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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
-
-
-
-
?
agmatine + H2O
1,4-diaminobutane + urea
argininic acid + H2O
urea + 5-amino-2-hydroxypentanoate
-
-
-
-
?
canavanine + H2O
urea + NH2OCH2CH2CH(NH2)COOH
D-arginine + H2O
D-ornithine + urea
isoform LeARG1, 2.2% of the activity with L-arginine, LeARG2, 3.6% of the activity with L-arginine
-
-
?
L-Arg + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
?
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
L-canavanine + H2O
L-canaline + urea
-
-
-
-
?
L-homoarginine + H2O
L-2,6-diaminohexanoate + urea
isoform LeARG1, 14% of the activity with L-arginine, LeARG2, 13% of the activity with L-arginine
-
-
?
L-phenylalanine + H2O
2-oxo-3-phenylpropanoate + NH3
L-thioarginine + H2O
(2S)-2-amino-5-mercaptopentanoate + urea
-
-
-
-
?
p-nitrophenyl glyoxal + arginine
?
-
-
-
-
?
S-(4-aminobutyl)isothiourea + H2O
?
-
-
-
-
?
thioguanidino-valeric acid + H2O
?
-
-
-
-
?
additional information
?
-
agmatine + H2O
1,4-diaminobutane + urea
-
for wild-type, no substrate. Hydrolysis by mutant N149D
-
-
?
agmatine + H2O
1,4-diaminobutane + urea
isoform LeARG1, 0.5% of the activity with L-arginine, LeARG2, 0.6% of the activity with L-arginine
-
-
?
agmatine + H2O
1,4-diaminobutane + urea
Vigna catjang
-
16% of the activity with L-arginine
-
-
?
canavanine + H2O
urea + NH2OCH2CH2CH(NH2)COOH
-
-
-
-
?
canavanine + H2O
urea + NH2OCH2CH2CH(NH2)COOH
-
9.6% of the activity with L-arginine
-
-
?
canavanine + H2O
urea + NH2OCH2CH2CH(NH2)COOH
Glycine hispida
-
-
-
-
?
canavanine + H2O
urea + NH2OCH2CH2CH(NH2)COOH
-
-
-
-
?
canavanine + H2O
urea + NH2OCH2CH2CH(NH2)COOH
Vigna catjang
-
12.7% of the activity with L-arginine
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
the enzyme involved in urea cycle
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
the enzyme does not hydrolyse D-arginine and other arginine analogues (L-agmatine, L-canavanine, L-argininamide and L-homoarginine)
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
the enzyme catalyses the catabolism of L-arginine to L-ornithine and urea
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
the biosynthesis yield of L-ornithine by the purified enzyme is 36.9 g/l, and the molar yield is 97.2%
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
the biosynthesis yield of L-ornithine by the purified enzyme is 36.9 g/l, and the molar yield is 97.2%
-
-
?
L-arginine + H2O
L-ornithine + urea
Glycine hispida
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
enzyme is involved in acid resistance and inhibits host nitric oxide production
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
enzyme is involved in acid resistance and inhibits host nitric oxide production
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
654333, 654346, 668556, 685856, 686308, 686646, 687312, 696307, 697070, 697084, 699351, 735115 -
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
ir
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
enzyme is involved in net production of ornithine, a precursor of polyamines, glutamate, and proline, enzyme is also involved in regulation of nitric oxide biosynthesis by modulating arginine availability for nitric oxide synthase
-
-
?
L-arginine + H2O
L-ornithine + urea
-
enzyme is involved in regulating L-arginine bioavailability to NO synthase in human penile corpus cavernosum smooth muscle, and in clitoral corpus cavernosum and vagina, enzyme plays a role in both female and male sexual arousal
-
-
ir
L-arginine + H2O
L-ornithine + urea
-
enzyme is involved in regulation of nitric oxide biosynthesis by modulating arginine availability for nitric oxide synthase
-
-
?
L-arginine + H2O
L-ornithine + urea
-
reaction intermediate is Nomega-hydroxy-L-arginine
-
-
?
L-arginine + H2O
L-ornithine + urea
-
arginase competes with nitric oxide synthases for L-arginine as the common substrate
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
arginase catalyzes the first committed step in the biosynthesis of polyamines
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
assay at pH 7.4, 37°C
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
ir
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
Pista pacifica
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + 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
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
mechanism of positive cooperativity. The kinetic characterization of arginase from yeast crude extract indicates that both fermentation temperature and timing clearly affect enzymatic activity, which gradually increases after the inoculum, reaching the highest Vmax value when yeast assimilable nitrogen is nearly completely exhausted and the arginine added to the semi-synthetic grape juice is significantly consumed (approximately 40-50% of its initial level). Yeast arginase shows the best catalytic properties when alcoholic fermentation occurrs at 20°C approximately 3 days after the inoculum
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
Vigna catjang
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-arginine + H2O
L-ornithine + urea
-
-
-
?
L-phenylalanine + H2O
2-oxo-3-phenylpropanoate + NH3
-
-
-
-
?
L-phenylalanine + H2O
2-oxo-3-phenylpropanoate + NH3
-
-
-
-
?
additional information
?
-
-
no substrate: agmatine, D-arginine, L-homoarginine, L-argininic acid, gamma-guanidinobutyric acid, beta-guanidinopropionic acid, streptomycin
-
-
?
additional information
?
-
-
isozyme selectivity in binding and substrate, products, and inhibitors
-
-
?
additional information
?
-
-
presence of arginine pools, which are accessible to NO synthase and enzyme, but not exchangeable
-
-
?
additional information
?
-
-
the wild type enzyme does not hydrolyze 1-amino-4-guanidinobutane (agmatine)
-
-
?
additional information
?
-
-
complex regulation of natural killer cell functions by arginine availability
-
-
?
additional information
?
-
hereditary defects in arginase compromise structure and catalysis, which results in an accumulation of arginine in the blood known as hyperarginemia. Arginase deficiency can also result in the accumulation of nitrogen in the form of ammonia, which results in hyperammonemia
-
-
?
additional information
?
-
hereditary defects in arginase compromise structure and catalysis, which results in an accumulation of arginine in the blood known as hyperarginemia. Arginase deficiency can also result in the accumulation of nitrogen in the form of ammonia, which results in hyperammonemia
-
-
?
additional information
?
-
-
recombinant human arginase I (rhArg-PEG), an arginine-depleting enzyme, can inhibit the growth of arginine-dependent tumors
-
-
?
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
-
-
?
additional information
?
-
-
enzyme may be involved in cellular proliferation in atherosclerosis, inhibiton of enzyme expression by 17beta-estradiol as mechanism in attenuating atherogenensis
-
-
?
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)
-
-
?
additional information
?
-
infection of mice with Schistosoma mansoni cercariae elevates arginase activity
-
-
?
additional information
?
-
-
infection of mice with Schistosoma mansoni cercariae elevates arginase activity
-
-
?
additional information
?
-
Vigna catjang
-
no substrate: D-arginine, L-homoarginine, L-argininic acid, gamma-guanidinobutyric acid, beta-guanidinopropionic acid, streptomycin
-
-
?
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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
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
Fe
-
cysteine-iron promotes arginase activity
Fe3+
-
the enzyme retains 38.7% of its original activity after dialysis. In the presence of Mn2+ as a cofactor, the enzyme regains 95% of its initial activity
Guanidinium chloride
the single mutant R308A changes to a trimeric and kinetically cooperative form, whereas the other enzyme variants are not altered
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
Magnesium
stabilizes the protein. In the absence of Mg2+, a complete loss of secondary structure is observed for certain elements
Manganese
the more deeply buried Mn2+ ion A is coordinated by residues His193, Asp216, Asp220 and Asp323. The second metal, Mn2+B is co-ordinated by His218, Asp216, Asp323, Asp325
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
Ca2+
-
60% of the activation as compared to Mn2+
Ca2+
-
52% of the activity with Mn2+
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
Ca2+
Vigna catjang
-
35% of the activity with Mn2+
Co2+
-
displays remarkable activity in the absence of exogenous metals, although manganese, cobalt, and nickel all improve activity. Enzyme shifts its metal preference from Ni, Co,and Mn (decreasing order) when assayed at pH 6 to Ni, Mn, and Co (decreasing order) at pH 9
Co2+
-
45% of the activity with Mn2+
Co2+
-
the enzyme retains 38.7% of its original activity after dialysis. In the presence of Mn2+ as a cofactor, the enzyme regains 95% of its initial activity
Co2+
-
0.5 mM, 43% of the activity compared to activity with Mn2+
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
Co2+
enhances the activity
Co2+
-
required, activates, best metal cofactor
Co2+
-
enzyme is optimally active with cobalt at pH 6
Co2+
-
enzyme is selective for Co2+
Co2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
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+
Co2+
effective activator, 144% activity at 1 mM
Co2+
-
activates isozyme II 1.46fold, no activation of isozyme I
Co2+
Vigna catjang
-
66% of the activity with Mn2+
Fe2+
-
slight activation
Fe2+
Vigna catjang
-
52% of the activity with Mn2+
Mg2+
-
90% of the activation as compared to Mn2+
Mg2+
-
93% of the activity with Mn2+
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
Mg2+
Vigna catjang
-
61% of the activity with Mn2+
Mn2+
-
displays remarkable activity in the absence of exogenous metals, although manganese, cobalt, and nickel all improve activity. Enzyme shifts its metal preference from Ni, Co,and Mn (decreasing order) when assayed at pH 6 to Ni, Mn, and Co (decreasing order) at pH 9
Mn2+
-
acts as co-factor and as activator
Mn2+
-
metalloenzyme binding 4 mol Mn2+ per mol enzyme
Mn2+
-
3fold increase in Vmax-value in presence of 0.1 mM Mn2+
Mn2+
-
exogenous addition of Mn2+ results in increased sensitivity to inhibitor sodium fluoride
Mn2+
-
maximal activity at 2.0 mM
Mn2+
-
maximum activity at 0.1 mM, presence of Mn2+ results in increase in Vmax, and a higher sensitivity to product and L-lysine inhibition, with no change in KM-value for L-arginine
Mn2+
-
full activation after preincubation for 20 min at 55°C with 2 mM Mn2+
Mn2+
-
the enzyme retains 38.7% of its original activity after dialysis. In the presence of Mn2+ as a cofactor, the enzyme regains 96% of its initial activity
Mn2+
-
maximum activity (100%) with 1 mM Mn2+. 0.5mM of Mn2+ exhibits 70% of total activity
Mn2+
two Mn2+ ions are required for the enzyme to be fully functional
Mn2+
-
required for catalysis, enhances lectin function of enzyme
Mn2+
optimum metal cofactor. The optimal concentration of Mn2+ is approximately 2 mM. When the concentration is higher than 2 mM, there is a slight drop in relative activity. The active site of L-arginase contains two Mn2+ ions (Mn2+A and Mn2+B), which are coordinated by Asp and His residues. When Mn2+ concentration increases from 0 to 10 mM, the ellipticity of L-arginase at 208 nm and 222 nm increases accordingly. The percentage of helix increases to 66% in the presence of 10 mM Mn2+. This suggests that the addition of Mn2+ can affect the structure of L-arginase by increasing the helix content of the enzyme
Mn2+
-
activates slightly, 14.6% of the activity with Co2+
Mn2+
-
15-20% of the activity with Co2+
Mn2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
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+
Mn2+
effective activator, 207% activity at 1 mM
Mn2+
-
essentiell for activity
Mn2+
-
activates, role of weakly and tightly bound metal ions in wild-type and mutant enzymes, metal content, overview
Mn2+
-
manganese-metalloenzyme, binuclear cluster, binding structure
Mn2+
-
activation. after dialysis with EDTA, wild-type and mutant H145N contain 1.1 and 1.3 Mn2+ per subunit, resp., and are hlaf-.active. Mutant H120N contains less than 0.1 Mn2+ per subunit and is inactive
Mn2+
manganese metalloenzyme, each monomer contains two manganese ions
Mn2+
-
binuclear manganese metalloenzyme
Mn2+
increase in enzyme activity by incubation with 5 mM Mn2+ for 10 min at 60°C
Mn2+
manganese metalloenzyme
Mn2+
-
a manganese wash at room temperature is the best condition to purify active enzyme, activity in the presence of 10 mM Mn2+ is at least 15fold higher than in the absence of Mn2+
Mn2+
binuclear manganese metalloenzyme
Mn2+
Pista pacifica
-
activating
Mn2+
-
no effect on rat kidney enzyme
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+
binuclear manganese metalloenzyme
Mn2+
manganese metalloenzyme, Mn2+-Mn2+ cluster in the active site of each monomer
Mn2+
Vigna catjang
-
maximal activity at 0.6 mM
Mn2+
Vigna catjang
-
full activation after preincubation for 8 min at 35°C with 0.6 mM Mn2+
Mn2+
-
required for catalysis, enhances lectin function of enzyme
Mn2+
-
binds one Mn atom per subunit
Mn2+
all recombinant variants are active even in the absence of added Mn2+ but express about2.5-fold increased activity in the presence of 2 mM Mn2+. After extensive dialysis against 25 mM EDTA, they became totally dependent on added Mn2+ for catalytic activity. The manganese-reactivation of all fully inactivated species followed hyperbolic kinetics
Ni2+
-
optimal arginase activity occurrs with nickel at an alkaline pH
Ni2+
-
51% of the activity with Mn2+
Ni2+
-
1 mM, 15% of the activity compared to activity with Mn2+
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
Ni2+
enhances the activity
Ni2+
-
activates slightly, 6.1% of the activity with Co2+
Ni2+
-
6-30% of the activity with Co2+
Ni2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
Ni2+
Vigna catjang
-
55% of the activity with Mn2+
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
Zn2+
Vigna catjang
-
38% of the activity with Mn2+
additional information
-
Fe2+, Ca2+, Mg2+, Zn2+, Cu2+ have no effect on enzyme activity
additional information
-
no activity with Fe2+, Zn2+
additional information
-
metalloenzyme, a metal ion is absolutely required for activity, no activation with Zn2+, Cu2+, Fe2+, Ca2+, and Mg2+
additional information
Ca2+, Na+, K+, Mg2+, and Ni2+ do not show any significant effect on enzyme activity
additional information
Ca2+, Na+, K+, Mg2+, and Ni2+ do not show any significant effect on enzyme activity
additional information
-
Ca2+, Na+, K+, Mg2+, and Ni2+ do not show any significant effect on enzyme activity
additional information
pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I shows that several metal binding ligands are actually quite tolerant to amino acid substitutions. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution
additional information
-
pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I shows that several metal binding ligands are actually quite tolerant to amino acid substitutions. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution
additional information
-
isozymes are not affected by Mg2+ and Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-2-amino-3-(2-amino-1H-imidazol-5-yl)propanoic acid
(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
(2S,5E)-2-amino-7-oxohept-5-enoic acid
-
-
(DL)-2-amino-6-borono-2-[1-(3,4-dichlorobenzyl)piperidin-4-yl]-hexanoic acid
-
(R)-2-amino-6-borono-2-[1-(3,4-dichlorobenzyl)piperidin-4-yl]-hexanoic acid
-
(R)-2-amino-6-borono-2-[2-(piperidin-1-yl)ethyl]hexanoic acid
(R)-2-amino-6-borono-2[1-(3,4-dichlorobenzyl)piperidin-4-yl]hexanoic acid
-
(S)-(2-boronoethyl)-L-cysteine
-
boronic acid-based transition state analogue, classical competitive inhibition at pH 7.5, slow-binding inhibition at pH 9.5
(S)-2-amino-6-borono-2-[2-(piperidin-1-yl)ethyl]hexanoic acid
-
(S)-2-amino-7-oxoheptanoic acid
2(S)-amino-6-boronohexanoic acid
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-(aminomethyl)-6-borononorleucine
-
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-(S)-amino-6-boronohexanoic acid
2-amino-6-borono-2-(difluoromethyl)-hexanoic acid
-
2-amino-6-borono-2-butylhexanoic acid
-
2-amino-6-borono-2-methyl-hexanoic acid
-
2-amino-6-boronohexanoic acid
2-mercaptopropionate
5 mM, isoform LeARG1, 38% residual activity, LeARG2, 38% residual activity; 5 mM, isoform LeARG1, 38% residual activity, LeARG2, 38% residual activity
2-[(benzylamino)methyl]-6-borononorleucine
-
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
6-borono-2-(2-hydroxyethyl)norleucine
-
6-borono-2-(3-methoxypropyl)norleucine
-
6-borono-2-(hydroxymethyl)norleucine
-
6-borono-2-ethylnorleucine
-
6-borono-2-methylnorleucine
-
6-borono-2-propan-2-ylnorleucine
-
6-borono-2-[2-(4-hydroxypiperidin-1-yl)ethyl]norleucine
-
6-borono-2-[2-(diethylamino)ethyl]norleucine
-
6-borono-2-[2-(morpholin-4-yl)ethyl]norleucine
-
6-borono-2-[2-(pyrrolidin-1-yl)ethyl]norleucine
-
7-(4-chlorophenylamine)-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidine
42% inhibition at 1 mM
Al3+
-
no inhibition of isozyme I, 33% inhibition of isozyme II
alpha-(4-boronobutyl)histidine
-
alpha-(4-boronobutyl)phenylalanine
-
apigenin 7-O-beta-D-glucoside
0.1 mM, about 40% inhibition
asymmetric dimethylarginine
poor arginase 1 inhibitor
catechin
0.1 mM, about 40% inhibition
Chloroquine
-
inhibits arginase in a dose-dependent manner, and displays a linear competitive inhibition on sickle erythrocyte arginase
cycloheximide
-
inhibits protein synthesis
diethylene triamine-nitric oxide
-
50% inhibition at 2 mM
diethylpyrocarbonate
1 mM, 83% loss of activity
dihydroquercetin
0.1 mM, about 25% inhibition
DL-isoleucine
-
competitive inhibitor
DTT
-
50% inhibition at 0.025 mM
eugenol
0.1 mM, about 20% inhibition
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
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
hydrogen peroxide
-
50% inhibition at 0.003 mM
indole-propionic acid
-
-
Insulin
-
reduces arginase activity
-
isorhamnetin
0.1 mM, about 55% inhibition
L-2-amino-3-guanidinopropionic acid
-
-
L-histidine
strongly blocked SmARG-activity
L-N5-(1-iminoethyl)-ornithine
-
-
L-N6-(1-iminoethyl)-lysine
-
-
L-norvaline
-
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
N-acetyl-5-hydroxytryptamine
N-hydroxy-nor-L-arginine
-
-
N-omega-hydroxy-L-arginine
-
moderate inhibition
NG-monomethyl-L-arginine
poor arginase 1 inhibitor
Nomega-amino-L-arginine
-
-
Nomega-hydroxy-L-arginine
Nomega-hydroxy-nor-arginine
-
Nomega-hydroxy-nor-L-arginine
Nomega-Nitro-L-arginine
-
-
Nomega-nitro-L-arginine methyl ester
-
i.e. L-NAME, inhibition of enzyme from liver and colon cancer cells in vitro and in vivo
nor-N-hydroxy-L-arginine
-
nor-NOHA
-
competitive inhibitor of both isoforms of arginase
nor-Nomega-hydroxy-L-arginine
-
Pb2+
-
74% inhibition of isozyme I, 92% inhibition of isozyme II
PEG-SOD
-
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
-
Polymyxin B
-
blocks arginase activity in Actinobacillus actinomycetemcomitans-lipopolysaccharide-stimulated cells
proline
poor arginase 1 inhibitor
quercetin
0.1 mM, about 70% inhibition
Rhamnetin
0.1 mM, about 50% inhibition
rhaponticin
0.1 mM, about 60% inhibition
rosmarinic acid
0.1 mM, 71.48% inhibition
S-(2-aminoethyl)isothiourea
-
-
S-(2-boronoethyl)-L-cysteine
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
S-(3-aminopropyl)isothiourea
-
-
S-(boronoethyl)-L-cysteine
-
S-methyl-L-thiocitrulline
-
-
S-nitrosoglutathione
-
50% inhibition at 0.050 mM
Sodium fluoride
-
noncompetitive
sodium nitroprusside
-
50% inhibition at 0.005 mM
spermidine
-
inhibition in a dose-dependent fashion below 5 mM and above 25 mM
symmetric dimethylarginine
poor arginase 1 inhibitor
Woodward's reagent K
-
complete inactivation, reactivation by 0.5 M hydroxylamine. Reactivated enzyme can be inactivated again
(-)-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
(-)-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
(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
-
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
(R)-2-amino-6-borono-2-[2-(piperidin-1-yl)ethyl]hexanoic acid
-
(R)-2-amino-6-borono-2-[2-(piperidin-1-yl)ethyl]hexanoic acid
-
(S)-2-amino-7-oxoheptanoic acid
-
(S)-2-amino-7-oxoheptanoic acid
-
-
(S)-2-amino-7-oxoheptanoic acid
-
2(S)-amino-6-boronohexanoic acid
-
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
-
transition state analogue inhibitor
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
-
2(S)-amino-6-boronohexanoic acid
-
-
2(S)-amino-6-boronohexanoic acid
-
2(S)-amino-6-boronohexanoic acid
-
0.005 mM, selective arginase inhibitor
2(S)-amino-6-boronohexanoic acid
-
transition state analogue inhibitor, effect on female and male hemodynamics, overview
2(S)-amino-6-boronohexanoic acid
-
2(S)-amino-6-boronohexanoic acid
-
2(S)-amino-6-boronohexanoic acid
-
-
2(S)-amino-6-boronohexanoic acid
-
2-(1H-indol-3-yl)ethanol
-
-
2-(1H-indol-3-yl)ethanol
-
-
2-(S)-amino-6-boronohexanoic acid
-
-
2-(S)-amino-6-boronohexanoic acid
-
2-amino-6-boronohexanoic acid
-
2-amino-6-boronohexanoic acid
-
-
2-mercaptoethanol
-
-
2-mercaptoethanol
1 mM, 12% loss of activity
2-mercaptoethanol
-
50% inhibition at 0.8 mM
5-hydroxy-L-tryptophan
-
-
5-hydroxy-L-tryptophan
-
-
5-hydroxytryptamine
-
-
Ag+
20.41% residual activity at 1 mM; 20.41% residual activity at 1 mM
agmatine
-
-
agmatine
poor arginase 1 inhibitor
Ba2+
-
80% residual activity at 1.5 mM
Ba2+
2 mM, slight inhibition
Borate
-
noncompetitive
Ca2+
-
inhibitory to enzymic activity in presence of Mn2+, enhances lectin function of enzyme
Ca2+
2 mM, slight inhibition
Ca2+
-
inhibitory to enzymic activity in presence of Mn2+, enhances lectin function of enzyme
caffeic acid
0.1 mM, 56.98% inhibition
caffeic acid
-
inhibiting arginase activity by caffeic acid and chlorogenic acid might be a possible mechanism by which they exert their cardio-protective effect
Cd2+
-
-
Cd2+
58.78% residual activity at 1 mM; 58.78% residual activity at 1 mM
Cd2+
-
10% inhibition of isozyme I, 86% inhibition of isozyme II
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+
chlorogenic acid
0.1 mM, about 30% inhibition
chlorogenic acid
-
inhibiting arginase activity by caffeic acid and chlorogenic acid might be a possible mechanism by which they exert their cardio-protective effect
Co2+
-
84% residual activity at 1.5 mM
Creatine
-
-
Cu2+
2 mM, slight inhibition
Cu2+
30.2% residual activity at 1 mM; 30.2% residual activity at 1 mM
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
D-tryptophan
-
-
diethyl dicarbonate
-
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
-
second-order rate constant of 113 per M and s for inactivation process. L-ornithine partially protects, L-ornithine plus borate completely protect
dithiothreitol
-
-
dithiothreitol
-
50% inhibition at 0.025 mM
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+
EDTA
-
-
EDTA
-
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+
-
78% residual activity at 1.5 mM
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
Fe3+
-
12% inhibition of isozyme I, 36% inhibition of isozyme II
flavanol-rich cocoa
-
cocoa flavanols lower arginase-2 mRNA expression and activity
-
flavanol-rich cocoa
-
cocoa flavanols lower arginase-2 mRNA expression and activity
-
gamma-guanidinobutyrate
-
-
gamma-guanidinobutyrate
-
-
Hg2+
-
-
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
imidazole-3-lactate
-
-
indole
-
-
indole-3-L-lactic acid
-
-
indole-3-L-lactic acid
-
-
L-argininamide
-
mixed type of inhibition
L-argininic acid
-
-
L-canavanine
-
non-competitive type of inhibition
L-cysteine
strongly blocked SmARG-activity
L-homoarginine
-
mixed type of inhibition
L-isoleucine
-
-
L-isoleucine
Vigna catjang
-
-
L-leucine
-
-
L-leucine
-
competitive inhibitor
L-leucine
Vigna catjang
-
-
L-lysine
-
-
L-lysine
-
competitive inhibitor
L-lysine
binds to isoform arginase I with Kd of 13.1 microM
L-lysine
Vigna catjang
-
-
L-ornithine
-
-
L-ornithine
-
product inhibition
L-ornithine
-
competitive inhibitor
L-ornithine
mixed type inhibition; mixed type inhibition
L-ornithine
moderately inhibitory
L-ornithine
Vigna catjang
-
-
L-proline
-
-
L-proline
Vigna catjang
-
-
L-tryptophan
-
-
L-valine
-
-
L-valine
-
competitive inhibitor
L-valine
Vigna catjang
-
-
lysine
-
-
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
Mg2+
-
64% residual activity at 1.5 mM
Mg2+
2 mM, slight inhibition
N-acetyl-5-hydroxytryptamine
-
-
N-acetyl-5-hydroxytryptamine
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
1 mM, 93% loss of activity
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
Ni2+
-
83% residual activity at 1.5 mM
Ni2+
-
no inhibition of isozyme I, 11% inhibition of isozyme II
Nomega-hydroxy-L-arginine
-
Nomega-hydroxy-L-arginine
mixed type inhibition; mixed type inhibition
Nomega-hydroxy-L-arginine
-
competitive, reaction intermediate
Nomega-hydroxy-L-arginine
-
-
Nomega-hydroxy-L-arginine
i.e. NOHA, binds to isoform arginase I with Kd of 3.6 microM
Nomega-hydroxy-L-arginine
-
-
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
-
competitive, reaction intermediate analogue
Nomega-hydroxy-nor-L-arginine
-
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
Nomega-hydroxy-nor-L-arginine
-
-
Nomega-hydroxy-nor-L-arginine
-
-
Nomega-hydroxy-nor-L-arginine
nor-NOHA; nor-NOHA
Nomega-hydroxy-nor-L-arginine
norNOHA
Nomega-hydroxy-nor-L-arginine
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
S-(2-boronoethyl)-L-cysteine
-
-
S-(2-boronoethyl)-L-cysteine
-
inhibition results in in reduced fractional shortening, maximal rate of shortening, and relengthening of myocyte contractions
S-(2-boronoethyl)-L-cysteine
-
S-(2-boronoethyl)-L-cysteine
-
transition state analogue inhibitor
S-(2-boronoethyl)-L-cysteine
Kd-value 270 nM
S-(2-boronoethyl)-L-cysteine
-
-
S-(2-boronoethyl)-L-cysteine
-
S-(2-boronoethyl)-L-cysteine
BEC; BEC
S-(2-boronoethyl)-L-cysteine
-
transition state analogue inhibitor
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
S-(2-boronoethyl)-L-cysteine
-
tryptamine
-
-
tyramine
-
-
Urea
-
-
Zn2+
-
potent inhibitor
Zn2+
2 mM, slight inhibition
Zn2+
33.47% residual activity at 1 mM; 33.47% residual activity at 1 mM
Zn2+
-
13% inhibition of isozyme I, 75% inhibition of isozyme II
additional information
-
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
-
additional information
-
binding to lectins is inhibitory to enzymic activity, which is recovered after desorption of the lectin with alpha-D-galactose
-
additional information
-
ornithine is a poor inhibitor of isozyme type II, isozyme selectivity in binding and substrate, products, and inhibitors
-
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
-
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
-
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
-
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
-
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
-
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; 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
-
additional information
-
isothiourea homologues undergo rapid non-enzymic rearrangement to probably give inhibitory compouds, overview
-
additional information
-
effect of preincubation of the isozymes with metal ions, 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
-
additional information
L-lysine and diaminopimelic acid failed to block SmARG activity
-
additional information
-
L-lysine and diaminopimelic acid failed to block SmARG activity
-
additional information
-
binding to lectins is inhibitory to enzymic activity, which is recovered after desorption of the lectin with alpha-D-galactose
-
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1.6
1-nitro-3-guanidinobenzene
-
pH 9.0
0.01
4-guanidino-2-nitrophenylacetic acid
-
pH 9.0
0.007
4-guanidino-3-nitrobenzoic acid
-
pH 9.0
2.5
agmatine
-
37°C, pH 9.0, mutant N149D
22.1 - 57.5
L-phenylalanine
0.5
L-thioarginine
-
pH 9.0
4
S-(4-aminobutyl)isothiourea
-
pH 9.0
2.1
thioguanidino-valeric acid
-
pH 9.0
additional information
additional information
-
0.69
L-Arg
-
-
2.05
L-Arg
-
membrane bound form
50
L-Arg
Glycine hispida
-
-
130
L-Arg
-
membrane bound form
0.02
L-arginine
pH 9.5
0.08
L-arginine
mutant S230G, activated by Co2+, pH 7.4, 37°C
0.15
L-arginine
mutant D181E/S230A, activated by Co2+, pH 7.4, 37°C
0.15
L-arginine
mutant S230C, activated by Co2+, pH 7.4, 37°C
0.15
L-arginine
mutant S230D, activated by Co2+, pH 7.4, 37°C
0.16
L-arginine
mutant S230T, activated by Co2+, pH 7.4, 37°C
0.19
L-arginine
mutant D181S/S230G, activated by Co2+, pH 7.4, 37°C
0.21
L-arginine
mutant D181N/S230G, activated by Co2+, pH 7.4, 37°C
0.27
L-arginine
mutant D181E, activated by Co2+, pH 7.4, 37°C
0.28
L-arginine
mutant D181S, activated by Co2+, pH 7.4, 37°C
0.3
L-arginine
-
wild-type enzyme, pH 9.5
0.3
L-arginine
mutant D181N, activated by Co2+, pH 7.4, 37°C
0.8
L-arginine
mutant S230G, activated by Mn2+, pH 7.4, 37°C
1.07
L-arginine
-
wild-type enzyme, pH 9.0
1.4
L-arginine
-
37°C, pH 9.0, wild-type
1.5
L-arginine
-
wild type
1.5
L-arginine
-
37°C, pH 9.0, mutant H145N
1.5
L-arginine
-
wild type enzyme, at 37°C
1.5
L-arginine
wild-type, pH 9.5
1.6
L-arginine
-
37°C, pH 9.0, mutant H120N
1.81
L-arginine
-
at pH 6.8 and 37°C
1.9
L-arginine
-
native rhArg1
1.9
L-arginine
arginase 2, pH and temperature not specified in the publication
2
L-arginine
-
pH 9.2, 37°C
2.08
L-arginine
-
at pH 6.8 and 37°C
2.1
L-arginine
mutant S230C, activated by Mn2+, pH 7.4, 37°C
2.4
L-arginine
-
truncated mutant enzyme, pH 9.5
2.5
L-arginine
-
mutant R308A, pH 9.0
2.5
L-arginine
T135S mutant, KM increases 2.5fold relatively to values measured for the wild-type enzyme
2.6
L-arginine
-
mutant R308E, pH 9.0
2.7
L-arginine
-
mutant R308K, pH 9.0
2.8
L-arginine
mutant D181N/S230G, activated by Mn2+, pH 7.4, 37°C
2.9
L-arginine
-
Km of pegylated rhArg1 (rhArg1-peg5,000 mw)
3
L-arginine
mutant D181N, activated by Mn2+, pH 7.4, 37°C
3.1
L-arginine
-
mutant S89G, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 2.1
3.3
L-arginine
mutant dN-PFA, pH 8.5, 37°C
3.3
L-arginine
arginase 1, pH and temperature not specified in the publication
3.4
L-arginine
pH 9.5, 55°C, wild-type enzyme
3.7
L-arginine
monomeric E256Q variant, pH 9.5
4
L-arginine
mutant dN-PFA, pH 8.0, 37°C
4
L-arginine
mutant dN-PFA-L2S, pH 8.0, 37°C
4.4
L-arginine
-
mutant H91A, Co2+-activated, pH 5.0, 37°C, Hill coefficient 2.3
4.6
L-arginine
at pH 8.4 and 45°C
4.8
L-arginine
-
about pH 7.0
4.8
L-arginine
-
free and chitosan-immobilized enzyme, at pH 7.0 and 40°C
4.98
L-arginine
-
pH 9.4, 37°C, presence of 0.1 mM Mn2+
5
L-arginine
-
mutant C73A, pH 7.2, 37°C
5
L-arginine
pH 9.5, 55°C, mutant enzyme E278A
5.1
L-arginine
pH 9.5, 37°C
5.14
L-arginine
-
pH 9.4, 37°C
5.2
L-arginine
-
mutant A92S, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 1.6
5.25
L-arginine
at pH 7.0 and 30°C
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
L-arginine
-
mutant C66A, pH 7.2, 37°C
6.2
L-arginine
-
wild-type, pH 7.2, 37°C
6.3
L-arginine
-
mutant S88G, Co2+-activated, pH 5.0, 37°C, Hill coefficient 2.0
6.3
L-arginine
pH 9.5, 55°C, mutant enzyme E256A
6.4
L-arginine
-
mutant E90A, Co2+-activated, pH 5.0, 37°C, Hill coefficient 1.7
6.5
L-arginine
pH 9.5, 55°C, mutant enzyme D199N
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
7.1
L-arginine
-
pH 7.5, 37°C
7.14
L-arginine
-
in absence of dihydropyrimidine derivative, pH and temperature not specified in the publication
7.2
L-arginine
pH 9.5, 55°C, mutant enzyme E256A/E278A
7.6
L-arginine
at pH 8.5, in H2O buffer
7.7
L-arginine
at pH 8.5, in D2O buffer
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
9.1
L-arginine
pH 9.5, 55°C, mutant enzyme E256Q
9.2
L-arginine
-
mutant S88G/A92S, Mn2+-activated, pH 5.0, 37°C, Hill coefficient 2.2
9.8
L-arginine
pH 9.5, 55°C, mutant enzyme D199A
10
L-arginine
mutant dN-PFA-H381A, pH 8.0, 37°C
12
L-arginine
mutant dN-PFA-C6H, pH 8.0, 37°C
13
L-arginine
T135A mutant, KM is increased 13fold relatively to values measured for the wild-type enzyme
13
L-arginine
wild-type, pH 8.0, temperature not specified in the publication
13.3
L-arginine
-
mutant enzyme N130D, at 37°C
13.9
L-arginine
D183A mutant
15.2
L-arginine
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
17
L-arginine
pH 10, 37°C
19.3
L-arginine
N130F mutant
20
L-arginine
mutant dN-PFA-L8, pH 8.0, 37°C
21.4
L-arginine
N130Y mutant
21.5
L-arginine
-
native enzyme
21.8
L-arginine
-
pH 7.1, 37°C
21.8
L-arginine
pH 9.4, 37°C
21.8
L-arginine
-
pH 7.1, 37°C, recombinant enzyme
23.9
L-arginine
-
native enzyme
24.76
L-arginine
pH 9.0, 37°C, wild-type enzyme
25
L-arginine
mutant dN-PFA, pH 7.4, 37°C
29.5
L-arginine
-
pH 7.8, 37°C
40
L-arginine
-
D183N mutant
42
L-arginine
Vigna catjang
-
pH 10.0, 37°C
45
L-arginine
mutant R404A, pH 8.0, temperature not specified in the publication
50
L-arginine
N130A mutant
107
L-arginine
pH 9.0, 37°C, mutant enzyme E288Q
136
L-arginine
-
D183A mutant
146
L-arginine
mutant E295R, pH 8.0, temperature not specified in the publication
171.9
L-arginine
pH 9.0, 80°C
22.1
L-phenylalanine
-
free enzyme, at pH 7.0 and 40°C
32.8
L-phenylalanine
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
57.5
L-phenylalanine
-
chitosan-immobilized enzyme, at pH 7.0 and 40°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Pista pacifica
-
-
-
additional information
additional information
-
-
-
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0.0015
1-nitro-3-guanidinobenzene
-
pH 9.0
0.09
4-guanidino-2-nitrophenylacetic acid
-
pH 9.0
0.058
4-guanidino-3-nitrobenzoic acid
-
pH 9.0
0.25 - 0.94
L-phenylalanine
300
L-thioarginine
-
pH 9.0
3.33
S-(4-aminobutyl)isothiourea
-
pH 9.0
0.013
thioguanidino-valeric acid
-
pH 9.0
0.013
L-arginine
-
mutant E90A, Co2+-activated, pH 5.0, 37°C
0.013
L-arginine
-
mutant H91A, Co2+-activated, pH 5.0, 37°C
0.04
L-arginine
-
mutant S89G, Mn2+-activated, pH 5.0, 37°C
0.067
L-arginine
-
pH 5.0, 37°C, Mn2+-activited enzyme
0.067
L-arginine
-
wild-type, Mn2+-activated, pH 5.0, 37°C
0.12
L-arginine
-
mutant S89G, Co2+-activated, pH 5.0, 37°C
0.18
L-arginine
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
0.25
L-arginine
-
chitosan-immobilized enzyme, at pH 7.0 and 40°C
0.27
L-arginine
-
mutant S88G, Mn2+-activated, pH 5.0, 37°C
0.27
L-arginine
-
free enzyme, at pH 7.0 and 40°C
0.28
L-arginine
-
mutant S88G/A92S, Mn2+-activated, pH 5.0, 37°C
0.28
L-arginine
-
pH 5.0, 37°C, Co2+-activited enzyme
0.28
L-arginine
-
wild-type, Co2+-activated, pH 5.0, 37°C
0.37
L-arginine
-
mutant C66A, pH 7.2, 37°C
0.52
L-arginine
-
wild-type, pH 7.2, 37°C
0.53
L-arginine
-
mutant C73A, pH 7.2, 37°C
0.84
L-arginine
-
mutant A92S, Mn2+-activated, pH 5.0, 37°C
0.92
L-arginine
-
mutant A92S, Co2+-activated, pH 5.0, 37°C
1
L-arginine
mutant E295A, pH 8.0, temperature not specified in the publication
1.01
L-arginine
-
mutant S88G, Co2+-activated, pH 5.0, 37°C
1.3
L-arginine
mutant E295A/R404A, pH 8.0, temperature not specified in the publication
1.37
L-arginine
-
mutant S88G/A92S, Co2+-activated, pH 5.0, 37°C
2 - 8
L-arginine
mutant dN-PFA-H381A, pH 8.0, 37°C
4.8
L-arginine
N130F mutant
6.7
L-arginine
mutant E295R, pH 8.0, temperature not specified in the publication
11.4
L-arginine
mutant R404A, pH 8.0, temperature not specified in the publication
14.7
L-arginine
D183A mutant
17
L-arginine
N130Y mutant
24.8
L-arginine
wild-type, pH 8.0, temperature not specified in the publication
33
L-arginine
-
mutant enzyme N130D, at 37°C
68
L-arginine
-
D183A mutant
72
L-arginine
-
mutant R308K, pH 9.0
76
L-arginine
mutant dN-PFA-C6H, pH 8.0, 37°C
77
L-arginine
mutant dN-PFA, pH 7.4, 37°C
84
L-arginine
-
mutant R308A, pH 9.0
89
L-arginine
-
mutant R308E, pH 9.0
131
L-arginine
-
37°C, pH 9.0, mutant H120N
140
L-arginine
mutant S230D, activated by Co2+, pH 7.4, 37°C
167
L-arginine
-
D183N mutant
179
L-arginine
pH 9.0, 37°C, wild-type enzyme
180
L-arginine
monomeric E256Q variant, pH 9.5
180
L-arginine
mutant D181S/S230G, activated by Co2+, pH 7.4, 37°C
190
L-arginine
-
wild type
190
L-arginine
-
wild type enzyme, at 37°C
190
L-arginine
wild-type, pH 9.5
190
L-arginine
pH 9.0, 37°C, mutant enzyme E288Q
200
L-arginine
mutant S230G, activated by Co2+, pH 7.4, 37°C
203
L-arginine
-
truncated mutant enzyme, pH 9.5
220
L-arginine
-
wild-type enzyme, pH 9.0
220
L-arginine
N130A mutant
220
L-arginine
mutant D181E/S230A, activated by Co2+, pH 7.4, 37°C
231
L-arginine
-
wild-type enzyme, pH 9.5
238
L-arginine
-
37°C, pH 9.0, mutant H145N
247
L-arginine
mutant D181N/S230G, activated by Co2+, pH 7.4, 37°C
249
L-arginine
-
37°C, pH 9.0, wild-type
260
L-arginine
T135A mutant, is reduced 26% relative to values measured for the wild-type enzyme
266
L-arginine
mutant S230G, activated by Mn2+, pH 7.4, 37°C
285
L-arginine
mutant S230C, activated by Mn2+, pH 7.4, 37°C
300
L-arginine
pH 9.5, 55°C, mutant enzyme E256A
300
L-arginine
pH 9.5, 55°C, mutant enzyme E256A/E278A
315
L-arginine
mutant S230T, activated by Co2+, pH 7.4, 37°C
320
L-arginine
mutant dN-PFA, pH 8.0, 37°C
327
L-arginine
mutant S230C, activated by Co2+, pH 7.4, 37°C
344
L-arginine
mutant D181E, activated by Co2+, pH 7.4, 37°C
350
L-arginine
T135S mutant, kcat is unchanged relatively to values measured for the wild-type enzyme
360
L-arginine
mutant D181N, activated by Mn2+, pH 7.4, 37°C
387
L-arginine
mutant D181N, activated by Co2+, pH 7.4, 37°C
388
L-arginine
mutant D181S, activated by Co2+, pH 7.4, 37°C
400
L-arginine
pH 9.5, 55°C, mutant enzyme D199N
400
L-arginine
pH 9.5, 55°C, mutant enzyme E256Q
440
L-arginine
mutant dN-PFA, pH 8.5, 37°C
500
L-arginine
pH 9.5, 55°C, mutant enzyme D199A
517
L-arginine
mutant D181N/S230G, activated by Mn2+, pH 7.4, 37°C
537
L-arginine
pH 10, 37°C
657
L-arginine
pH 9.0, 80°C
700
L-arginine
pH 9.5, 55°C, wild-type enzyme
750
L-arginine
pH 9.5, 55°C, mutant enzyme E278A
1132
L-arginine
pH 9.4, 37°C
0.25
L-phenylalanine
-
free enzyme, at pH 7.0 and 40°C
0.46
L-phenylalanine
-
chitosan-immobilized enzyme, at pH 7.0 and 40°C
0.94
L-phenylalanine
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
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0.3
(2S)-2-amino-3-(2-amino-1H-imidazol-5-yl)propanoic acid
pH not specified in the publication, temperature not specified in the publication
0.5
(2S)-2-amino-5-(1H-imidazol-2-ylamino)pentanoic acid
pH not specified in the publication, temperature not specified in the publication
0.36
(2S,5E)-2-amino-7-oxohept-5-enoic acid
-
pH 9.5
0.0011
(DL)-2-amino-6-borono-2-[1-(3,4-dichlorobenzyl)piperidin-4-yl]-hexanoic acid
pH 8.0, 21°C
0.00003 - 0.00031
(S)-(2-boronoethyl)-L-cysteine
0.0014
(S)-2-amino-6-borono-2-[2-(piperidin-1-yl)ethyl]hexanoic acid
pH 8.0, 21°C
0.06
(S)-2-amino-7-oxoheptanoic acid
0.0000085 - 0.053
2(S)-amino-6-boronohexanoic acid
0.017
2-(5-methyl-2-(trifluoromethyl)-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)hydrazinecarbothioamide
at pH 9.5 and 37°C
0.004
2-(S)-amino-5-(2-aminoimidazol-1-yl)pentanoic acid
pH not specified in the publication, temperature not specified in the publication
0.00015 - 0.0009
2-(S)-amino-6-boronohexanoic acid
0.023 - 0.041
Chloroquine
17.5
DL-isoleucine
-
pH 7.5, 37°C
39 - 56
Guanidinium chloride
0.0442 - 0.0808
hydroxylamine
0.0362 - 0.0658
iodoacetamide
10.96
L-canavanine
-
pH 7.8, 37°C
10
L-leucine
-
pH 7.5, 37°C
5
L-valine
-
pH 7.5, 37°C
179.3
N-omega-hydroxy-L-arginine
-
pH 7.8, 37°C
0.0016 - 0.061
Nomega-hydroxy-L-arginine
0.000051
Nomega-hydroxy-nor-L-arginine
-
pH 7.5, 22°C
0.0305 - 0.0857
propargylglycine
0.000125 - 0.013
S-(2-boronoethyl)-L-cysteine
0.38 - 1.84
Sodium fluoride
additional information
additional information
-
0.00003
(S)-(2-boronoethyl)-L-cysteine
-
pH 9.5, 22°C
0.00031
(S)-(2-boronoethyl)-L-cysteine
-
pH 7.5, 22°C
0.06
(S)-2-amino-7-oxoheptanoic acid
-
0.06
(S)-2-amino-7-oxoheptanoic acid
-
pH 9.5
0.0000085
2(S)-amino-6-boronohexanoic acid
-
pH 9.5, 22°C
0.00025
2(S)-amino-6-boronohexanoic acid
-
pH 7.5, 22°C
0.01
2(S)-amino-6-boronohexanoic acid
mutant dN-PFA, pH 8.5, 37°C
0.011
2(S)-amino-6-boronohexanoic acid
mutant dN-PFA, pH 7.4, 37°C
0.012
2(S)-amino-6-boronohexanoic acid
mutant dN-PFA, pH 8.0, 37°C
0.053
2(S)-amino-6-boronohexanoic acid
mutant dN-PFA-H381A, pH 8.0, 37°C
0.00015
2-(S)-amino-6-boronohexanoic acid
-
pH 9.5, 25°C, supramolecular tandem assay method
0.0009
2-(S)-amino-6-boronohexanoic acid
pH 8.0, 21°C
0.023
Chloroquine
-
at pH 6.8 and 37°C
0.041
Chloroquine
-
at pH 7.4 and 37°C
39
Guanidinium chloride
-
mutant enzyme N130D
56
Guanidinium chloride
-
wild type enzyme
1.73
homoarginine
arginase 2, pH and temperature not specified in the publication
6.1
homoarginine
arginase 1, pH and temperature not specified in the publication
0.0442
hydroxylamine
-
chitosan-immobilized enzyme, at pH 7.0 and 40°C
0.0656
hydroxylamine
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
0.0808
hydroxylamine
-
free enzyme, at pH 7.0 and 40°C
0.0362
iodoacetamide
-
chitosan-immobilized enzyme, at pH 7.0 and 40°C
0.0618
iodoacetamide
-
free enzyme, at pH 7.0 and 40°C
0.0658
iodoacetamide
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
3.1
L-lysine
-
presence of 0.1 mM Mn2+, pH 9.4, 37°C
5.6
L-lysine
-
pH 9.4, 37°C
8
L-lysine
-
pH 7.5, 37°C
0.05
L-ornithine
product inhibition constant, Co2+-activated mutant S230G, pH 7.4, 37°C
0.09
L-ornithine
product inhibition constant, Co2+-activated mutant D181N/S230G, pH 7.4, 37°C
0.11
L-ornithine
product inhibition constant, Co2+-activated mutant D181N, pH 7.4, 37°C
0.7
L-ornithine
-
presence of 0.1 mM Mn2+, pH 9.4, 37°C
0.7
L-ornithine
product inhibition constant, Mn2+-activated mutant S230G, pH 7.4, 37°C
1
L-ornithine
-
wild type enzyme
1
L-ornithine
product inhibition constant, Mn2+-activated mutant D181N/S230G, pH 7.4, 37°C
1.18
L-ornithine
-
pH 9.4, 37°C
1.4
L-ornithine
-
pH 9.5, 37°C, liver enzyme
1.9
L-ornithine
pH 10, 37°C
2.16
L-ornithine
at pH 7.0 and 30°C
2.4
L-ornithine
product inhibition constant, Mn2+-activated mutant D181N, pH 7.4, 37°C
7.8
L-ornithine
-
pH 9.5, 37°C, enzyme from submandibular gland
7.8
L-ornithine
-
mutant enzyme N130D
30
L-ornithine
-
pH 7.5, 37°C
0.5
lysine
arginase 2, pH and temperature not specified in the publication
1.79
lysine
arginase 1, pH and temperature not specified in the publication
0.0016
Nomega-hydroxy-L-arginine
-
pH 7.5, 22°C
0.014
Nomega-hydroxy-L-arginine
pH 9.6, 37°C
0.02
Nomega-hydroxy-L-arginine
at pH 7.0 and 30°C
0.05
Nomega-hydroxy-L-arginine
-
pH 9.5, 37°C, liver enzyme
0.061
Nomega-hydroxy-L-arginine
-
pH 9.5, 37°C, enzyme from submandibular gland
0.0305
propargylglycine
-
chitosan-immobilized enzyme, at pH 7.0 and 40°C
0.0626
propargylglycine
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
0.0857
propargylglycine
-
free enzyme, at pH 7.0 and 40°C
0.000125
S-(2-boronoethyl)-L-cysteine
T135S mutant
0.0004
S-(2-boronoethyl)-L-cysteine
wild type
0.0036
S-(2-boronoethyl)-L-cysteine
-
pH 9.5, 25°C, supramolecular tandem assay method
0.0045
S-(2-boronoethyl)-L-cysteine
T135A mutant
0.013
S-(2-boronoethyl)-L-cysteine
N130A mutant
0.38
Sodium fluoride
-
pH 7.4, 37°C, thermokinetic method, presence of 0.167 mM Mn2+
0.51
Sodium fluoride
-
pH 7.4, 37°C, thermokinetic method
1.48
Sodium fluoride
-
pH 7.4, 37°C, initial rate method, presence of 0.167 mM Mn2+
1.84
Sodium fluoride
-
pH 7.4, 37°C, initial rate method
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
estimated Ki for several inhibitors, overview, inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0017
(DL)-2-amino-6-borono-2-[1-(3,4-dichlorobenzyl)piperidin-4-yl]-hexanoic acid
Leishmania mexicana
pH 8.0, 21°C
0.0021
(S)-2-amino-6-borono-2-[2-(piperidin-1-yl)ethyl]hexanoic acid
Leishmania mexicana
pH 8.0, 21°C
4.8 - 5.3
2-(1H-indol-3-yl)ethanol
0.0165
2-(5-methyl-2-(trifluoromethyl)-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)hydrazinecarbothioamide
Leishmania amazonensis
at pH 9.5 and 37°C
0.00135 - 0.00207
2-(aminomethyl)-6-borononorleucine
0.00022 - 0.0013
2-(S)-amino-6-boronohexanoic acid
0.0045
2-amino-6-borono-2-butylhexanoic acid
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00145 - 0.00192
2-amino-6-boronohexanoic acid
0.03 - 1.196
2-mercaptoethanol
0.00326 - 0.00598
2-[(benzylamino)methyl]-6-borononorleucine
3.6 - 3.9
5-hydroxy-L-tryptophan
3.3 - 3.6
5-hydroxytryptamine
0.019 - 0.057
6-borono-2-(2-hydroxyethyl)norleucine
0.00512 - 0.00644
6-borono-2-(3-methoxypropyl)norleucine
0.00225 - 0.00428
6-borono-2-(hydroxymethyl)norleucine
0.0041 - 0.0046
6-borono-2-ethylnorleucine
0.0034 - 0.0057
6-borono-2-methylnorleucine
0.01124 - 0.0155
6-borono-2-propan-2-ylnorleucine
0.00037 - 0.00098
6-borono-2-[2-(4-hydroxypiperidin-1-yl)ethyl]norleucine
0.00052 - 0.000934
6-borono-2-[2-(diethylamino)ethyl]norleucine
0.00402 - 0.00538
6-borono-2-[2-(morpholin-4-yl)ethyl]norleucine
0.00032 - 0.00062
6-borono-2-[2-(pyrrolidin-1-yl)ethyl]norleucine
0.00228 - 0.00372
alpha-(4-boronobutyl)histidine
0.0105 - 0.017
alpha-(4-boronobutyl)phenylalanine
0.0219 - 0.0608
caffeic acid
0.077 - 0.109
Chloroquine
0.01 - 7.789
dithiothreitol
9.5
DL-isoleucine
Camelus dromedarius
-
pH 7.5, 37°C
0.33
EDTA
Coriandrum sativum
-
pH 7.8, 37°C
0.00005
fungizone
Leishmania infantum
pH 9.5, 37°C, activity in promastigote
0.0656 - 0.0808
hydroxylamine
3.4 - 3.6
indole-3-L-lactic acid
0.0618 - 0.0658
iodoacetamide
0.818
isorhamnetin
Leishmania infantum
pH 9.5, 37°C, activity in promastigote
20
N-acetyl-5-hydroxytryptamine
Bos taurus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
0.5
Nomega-hydroxy-nor-arginine
Helicobacter pylori
pH 7.5, 37°C
0.0626 - 0.0857
propargylglycine
0.832
Rhamnetin
Leishmania infantum
pH 9.5, 37°C, activity in promastigote
0.0079 - 0.0573
rosmarinic acid
0.0037 - 1
S-(2-boronoethyl)-L-cysteine
4.8
2-(1H-indol-3-yl)ethanol
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
5.3
2-(1H-indol-3-yl)ethanol
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
0.00135
2-(aminomethyl)-6-borononorleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00207
2-(aminomethyl)-6-borononorleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00022
2-(S)-amino-6-boronohexanoic acid
Bos taurus
-
pH 9.5, 25°C, supramolecular tandem assay method
0.0013
2-(S)-amino-6-boronohexanoic acid
Leishmania mexicana
pH 8.0, 21°C
0.00145
2-amino-6-boronohexanoic acid
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00192
2-amino-6-boronohexanoic acid
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.03
2-mercaptoethanol
Helicobacter pylori
pH 7.5, 37°C
1.196
2-mercaptoethanol
Coriandrum sativum
-
pH 7.8, 37°C
0.00326
2-[(benzylamino)methyl]-6-borononorleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00598
2-[(benzylamino)methyl]-6-borononorleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
3.6
5-hydroxy-L-tryptophan
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
3.9
5-hydroxy-L-tryptophan
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
3.3
5-hydroxytryptamine
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
3.6
5-hydroxytryptamine
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
0.019
6-borono-2-(2-hydroxyethyl)norleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.057
6-borono-2-(2-hydroxyethyl)norleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00512
6-borono-2-(3-methoxypropyl)norleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00644
6-borono-2-(3-methoxypropyl)norleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00225
6-borono-2-(hydroxymethyl)norleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00428
6-borono-2-(hydroxymethyl)norleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.0041
6-borono-2-ethylnorleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.0046
6-borono-2-ethylnorleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.0034
6-borono-2-methylnorleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.0057
6-borono-2-methylnorleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.01124
6-borono-2-propan-2-ylnorleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.0155
6-borono-2-propan-2-ylnorleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00037
6-borono-2-[2-(4-hydroxypiperidin-1-yl)ethyl]norleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00098
6-borono-2-[2-(4-hydroxypiperidin-1-yl)ethyl]norleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00052
6-borono-2-[2-(diethylamino)ethyl]norleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.000934
6-borono-2-[2-(diethylamino)ethyl]norleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00402
6-borono-2-[2-(morpholin-4-yl)ethyl]norleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00538
6-borono-2-[2-(morpholin-4-yl)ethyl]norleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00032
6-borono-2-[2-(pyrrolidin-1-yl)ethyl]norleucine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00062
6-borono-2-[2-(pyrrolidin-1-yl)ethyl]norleucine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.00228
alpha-(4-boronobutyl)histidine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.00372
alpha-(4-boronobutyl)histidine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.0105
alpha-(4-boronobutyl)phenylalanine
Homo sapiens
arginase I, at pH 7.4 and 37°C
0.017
alpha-(4-boronobutyl)phenylalanine
Homo sapiens
arginase II, at pH 7.4 and 37°C
0.0219
caffeic acid
Leishmania infantum
pH 9.5, 37°C, activity in intracellular amastigote
0.0608
caffeic acid
Leishmania infantum
pH 9.5, 37°C, activity in promastigote
0.287
catechin
Leishmania infantum
pH 9.5, 37°C, activity in intracellular amastigote
0.395
catechin
Leishmania infantum
pH 9.5, 37°C, activity in promastigote
0.077
Chloroquine
Homo sapiens
-
at pH 6.8 and 37°C
0.109
Chloroquine
Homo sapiens
-
at pH 7.4 and 37°C
8.4
D-tryptophan
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
10
D-tryptophan
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
0.01
dithiothreitol
Helicobacter pylori
pH 7.5, 37°C
7.789
dithiothreitol
Coriandrum sativum
-
pH 7.8, 37°C
2.52
homoarginine
Homo sapiens
arginase 2, pH and temperature not specified in the publication
8.14
homoarginine
Homo sapiens
arginase 1, pH and temperature not specified in the publication
0.0656
hydroxylamine
Penicillium chrysogenum
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
0.0808
hydroxylamine
Penicillium chrysogenum
-
free enzyme, at pH 7.0 and 40°C
20
imidazole-3-lactate
Mus musculus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
20
imidazole-3-lactate
Bos taurus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
20
indole
Mus musculus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
20
indole
Bos taurus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
3.4
indole-3-L-lactic acid
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
3.6
indole-3-L-lactic acid
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
2.8
Indolepropionic acid
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
2.8
Indolepropionic acid
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
0.0618
iodoacetamide
Penicillium chrysogenum
-
free enzyme, at pH 7.0 and 40°C
0.0658
iodoacetamide
Penicillium chrysogenum
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
2
L-isoleucine
Bos taurus
-
-
70
L-isoleucine
Vigna catjang
-
IC50 above 70 mM
2
L-leucine
Bos taurus
-
-
9
L-leucine
Camelus dromedarius
-
pH 7.5, 37°C
70
L-leucine
Vigna catjang
-
IC50 above 70 mM
2
L-lysine
Bos taurus
-
-
22
L-lysine
Camelus dromedarius
-
pH 7.5, 37°C
70
L-lysine
Vigna catjang
-
IC50 above 70 mM
2
L-ornithine
Bos taurus
-
-
24
L-ornithine
Camelus dromedarius
-
pH 7.5, 37°C
70
L-ornithine
Vigna catjang
-
IC50 above 70 mM
10
L-proline
Vigna catjang
-
-
70
L-proline
Bos taurus
-
-
7.5
L-tryptophan
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
8.4
L-tryptophan
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
2
L-valine
Bos taurus
-
-
13
L-valine
Camelus dromedarius
-
pH 7.5, 37°C
70
L-valine
Vigna catjang
-
IC50 above 70 mM
0.88
lysine
Homo sapiens
arginase 2, pH and temperature not specified in the publication
3.64
lysine
Homo sapiens
arginase 1, pH and temperature not specified in the publication
0.0626
propargylglycine
Penicillium chrysogenum
-
PEG-immobilized enzyme, at pH 7.0 and 40°C
0.0857
propargylglycine
Penicillium chrysogenum
-
free enzyme, at pH 7.0 and 40°C
0.0079
rosmarinic acid
Leishmania infantum
pH 9.5, 37°C, activity in intracellular amastigote
0.0573
rosmarinic acid
Leishmania infantum
pH 9.5, 37°C, activity in promastigote
0.0037
S-(2-boronoethyl)-L-cysteine
Bos taurus
-
pH 9.5, 25°C, supramolecular tandem assay method
1
S-(2-boronoethyl)-L-cysteine
Helicobacter pylori
pH 7.5, 37°C
3.2
tryptamine
Bos taurus
-
in the presence of 0.5 mM MnCl2, at 37°C
3.4
tryptamine
Mus musculus
-
in the presence of 0.5 mM MnCl2, at 37°C
20
tyramine
Mus musculus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
20
tyramine
Bos taurus
-
IC50 above 20 mM, in the presence of 0.5 mM MnCl2, at 37°C
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highest expression in 7 week old adult
brenda
Capra capra
-
-
brenda
intracellular
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
Vigna catjang
-
-
brenda
low expression
brenda
-
-
brenda
-
endothelial cells isolated from umbilical veins
brenda
-
type I, postweaning mammals
brenda
-
carcinoma tissue, increased arginase activity in various malignancies. In the event of carcinoma of the gallbladder the enzyme activity is significantly higher in comparison with cholecystitis
brenda
-
-
brenda
-
HBsAg-positive HCC, HB-8064, liver cancer cell line
brenda
-
-
brenda
-
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
brenda
-
-
brenda
-
-
brenda
-
type I
brenda
very low expression
brenda
-
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
brenda
-
type II
brenda
-
-
brenda
-
placental villi, isoform arginase-I is observed only in cytophoblasts, arginase-II in both cytophoblasts and synciotrophoblasts. Both isoforms are expressed in the first trimester and at term, enzyme activity is greater in the first trimester than at term
brenda
-
-
brenda
-
for ARGAH1, but not ARGAH2
brenda
-
-
brenda
-
arginase II
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
S180 cells
brenda
highest expression in 3 h old schistosomulum
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
very low expression
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
-
-
brenda
-
-
brenda
-
mucosal layer of uterine horn, high enzyme activiy
brenda
-
mucosal layer of vestibula, high enzyme activiy
brenda
-
-
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
intact aorta
brenda
-
-
brenda
-
coronary arteriole
brenda
-
coronary arteriole, enzyme activity increases twofold with hypertension. Inhibition of enzyme activity by Nomega-hydroxy-nor-L-arginine or incubation with L-arginine partially restores NO release and dilation to adenosine in hypertrophic vessels
brenda
-
-
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
-
brenda
-
-
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
smooth muscle
brenda
-
smooth muscle
brenda
-
-
brenda
-
type I
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
sickle erythrocyte
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
normal and hypertrophied feline myocardium, both isoforms arginase-I and arginase-II in crude myocardial homogenate. Arginase-I is downregulated in left ventricular hypertrophy
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
-
brenda
-
heart homogenate
brenda
-
-
brenda
-
HBV-negative hepatoblastoma, HB-8065, liver cancer cell line
brenda
-
type I
brenda
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
brenda
-
arginase activity in hepatoma cell is nearly 5fold and 15fold lower than in cirrhotic and normal livers, respectively. The amount of arginase I, as well as the expression of arginase I-mRNA are lower in hepatoma cell, in comparison with normal liver, and those of arginase II are significantly higher
brenda
-
brenda
arginase activity in hepatoma cell is nearly 5fold and 15fold lower than in cirrhotic and normal livers, respectively. The amount of arginase I, as well as the expression of arginase I-mRNA are lower in HCC, in comparison with normal liver, and those of arginase II are significantly higher
brenda
-
HCC
brenda
-
intesintal lumen
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
mid kidney, basal enzyme expression
brenda
-
brenda
-
arginase II
brenda
-
-
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney. Arginase 1a is often higher than arginase 1b, with highest expression seen in the posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
-
brenda
-
isozyme II
brenda
-
-
brenda
induction of isoform LeARG2 upon wounding and treatment with jasmonic acid
brenda
-
-
brenda
-
-
172099, 172116, 172133, 668256, 668975, 670050, 670051, 670930, 684384, 688021, 696006, 696016, 704175 brenda
-
-
brenda
-
-
brenda
-
-
brenda
highest expression of all organs examined
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
arginase I
brenda
-
-
brenda
-
-
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
-
brenda
-
-
brenda
-
-
172101, 172111, 172116, 172124, 654949, 655995, 656381, 656441, 667319, 669653, 697334, 711094 brenda
-
brenda
-
highest enzymic activity
brenda
-
isozyme I
brenda
-
brenda
-
brenda
-
airways
brenda
-
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
brenda
developmental changes in arginase expression and activity in the lung
brenda
cultured head-kidney derived macrophages, significant enzyme activity, inhibitable by Nomega-hydroxy-L-arginine and induced by dibutyryl cyclic adenosine
brenda
cultured head-kidney derived macrophages, significant enzyme activity, inhibitable by Nomega-hydroxy-L-arginine, not inducible by dibutyryl cyclic adenosine
brenda
-
alveolar macrophage
brenda
-
type I
brenda
-
-
brenda
-
alveolar macrophage
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
isolated cardiac myocyte shows only isoform arginase-I
brenda
-
isolated myocyte, isoform arginase II
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
submandibular, sublingual, and parotid gland
brenda
-
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
brenda
-
GUS staining of seedlings
brenda
-
-
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
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
brenda
-
of penile corpus cavernosum
brenda
-
of penile corpus cavernosum
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. intestine; 2. adipose tissue, spleen, blood, head kidney, scales and tail fin; 3. adipose fin, brain, heart, gonad, muscle and thymus; 4. skin; 5. gills and liver; 6. posterior kidney
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. intestine and tail fin; 3. adipose tissue, spleen, gills and scales; 4. adipose fin, skin, blood, posterior kidney, gonad, head kidney and thymus; 5. heart; 6. brain and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. liver; 2. tail fin; 3. adipose tissue, intestine, posterior kidney, head kidney, heart and skin; 4. blood, gonad, scales, gills, spleen, brain, thymus; 5. adipose fin and muscle
brenda
tissues grouped based on their expression as follows, from lowest to highest: 1. tail fin, intestine and scales; 2. adipose tissue, spleen and head kidney; 3. adipose fin and posterior kidney; 4. blood, muscle and thymus; 5. gills; 6. brain, skin, heart, gonad and liver
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
additional information
-
enzyme is present at different levels in all parts of cattle reproductive system
brenda
additional information
enzyme found in all organs examined
brenda
additional information
enzyme found in all organs examined
brenda
additional information
enzyme found in all organs examined
brenda
additional information
enzyme found in all organs examined
brenda
additional information
-
enzyme found in all organs examined
brenda
additional information
-
extrahepatic
brenda
additional information
nonhepatic tissue
brenda
additional information
nonhepatic tissue
brenda
additional information
-
preparation of all and tissue extract
brenda
additional information
-
type II in mitochondria-containing extrahepatic cells
brenda
additional information
-
extrahepatic
brenda
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
brenda
additional information
arginase II is regulated developmentally, and both expression and activity are maximal during fetal life
brenda
additional information
arginase II is regulated developmentally, and both expression and activity are maximal during fetal life
brenda
additional information
highest levels of enzyme activity in reproductive tissues
brenda
additional information
highest levels of enzyme activity in reproductive tissues
brenda
additional information
-
highest levels of enzyme activity in reproductive tissues
brenda
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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
D116A
-
no detectable activity
E90A
-
residue E90 is important for catalytic activity and plays a crucial role in retaining the metal ion at the active site
E90A/H118A
-
no detectable activity
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
S89G
-
1.5fold decrease in catalytic activity
D181E
with Co2+, rate similar to wild-type
D181E/S230A
with Co2+, rate similar to wild-type
D181N
with Co2+, rate similar to wild-type
D181N/S230G
with Co2+, rate similar to wild-type
D181S
with Co2+, rate similar to wild-type
D181S/S230G
with Co2+, rate similar to wild-type
D183A
-
site-directed mutagenesis. D183A substitution completely abolishes the hydrogen bond with the alpha-amino group of the inhibitor, resulting in 1400fold diminished affinity as well as a diminished occupancy of 0.5 for inhibitor binding in the crystal structure
D183N
-
site-directed mutagenesis. D183N substitution results solely from the altered electrostatics of the interaction with the alpha-amino group of the inhibitor
E256Q
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
H101N
-
60% of wild-type activity, unaltered Km for arginine and Ki for lysine compared to the wild-type enzyme
H120N
-
53% of wild-type activity, no alteration in KM-value
H126N
-
82% of wild-type activity, unaltered Km for arginine and Ki for lysine compared to the wild-type enzyme
H141C
-
site-directed mutagenesis, crystal structure determination with bound substrate and reaction intermediate
H145N
-
95% of wild-type activity, no alteration in KM-value
N130D
-
17% activity compared to the wild type enzyme, the mutant is also active on agmatine, the N130D mutant enzyme is inactive after dialysis against EDTA and assay in the absence of Mn2+
N130Q
-
after dialysis against EDTA and assay in the absence of Mn2+, the wild type-like N130Q mutant enzyme exhibits 50% activity
N149D
-
almost complete loss of activity with L-arginine, gain of activity with agmatine
R308A
site-directed mutagenesis, single mutant R308A changed to a trimeric and kinetically cooperative form, with or without truncation
S230C
with Co2+, about 2fold increase in rate, compared to wild-type
S230D
with Co2+, rate similar to wild-type
S230G
with Co2+, 2fold increase in rate, compared to wild-type
S230T
with Co2+, about 1.5fold increase in rate, compared to wild-type
E288Q
increase in KM value of the E288Q mutant enzyme as compared to wild-type enzyme suggests that substrate binding is significantly affected by the mutation
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
E295A
96% decrease in activity. Residue is not involved in inter-monomer salt bridge
E295A/R404A
95% decrease in activity
E295R
73% decrease in activity
R404A
54% decrease in activity, lack of trimer association. Residue is not involved in inter-monomer salt bridge
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
N130F
site-directed mutagenesis
N130Y
site-directed mutagenesis
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
D199A
in contrast with the Michaelis-Menten kinetics exhibited by the wild-type enzyme, the mutant enzyme exhibits positive cooperativity with respect to L-arginine. Mutation has no effect on the hexameric structure of the enzyme
D199N
in contrast with the Michaelis-Menten kinetics exhibited by the wild-type enzyme, the mutant enzyme exhibits positive cooperativity with respect to L-arginine. Mutation has no effect on the hexameric structure of the enzyme
E256A
in contrast with the Michaelis-Menten kinetics exhibited by the wild-type enzyme, the mutant enzyme exhibits positive cooperativity with respect to L-arginine. Mutation has no effect on the hexameric structure of the enzyme
E256A/E278A
sigmoidal kinetics
E256Q
in contrast with the Michaelis-Menten kinetics exhibited by the wild-type enzyme, the mutant enzyme exhibits positive cooperativity with respect to L-arginine. Mutation has no effect on the hexameric structure of the enzyme
E278A
the mutation compromises interactions at the trimer/trimer interface and yields trimeric species (MW 100000 Da) exhibiting hyperbolic kinetics that changed to sigmoidal by the additional E256A mutation
H141F
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activation by Mn2+
H141F
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mutant enzyme is completely resistant to inactivation by Woodwards reagent K
additional information
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disruption of enzyme structural genes ARGAH1 or ARGAH2 accentuates the increases of transcript levels of basic amino acid transporter BAC1 at germination and of BAC2 two days after germination. Early expression of BAC1 and BAC2 is consistent with the delivery of arginine to the mitochondrial enzyme and the export of ornithine
additional information
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activity is greatly reduced in an argah1-1 null mutant, but not in an argah2-1 null mutant
additional information
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arginase-negative mutants of Arabidopsis exhibit increased nitric oxide signaling in root development. argah1-1 and argah2-1 arginase-negative mutants. Arginase-negative mutant argah1-1 retains about 85% of total arginase activity. NO accumulation is differentially enhanced in argah1-1 and argah2-1 compared with the wild type
additional information
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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
additional information
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construction of the truncated mutant DELTAM1-V23/DELTAH331-I354 showing reduced acivity compared to the wild-type enzyme
additional information
pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I. Certain second-shell mutations can modulate the binding of both the nucleophilic water/hydroxide molecule and substrate or product ligands, resulting in activity greater than that of the wild-type enzyme. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution
additional information
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pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I. Certain second-shell mutations can modulate the binding of both the nucleophilic water/hydroxide molecule and substrate or product ligands, resulting in activity greater than that of the wild-type enzyme. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution
additional information
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enzyme deletion mutant, parasites express no enzymic activity, lack an intracellular ornithine pool, and are auxotrophic for ornithine or polyamines. Expression of a mutant enzyme lacking the glycosomal targeting sequence leads to an enzyme mislocalized to the cytosol and there restoring the polyamine auxotrophy of the deletion mutant
additional information
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OVA/OVA mice, murine models of ovalbumin-induced airway inflammation
additional information
OVA/OVA mice, murine models of ovalbumin-induced airway inflammation
additional information
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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
construction of a N-terminal truncation beginning with K22 and bearing an N-terminal His-tag, i.e. dN-PFA, a similar N-terminal truncation with residues N84-D157 of loop L2 deleted, i.e. dN-PFA-L2S, mutant dN-PFA-H381A, and the dN-PFA-L8 chimera in which loop L8 is replaced with the shorter human arginase I sequence, and analysis of kinetic parameters
additional information
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mutation of H141 to study its role in catalysis
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food industry
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when milk casein is hydrolyzed at 37°C by using commercial digestive enzymes, pancreatin F and protease A, a significant accumulation of L-ornithine in the hydrolysate and the simultaneous disappearance of L-arginine is noted. Transient but distinct arginase activity, which is sufficiently high for L-ornithine production, is detected in the hydrolysate for a certain period during casein hydrolysis. Findings suggest that an inactive precursor of arginase is contaminated in pancreatin F and is proteolytically activated during the incubation
nutrition
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oopherectomized animals treated with 0.5% cholesterol-enriched diet. Diet results in increase in plasma lipids, atheromatous lesions as well as expression of enzyme isoforms arginase I and II and an increase in cellular proliferation. Diet plus supplementation of 17beta-estradiol results in a decrease of atheromatous lesions and reduced expression of both enzyme isoforms and inducible NO synthase
pharmacology
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enzyme is a target for inhibitor design based on arginine analogues with uncharged, tetrahedral functional groups
analysis
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specific detection of NO production in intact mouse tissue, inhibition of enzyme by N-hydroxy-nor-L-arginine to avoid disturbances
analysis
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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
analysis
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assay method based on a combination of moderately selective host-guest binding with the specificity of enzymatic transformations which allows the real-time monitoring of enzymatic reactions in a homogeneous solution. The resulting supramolecular tandem assays exploit the dynamic binding of a fluorescent dye with a macrocyclic host in competition with the binding of the substrate and product. The depletion of the substrate allows the fluorescent dye to enter the macrocycle in the course of the enzymatic reaction, which leads to the desired fluorescence response. For arginase, p-sulfonatocalix[4]arene is used as the macrocycle, which displays binding constants of 6400 per M with arginine, 550 per M with ornithine, and 60 000 per M with the selected fluorescent dye 1-aminomethyl-2,3-diazabicyclo[2.2.2]oct-2-ene, the dye shows a weaker fluorescence in its complexed state, which leads to a switch-off fluorescence response in the course of the enzymatic reaction. Assays can be successfully used to probe the inhibition of enzymes
analysis
development of a high-throughput semiquantitative assay system using a colorimetric 96-well plate assay to monitor the formation of urea. The assay has a dynamic range of about 5-300 microM for the ureido product
drug development
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the application of rhArg-PEG alone or in combination with existing chemotherapeutic drugs may represent a specific and effective therapeutic strategy against human hepatocellular carcinoma
drug development
arginase catalyzes the first committed step in the biosynthesis of polyamines that enable cell growth and hence potential drug target for the treatment of leishmaniasis
medicine
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enzyme is a target for inhibitors used in therapeutic treatment of smooth muscle disorders, such as erectile dysfunction
medicine
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agents that elevate cAMP level significantly enhance induction of enzyme by cytokines. Consequences of increased enzyme expression should be evaluated when phosphodiesterase inhibitors are used for treatment of inflammatory disorders in which IL-4 and/or TGF-beta predominate
medicine
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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
medicine
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H2O2 specifically impairs endothelium-dependent NO-mediated dilation of coronary microvessels by reducing L-arginine availability through upregulation of enzyme
medicine
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in coronary arteriole, enzyme activity increases twofold with hypertension. Inhibition of enzyme activity by Nomega-hydroxy-nor-L-arginine or incubation with L-arginine partially restores NO release and dilation to adenosine in hypertrophic vessels
medicine
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oopherectomized animals treated with 0.5% cholesterol-enriched diet. Diet results in increase in plasma lipids, atheromatous lesions as well as expression of enzyme isoforms arginase I and II and an increase in cellular proliferation. Diet plus supplementation of 17beta-estradiol results in a decrease of atheromatous lesions and reduced expression of both enzyme isoforms and inducible NO synthase. Inhibiton of enzyme expression by 17beta-estradiol as mechanism in attenuating atherogenensis
medicine
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patients with cystic fibrosis, before and after 14 days of antibiotic treatment for pulmonary exacerbation. Systemic enzyme levles are significantly increased in cystic fibrosis with exacerbation. Enzyme levels normalize with antibiotic treatment. Plasma L-arginine is reduced before, but not after treatment, L-ornithine, L-proline, and L-glutamic acid are normal before and increased after treatment
medicine
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plasma arginase activity is significantly elevated in patients with sickle cell disease, with highest activity found in patients with secondary pulmonary hypertension. Arginase activity correlates with the arginine-ornithine ratio, and lower ratios are associated with greater severity of pulmonary hypertension and with mortality. Increased plasma enzyme activity is correlated with increased intravascular hemolytic rate and, to a lesser extent, with markers of inflammation and soluble adhesion molecule levels
medicine
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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
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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
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targeting vascular arginase as a therapeutic possibility for atherosclerosis. Thrombin enhances enzyme activity via small G-protein RhoA/ROCK in endothelial cells
medicine
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overexpression of arginase in the penis contributes to erectile dysfunction
medicine
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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
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enzyme serves as a therapeutic target for the treatment of asthma, erectile dysfunction, and atherosclerosis
medicine
enzyme serves as a therapeutic target for the treatment of asthma, erectile dysfunction, and atherosclerosis
medicine
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new forms of efficient arginase inhibitors, could be useful as therapeutic regimen in hemoglobinopathies and other related inflammation-mediated diseases
medicine
a significant decrease in arginase activity, dependent of the liver clinical stage, is observed in cirrhotic tissue. Arginase AI activity and its mRNA level are significantly decreased in cirrhotic liver, whereas the activity and expression of arginase AII are concurrently raised, as compared to normal liver
medicine
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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
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both ARG1 and ARG2 are expressed by hormone-sensitive and hormone-refractory prostate cancer cell lines, with the LNCaP cells having the highest arginase activity. In prostate tissue samples, ARG2 is more expressed in normal and non-malignant prostatic tissues compared to tumor tissues. Following androgen stimulation of LNCaP cells with 10 nM R1881, both ARG1 and ARG2 are overexpressed. The regulation of arginase expression following androgen stimulation is dependent on the androgen receptor. This observation is correlated in vivo in patients by immunohistochemistry. Patients treated by androgen-deprivation therapy prior to surgery have lower ARG2 expression in both nonmalignant and malignant tissues. ARG1 and ARG2 are enzymatically active and their decreased expression by siRNA results in reduced overall arginase activity and L-arginine metabolism. The decreased ARG1 and ARG2 expression also translates with diminished LNCaP cells cell growth and increased peripheral blood mononuclear cell activation following exposure to LNCaP cells conditioned media. Interleukin-8 is also upregulated following androgen stimulation and it directly increases the expression of ARG1 and ARG2 in the absence of androgens
medicine
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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
medicine
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comparison of the infectivity of arg- and wild-type Plasmodium berghei by inoculation of mice using sporozoites dissected from mosquito salivary glands shows a significant reduction in infectivity in the arg- strain 40 h postinfection
medicine
Co2+ substitution of the Mn2+ metal cofactor confers more than 10fold higher catalytic activity and 5fold greater stability. Based on the hypothesis that the Co-ArgI enzyme would decrease tumor burden by systemic elimination of L-arg in a murine model, Co-hArgI was conjugated to 5-kDa PEG to enhance circulation persistence and applied as monotherapy for hepatocellular carcinoma and pancreatic carcinoma in vitro and in vivo murine xenografts. Weekly treatment of 8 mg/kg Co-hArgI-PEG effectively controls human HepG2 and Panc-1 tumor xenografts. Both cell lines underwent apoptosis in vitro with significant increased expression of activated caspase-3 and showed evidence of autophagy in vitro and in vivo
medicine
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exposure to ONOO- generator SIN-1 or to H2O2 increases arginase I expression and arginase activity by 35% and 50%, respectively, which is prevented by ROCK inhibitor, Y-27632, PKC inhibitor, Gö6976 or siRNA to p115-Rho GEF. The oxidative species ONOO- and H2O2 increase arginase activity/expression through PKC-mediated activation of RhoA/Rho kinase pathway
medicine
inhibition of Leishmania arginase leads to a decrease in parasite growth and infectivity and thus represents an attractive therapeutic strategy
medicine
Leishmania arginase is a potential drug target for the treatment of leishmaniasis because this binuclear manganese metalloenzyme initiates de novo polyamine biosynthesis by catalyzing the hydrolysis of L-arginine to generate L-ornithine and urea. The product L-ornithine subsequently undergoes decarboxylation to yield putrescine, which in turn is utilized for spermidine biosynthesis. Polyamines such as spermidine are essential for the growth and survival of the parasite, so inhibition of enzymes in the polyamine-biosynthetic pathway comprises an effective strategy for treating parasitic infections
medicine
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overexpression of arginase in the penis contributes to erectile dysfunction
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synthesis
the enzyme can be used to produce L-ornithine from L-arginine
synthesis
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the enzyme can be used to produce L-ornithine from L-arginine
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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