
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
L-arginine
T135S mutant, KM increases 2.5fold relatively to values measured for the wild-type enzyme
13
L-arginine
T135A mutant, KM is increased 13fold relatively to values measured for the wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
260
L-arginine
T135A mutant, is reduced 26% relative to values measured for the wild-type enzyme
350
L-arginine
T135S mutant, kcat is unchanged relatively to values measured for the wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.061
Nomega-hydroxy-L-arginine
-
pH 9.5, 37°C, enzyme from submandibular gland
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
developmental changes in arginase expression and activity in the lung
24h culture, both enzyme and NOS-2 activity depend strongly on extracellular L-arginine concentrations. Competing for L-arginine influx by addition of L-lysine results in 60-70% inhibition of enzyme. Addition of enzyme inhibitor L-valine to cells leads to 80-90% decrease in enzyme activity and 25% increase in NOS-2 activity
developmental changes in arginase expression and activity in the lung
-
significant decrease of enzyme activity during 7th-21st day of gestation, significant increase in enzyme activity at term gestation, day 22. Gestational changes in enzyme activity negatively correlate with those in cyclic GMP production and positively correlate with those in endogenous NO synthase inhibitors and endothelin-1 contents. Enhanced enzyme activity at term gestation may be implicated in increasing myometrial contractions mediated by increase in endothelin-1
-
submandibular, sublingual, and parotid gland, 3.6-7.3% of the activity in liver. In submandibluar gland, presence of both isoform arginase I and arginase II
-
rejection of skin xenografts, but not allografts, is associated with a local high production of Th2 cytokines IL-4 and IL-10, overexpression of enzyme, strongly enhanced enzyme activity and attenuated NO generation in the graft
additional information
-
-
additional information
arginase II is regulated developmentally, and both expression and activity are maximal during fetal life
additional information
arginase II is regulated developmentally, and both expression and activity are maximal during fetal life
additional information
-
rejection of skin xenografts, but not allografts, is associated with a local high production of Th2 cytokines IL-4 and IL-10, overexpression of enzyme, strongly enhanced enzyme activity and attenuated NO generation in the graft
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). ARGI2_RAT
354
0
38640
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
additional information
trimer
trimeric quaternary structure in which each monomer adopts an alpha/betafold consisting of a central parallel eight-stranded beta-sheet flanked on both sides by several alpha-helices
additional information
-
isolated myocyte, enzyme arginase II co-immunoprecipitates with NO synthase 1, but not with NO synthase 3
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform arginase I in complex with inhibitor (S)-2-amino-7-oxoheptanoic acid. Inhibitor aldehyde moiety is hydrated to form the gem-diol, one hydroxyl group bridges the Mn2+ cluster and donates a hydrogen bond to D128, and the second hydroxyl group donates a hydrogen bond to E277
-
recombinant R308K mutant, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
T135A rat arginase I-BEC complex and unliganded N130A rat arginase I are crystallized by the hanging drop vapor diffusion method at 4°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D183A
site-directed mutagenesis. KM is increased 14fold, whereas the value of kcat is reduced 24fold, relative to values measured for the wild-type enzyme
N130A
site-directed mutagenesis. The value of KM is increased 50fold, whereas the value of kcat is reduced only 37%, relative to values measured for the wild-type enzyme
R308A
-
site-directed mutagenesis, 17% activity compared to the wild-type enzyme, mutant forms monomers instead of trimers like the wild-type enzyme, reduced unfolding temperature compared to the wild-type enzyme
R308E
-
site-directed mutagenesis, 17% activity compared to the wild-type enzyme, mutant forms monomers instead of trimers like the wild-type enzyme, reduced unfolding temperature compared to the wild-type enzyme
R308K
-
site-directed mutagenesis, 13% activity compared to the wild-type enzyme, mutant forms monomers instead of trimers like the wild-type enzyme, reduced unfolding temperature compared to the wild-type enzyme
T135A
site-directed mutagenesis, substitution of T135 with Ala destroys hydrogen-bonding potential
T135S
site-directed mutagenesis, substitution of T135 with serine conserves hydrogen-bonding potential
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants are overexpressed and purified from Escherichia coli BL21(DE3) cells using a pET29b expression vector
overexpression of wild-type and mutant enzymes in Escherichia coli BL21(DE3)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
arginase activity may interfere in nitric oxide activity assay. A nitric oxide synthase-independent radioactive signal in mitochondrial samples analyzed for nitric oxide synthase-catalyzed [14C]-L-arginine to [14C]-L-citrulline conversion is due to the arginase-catalyzed conversion of [14C]-L-arginine to [14C]-urea. The results, in addition to reconfirming the absence of nitric oxide synthase activity in rat liver MT, show the need to include arginase inhibitors in studies using mitochondrial samples in order to avoid confounding results when using nitric oxide synthase activity assays
medicine
additional information
medicine
-
rejection of skin xenografts, but not allografts, is associated with a local high production of Th2 cytokines IL-4 and IL-10, overexpression of enzyme, strongly enhanced enzyme activity and attenuated NO generation in the graft. Upregulation of enzyme activity limits the bioavailability of L-arginine for the inducible NO synthase and thus attenuates generation of NO by the graft-infiltrating macrophages
medicine
-
significant decrease of enzyme activity during 7th-21st day of gestation, significant increase in enzyme activity at term gestation, day 22. Gestational changes in enzyme activity negatively correlate with those in cyclic GMP production and positively correlate with those in endogenous NO synthase inhibitors and endothelin-1 contents. Enhanced enzyme activity at term gestation may be implicated in increasing myometrial contractions mediated by increase in endothelin-1
medicine
enzyme serves as a therapeutic target for the treatment of asthma, erectile dysfunction, and atherosclerosis
additional information
pulmonary vascular and airway diseases in which arginase activity is increased are associated with decreased NO production and reduced smooth muscle relaxation
additional information
pulmonary vascular and airway diseases in which arginase activity is increased are associated with decreased NO production and reduced smooth muscle relaxation
additional information
pulmonary vascular and airway diseases in which arginase activity is increased are associated with decreased NO production and reduced smooth muscle relaxation
additional information
pulmonary vascular and airway diseases in which arginase activity is increased are associated with decreased NO production and reduced smooth muscle relaxation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ratner, S.
Enzymes of arginine and urea synthesis
Adv. Enzymol. Relat. Areas Mol. Biol.
39
1-90
1973
Rattus norvegicus
Kaysen, G.A.; Strecker, H.J.
Purification and properties of arginase of rat kidney
Biochem. J.
133
779-788
1973
Rattus norvegicus
Fujimoto, M.; Kameji, T.; Kanaya, A.; Hagihira, H.
Purification and properties of rat small intestinal arginase
J. Biochem.
79
441-449
1976
Rattus norvegicus
Aguirre, R.; Kasche, V.
Catalytically active monomer forms of immobilized arginase
Eur. J. Biochem.
130
373-381
1983
Rattus norvegicus
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
Fuentes, J.M.; Campo, M.L.; Soler, G.
Physico-chemical properties of hepatocyte plasma-membrane-bound arginase
Arch. Int. Physiol. Biochim. Biophys.
99
413-417
1991
Rattus norvegicus
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
Han, S.; Moore, R.A.; Viola, R.E.
Synthesis and evaluation of alternative substrates for arginase
Bioorg. Chem.
30
81-94
2002
Rattus norvegicus
Lavulo, L.T.; Sossong, T.M., Jr.; Brigham-Burke, M.R.; Doyle, M.L.; Cox, J.D.; Christianson, D.W.; Ash, D.E.
Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid
J. Biol. Chem.
276
14242-14248
2001
Rattus norvegicus
Tormanen, C.D.
Allosteric inhibition of rat liver and kidney arginase by copper and mercury ions
J. Enzyme Inhib.
16
443-449
2001
Rattus norvegicus
Reisser, D.; Onier-Cherix, N.; Jeannin, J.F.
Arginase activity is inhibited by L-NAME, both in vitro and in vivo
J. Enzyme Inhib. Med. Chem.
17
267-270
2002
Rattus norvegicus
Tormanen, C.D.
Substrate inhibition of rat liver and kidney arginase with fluoride
J. Inorg. Biochem.
93
243-246
2003
Rattus norvegicus
Colleluori, D.M.; Reczkowski, R.S.; Emig, F.A.; Cama, E.; Cox, J.D.; Scolnick, L.R.; Compher, K.; Jude, K.; Han, S.; Viola, R.E.; Christianson, D.W.; Ash, D.E.
Probing the role of the hyper-reactive histidine residue of arginase
Arch. Biochem. Biophys.
444
15-26
2005
Rattus norvegicus
Busnel, O.; Carreaux, F.; Carboni, B.; Pethe, S.; Goff, S.V.; Mansuy, D.; Boucher, J.L.
Synthesis and evaluation of new omega-borono-alpha-amino acids as rat liver arginase inhibitors
Bioorg. Med. Chem.
13
2373-2379
2005
Rattus norvegicus (P07824)
Shin, H.; Cama, E.; Christianson, D.W.
Design of amino acid aldehydes as transition-state analogue inhibitors of arginase
J. Am. Chem. Soc.
126
10278-10284
2004
Rattus norvegicus
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
Tormanen, C.D.
Inhibition of rat liver and kidney arginase by cadmium ion
J. Enzyme Inhib. Med. Chem.
21
119-123
2006
Rattus norvegicus
Hirata, M.; Obayashi, S.; Sakamoto, S.; Aso, T.; Imamura, M.; Azuma, H.
Involvement of arginase in regulating myometrial contractions during gestation in the rat
Mol. Hum. Reprod.
12
513-518
2006
Rattus norvegicus
Lerzynski, G.; Suschek, C.V.; Kolb-Bachofen, V.
In hepatocytes the regulation of NOS-2 activity at physiological L-arginine levels suggests a close link to the urea cycle
Nitric Oxide
14
300-308
2006
Rattus norvegicus (P07824)
Steppan, J.; Ryoo, S.; Schuleri, K.H.; Gregg, C.; Hasan, R.K.; White, A.R.; Bugaj, L.J.; Khan, M.; Santhanam, L.; Nyhan, D.; Shoukas, A.A.; Hare, J.M.; Berkowitz, D.E.
Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism
Proc. Natl. Acad. Sci. USA
103
4759-4764
2006
Rattus norvegicus
Holan, V.; Pindjakova, J.; Krulova, M.; Neuwirth, A.; Fric, J.; Zajicova, A.
Production of nitric oxide during graft rejection is regulated by the Th1/Th2 balance, the arginase activity, and L-arginine metabolism
Transplantation
81
1708-1715
2006
Rattus norvegicus
Schnorr, O.; Brossette, T.; Momma, T.Y.; Kleinbongard, P.; Keen, C.L.; Schroeter, H.; Sies, H.
Cocoa flavanols lower vascular arginase activity in human endothelial cells in vitro and in erythrocytes in vivo
Arch. Biochem. Biophys.
476
211-215
2008
Homo sapiens, Rattus norvegicus
Matthiesen, S.; Lindemann, D.; Warnken, M.; Juergens, U.R.; Racke, K.
Inhibition of NADPH oxidase by apocynin inhibits lipopolysaccharide (LPS) induced up-regulation of arginase in rat alveolar macrophages
Eur. J. Pharmacol.
579
403-410
2008
Rattus norvegicus
Demougeot, C.; Prigent-Tessier, A.; Bagnost, T.; Andre, C.; Guillaume, Y.; Bouhaddi, M.; Marie, C.; Berthelot, A.
Time course of vascular arginase expression and activity in spontaneously hypertensive rats
Life Sci.
80
1128-1134
2007
Rattus norvegicus
Belik, J.; Shehnaz, D.; Pan, J.; Grasemann, H.
Developmental changes in arginase expression and activity in the lung
Am. J. Physiol. Lung Cell Mol. Physiol.
294
L498-L504
2008
Rattus norvegicus (O08701), Rattus norvegicus (P07824)
Shishova, E.Y.; Di Costanzo, L.; Emig, F.A.; Ash, D.E.; Christianson, D.W.
Probing the specificity determinants of amino acid recognition by arginase
Biochemistry
48
121-131
2009
Homo sapiens, Rattus norvegicus (P07824)
Dowling, D.P.; Di Costanzo, L.; Gennadios, H.A.; Christianson, D.W.
Evolution of the arginase fold and functional diversity
Cell. Mol. Life Sci.
65
2039-2055
2008
Homo sapiens (P05089), Homo sapiens (P78540), Rattus norvegicus (P07824)
Leopoldini, M.; Russo, N.; Toscano, M.
Determination of the catalytic pathway of a manganese arginase enzyme through density functional investigation
Chemistry
15
8026-8036
2009
Rattus norvegicus
Venkatakrishnan, P.; Nakayasu, E.S.; Almeida, I.C.; Miller, R.T.
Arginase activity in mitochondria - an interfering factor in nitric oxide synthase activity assays
Biochem. Biophys. Res. Commun.
394
448-452
2010
Rattus norvegicus
Agunloye, O.M.; Oboh, G.; Ademiluyi, A.O.; Ademosun, A.O.; Akindahunsi, A.A.; Oyagbemi, A.A.; Omobowale, T.O.; Ajibade, T.O.; Adedapo, A.A.
Cardio-protective and antioxidant properties of caffeic acid and chlorogenic acid Mechanistic role of angiotensin converting enzyme, cholinesterase and arginase activities in cyclosporine induced hypertensive rats
Biomed. Pharmacother.
109
450-458
2019
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 3.5.3.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
