3.5.3.1: arginase
This is an abbreviated version!
For detailed information about arginase, go to the full flat file.
Word Map on EC 3.5.3.1
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3.5.3.1
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endothelial
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tnf
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polyamines
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myeloid-derived
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necrosis
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myeloid
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monocyte
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arterial
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lps
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lipopolysaccharide
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peritoneal
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l-ornithine
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mdscs
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pulmonary
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microglia
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ammonia
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t-cells
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argininosuccinate
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airway
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leishmania
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hypertension
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asthma
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putrescine
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immunotherapy
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marrow-derived
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tumor-associated
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leishmaniasis
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transcarbamylase
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vasodilation
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neuroinflammation
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l-citrulline
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dimethylarginine
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interleukin-10
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tregs
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l-name
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endothelium-dependent
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urease
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agmatine
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m2-like
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hyperammonemia
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no-dependent
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amazonensis
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erectile
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no-synthase
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medicine
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dimethylaminohydrolase
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ng-monomethyl-l-arginine
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bmdms
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carbamoylphosphate
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il-4-induced
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analysis
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synthesis
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pharmacology
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food industry
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drug development
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nutrition
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phosphodiesterase-5
- 3.5.3.1
- endothelial
- tnf
- polyamines
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myeloid-derived
- necrosis
- myeloid
- monocyte
- arterial
- lps
- lipopolysaccharide
- peritoneal
- l-ornithine
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mdscs
- pulmonary
- microglia
- ammonia
- t-cells
- argininosuccinate
- airway
- leishmania
- hypertension
- asthma
- putrescine
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immunotherapy
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marrow-derived
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tumor-associated
- leishmaniasis
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transcarbamylase
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vasodilation
-
neuroinflammation
- l-citrulline
- dimethylarginine
- interleukin-10
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tregs
-
l-name
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endothelium-dependent
- urease
- agmatine
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m2-like
- hyperammonemia
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no-dependent
- amazonensis
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erectile
- no-synthase
- medicine
-
dimethylaminohydrolase
- ng-monomethyl-l-arginine
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bmdms
- carbamoylphosphate
-
il-4-induced
- analysis
- synthesis
- pharmacology
- food industry
- drug development
- nutrition
- phosphodiesterase-5
Reaction
Synonyms
ARG, Arg I, Arg II, ARG1, ARG2, ARGAH1, ARGAH2, ArgI, arginase, arginase 1, arginase 1a, arginase 1b, arginase 2a, arginase 2b, arginase I, arginase II, arginase type I, arginase-1, arginase-2, arginase1, arginine amidinase, arginine amidohydrolase-1, arginine amidohydrolase-2, arginine transamidinase, canavanase, human arginase type I, Kidney-type arginase, L-arginase, L-arginine amidino hydrolase, L-arginine amidinohydrolase, L-arginine amidohydrolase, L-arginine ureahydrolase, Liver-type arginase, mitochondrial arginase, More, Non-hepatic arginase, PMN arginase, recombinant human arginase I, rhArg-PEG, rhArg1, RocF, serum arginase, SmARG, tissue arginase, type II arginase
ECTree
3.5.3.1 arginaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.5.3.1 - arginase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(2S)-2-amino-5-(1H-imidazol-2-ylamino)pentanoic acid
2-aminoimidazole amino acid inhibitor in which the 2-aminoimidazole moiety serves as a guanidine mimetic
(DL)-2-amino-6-borono-2-[1-(3,4-dichlorobenzyl)piperidin-4-yl]-hexanoic acid
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(R)-2-amino-6-borono-2-[1-(3,4-dichlorobenzyl)piperidin-4-yl]-hexanoic acid
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(R)-2-amino-6-borono-2[1-(3,4-dichlorobenzyl)piperidin-4-yl]hexanoic acid
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(S)-(2-boronoethyl)-L-cysteine
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boronic acid-based transition state analogue, classical competitive inhibition at pH 7.5, slow-binding inhibition at pH 9.5
2-(5-methyl-2-(trifluoromethyl)-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)hydrazinecarbothioamide
non-competitive inhibitor, 79% inhibition at 1 mM
2-(S)-amino-5-(2-aminoimidazol-1-yl)pentanoic acid
2-aminoimidazole amino acid inhibitor in which the 2-aminoimidazole moiety serves as a guanidine mimetic
2-mercaptopropionate
5 mM, isoform LeARG1, 38% residual activity, LeARG2, 38% residual activity; 5 mM, isoform LeARG1, 38% residual activity, LeARG2, 38% residual activity
3-Mercaptopropionate
5 mM, isoform LeARG1, 24% residual activity, LeARG2, 26% residual activity; 5 mM, isoform LeARG1, 24% residual activity, LeARG2, 26% residual activity
5,5'-dithiobis (2-nitrobenzoic acid)
1 mM, 23% loss of activity
5-methyl-2-(trifluoromethyl)-N-[3-(trifluoromethyl)-1H-1,2,4-triazol-5-yl][1,2,4]triazolo[1,5-a]pyrimidin-7-amine
57% inhibition at 1 mM
5-methyl-7-(1H-1,2,4-triazol-1-yl)-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidine
47% inhibition at 1 mM
5-methyl-7-(1H-pyrrol-1-yl)-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidine
38% inhibition at 1 mM
5-methyl-7-(4-trifluoromethylphenylamine)-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidine
52% inhibition at 1 mM
5-methyl-7-(pyrrolidin-1-yl)-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidine
10% inhibition at 1 mM
5-methyl-N-(naphthalen-2-yl)-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
29% inhibition at 1 mM
5-methyl-N-phenyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
1% inhibition at 1 mM
7-(4-chlorophenylamine)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidine
42% inhibition at 1 mM
Chloroquine
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inhibits arginase in a dose-dependent manner, and displays a linear competitive inhibition on sickle erythrocyte arginase
fluoride
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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
homoarginine
at 2 mM arginine, 18% and 94% inhibition of arginase 2 is observed by homoarginine at the concentration of 1 and 10 mM. At 0.1 mM arginine, the conversion of arginine to ornithine by arginase 2 is inhibited by 47% and 88% in the presence of 1 mM and 10 mM homoarginine. No significant inhibition of arginase 2 is observed at physiological homoarginine concentrations; at Km concentration (3 mM) of the substrate arginine, 1 mM homoarginine inhibits arginase 1 activity by 14%, whereas a concentration of 10 mM results in 50% inhibition of the enzyme. At 0.1 mM arginine, arginase 1 inhibition by 1 mM and 10 mM homoarginine is 30% and 76%, respectively. No significant inhibitory effects of arginase 1 activity are observed with physiological concentrations of homoarginine, 0.001-0.01 mM
L-norvaline
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blocks arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
Mercaptoacetate
5 mM, isoform LeARG1, 28% residual activity, LeARG2, 26% residual activity; 5 mM, isoform LeARG1, 28% residual activity, LeARG2, 26% residual activity
Mn2+
the rate of arginase 1-mediated ornithine formation from L-arginine is 20% higher in absence of Mn2+ supplementation; the rate of arginase 1-mediated ornithine formation from L-arginine is 20% higher in absence of Mn2+ supplementation
N-(2,6-difluorophenyl)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
8% inhibition at 1 mM
N-(3,4-dichlorophenyl)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
3% inhibition at 1 mM
N-(3,5-dichlorophenyl)-2,5-bis(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
47% inhibition at 1 mM
N-(3,5-dichlorophenyl)-2,5-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
23% inhibition at 1 mM
N-(3,5-dichlorophenyl)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
71% inhibition at 1 mM
N-(3,5-dimethoxyphenyl)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
39% inhibition at 1 mM
N-(3-chlorophenyl)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
51% inhibition at 1 mM
N-(4-methoxyphenyl)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
5% inhibition at 1 mM
Nomega-nitro-L-arginine methyl ester
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i.e. L-NAME, inhibition of enzyme from liver and colon cancer cells in vitro and in vivo
PEG-SOD
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polyethylene glycol, covalently linked to superoxide dismutase. Significantly inhibits the arginase activity induced by cysteine-iron, indicating that oxygen species may be responsible in part for the observed increase in arginase activity
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Polymyxin B
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blocks arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
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
spermidine
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inhibition in a dose-dependent fashion below 5 mM and above 25 mM
Woodward's reagent K
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complete inactivation, reactivation by 0.5 M hydroxylamine. Reactivated enzyme can be inactivated again
(-)-epicatechin
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(-)-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
(-)-epicatechin
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(-)-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
(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
(2S)-2-amino-3-(2-amino-1H-imidazol-5-yl)propanoic acid
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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
2(S)-amino-6-boronohexanoic acid
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boronic acid-based transition state analogue, classical competitive inhibition at pH 7.5, slow-binding inhibition at pH 9.5
2(S)-amino-6-boronohexanoic acid
Kd-value 5 nM, complete inhibition of enzyme in cytoplasmic extracts of myeloid suppressor cells by 0.05 mM
2(S)-amino-6-boronohexanoic acid
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transition state analogue inhibitor, effect on female and male hemodynamics, overview
Ag+
20.41% residual activity at 1 mM; 20.41% residual activity at 1 mM
Ca2+
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inhibitory to enzymic activity in presence of Mn2+, enhances lectin function of enzyme
Ca2+
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inhibitory to enzymic activity in presence of Mn2+, enhances lectin function of enzyme
caffeic acid
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inhibiting arginase activity by caffeic acid and chlorogenic acid might be a possible mechanism by which they exert their cardio-protective effect
Cd2+
58.78% residual activity at 1 mM; 58.78% residual activity at 1 mM
Cd2+
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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+
chlorogenic acid
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inhibiting arginase activity by caffeic acid and chlorogenic acid might be a possible mechanism by which they exert their cardio-protective effect
Cu2+
30.2% residual activity at 1 mM; 30.2% residual activity at 1 mM
Cu2+
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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
diethyl dicarbonate
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causes a loss in ability of Mn2+ to reactivate inactive subunits of wild-type and mutant enzyme H141F, effect is reversed by hydroxylamine
diethyl dicarbonate
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second-order rate constant of 113 per M and s for inactivation process. L-ornithine partially protects, L-ornithine plus borate completely protect
dithiothreitol
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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+
EDTA
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after dialysis against EDTA and assay in the absence of Mn2+, the wild type enzyme exhibits 50% activity
EDTA
in contrast with R308A, the monomeric E256Q variant of the human enzyme is totally inactivated by dialysis in the presence of EDTA, leading to the suggestion that the quaternary structure could play a role in the affinity of metal binding to arginase
Fe2+
77.14% residual activity at 1 mM; 77.14% residual activity at 1 mM
Fe3+
77.14% residual activity at 1 mM; 77.14% residual activity at 1 mM
flavanol-rich cocoa
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cocoa flavanols lower arginase-2 mRNA expression and activity
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flavanol-rich cocoa
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cocoa flavanols lower arginase-2 mRNA expression and activity
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Hg2+
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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
L-ornithine
mixed type inhibition; mixed type inhibition
lysine
at 2 mM arginine, 42% and 67% inhibition of arginase 2 is observed by lasine at 1 mM and 10 mM. At 0.1 mM arginine, the conversion of arginine to ornithine by arginase 2 is inhibited by 44% and 88% in the presence of 1 mM and 10 mM lysine. No significant inhibition of arginase 2 is observed at physiological lysine concentrations; at concentrations of 1 and 10 mM, 39% and 78% inhibition of arginase 1 activity at Km concentration (3 mM) of the substrate arginine, and 44% and 81% inhibition at physiological arginine concentrations. No significant inhibitory effects of arginase 1 activity are observed with physiological concentrations of lysine, 0.1-1.0 mM
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
Nomega-hydroxy-L-arginine
mixed type inhibition; mixed type inhibition
Nomega-hydroxy-L-arginine
i.e. NOHA, binds to isoform arginase I with Kd of 3.6 microM
Nomega-hydroxy-L-arginine
0.2 mM, isoform LeARG1, 7% residual activity, LeARG2, 5% residual activity; 0.2 mM, isoform LeARG1, 7% residual activity, LeARG2, 5% residual activity
Nomega-hydroxy-nor-L-arginine
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in unstimulated HUVEC cells, dose-dependent reduction of enzyme activity, maximum inhibition at 0.02 mM. In cells stimulated by thrombin with or without extracellular L-arginine, stimulation of NO synthase and NO release, with significant reduction of enzyme activity
Nomega-hydroxy-nor-L-arginine
i.e. nor-NOHA, binds to isoform arginase I with Kd of 517 nM, surface plasmon resonance, or Kd of 50 nM, isothermal titration calorimetry
S-(2-boronoethyl)-L-cysteine
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inhibition results in in reduced fractional shortening, maximal rate of shortening, and relengthening of myocyte contractions
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
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inhibition results in augmented Ca2+-dependent NO synthase activity and NO production in isolated myocytes
Zn2+
33.47% residual activity at 1 mM; 33.47% residual activity at 1 mM
additional information
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combined polyethylene glycol, covalently linked to superoxide dismutase with a highly stable PEG-catalase, further decrease of arginase activity is observed; salicylic acid derivatives potently inhibited arginase activity. More significant inhibition of arginase activity in purified arginase-1 than in erythrocyte hemolysate, possibly due to the presence of increased extraneous macromolecular interactions in cell hemolysate than in purified enzyme
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additional information
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binding to lectins is inhibitory to enzymic activity, which is recovered after desorption of the lectin with alpha-D-galactose
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additional information
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ornithine is a poor inhibitor of isozyme type II, isozyme selectivity in binding and substrate, products, and inhibitors
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additional information
arginase activity functionally inhibits nitric oxide synthase by depleting the substrate pool of L-arginine, and nitric oxide synthase activity potentially inhibits arginase by generating and releasing small amounts of the intermediate N-hydroxy-L-arginine, a competitive inhibitor of arginase, and also by generating nitric oxide itself, which can nitrosylate cysteine residues of human arginase I to modulate its activity; arginase activity functionally inhibits nitric oxide synthase by depleting the substrate pool of L-arginine, and nitric oxide synthase activity potentially inhibits arginase by generating and releasing small amounts of the intermediate N-hydroxy-L-arginine, a competitive inhibitor of arginase, and also by generating nitric oxide itself, which can nitrosylate cysteine residues of human arginase I to modulate its activity
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additional information
arginase activity functionally inhibits nitric oxide synthase by depleting the substrate pool of L-arginine, and nitric oxide synthase activity potentially inhibits arginase by generating and releasing small amounts of the intermediate N-hydroxy-L-arginine, a competitive inhibitor of arginase, and also by generating nitric oxide itself, which can nitrosylate cysteine residues of human arginase I to modulate its activity; arginase activity functionally inhibits nitric oxide synthase by depleting the substrate pool of L-arginine, and nitric oxide synthase activity potentially inhibits arginase by generating and releasing small amounts of the intermediate N-hydroxy-L-arginine, a competitive inhibitor of arginase, and also by generating nitric oxide itself, which can nitrosylate cysteine residues of human arginase I to modulate its activity
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additional information
arginase inhibition is unlikely to play a significant role in the cardio-protective effects of homoarginine; arginase inhibition is unlikely to play a significant role in the cardio-protective effects of homoarginine
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additional information
arginase inhibition is unlikely to play a significant role in the cardio-protective effects of homoarginine; arginase inhibition is unlikely to play a significant role in the cardio-protective effects of homoarginine
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additional information
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arginase inhibition is unlikely to play a significant role in the cardio-protective effects of homoarginine; arginase inhibition is unlikely to play a significant role in the cardio-protective effects of homoarginine
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additional information
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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; DL-norvaline does not block arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
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additional information
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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
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additional information
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isothiourea homologues undergo rapid non-enzymic rearrangement to probably give inhibitory compouds, overview
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additional information
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effect of preincubation of the isozymes with metal ions, overview
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additional information
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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
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additional information
L-lysine and diaminopimelic acid failed to block SmARG activity
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additional information
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L-lysine and diaminopimelic acid failed to block SmARG activity
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additional information
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binding to lectins is inhibitory to enzymic activity, which is recovered after desorption of the lectin with alpha-D-galactose
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