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Information on EC 3.5.3.18 - dimethylargininase
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3.5.3.18 dimethylargininaseIUBMB Comments
Also acts on Nomega-methyl-L-arginine.
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Word Map
- 3.5.3.18
- endothelial
- cardiovascular
- artery
- hypertension
- angiotensin
- l-citrulline
- aortic
-
umbilical
-
vasodilation
- vein
-
endothelium-dependent
- dimethylamine
- atherosclerosis
- coronary
-
methylarginines
- ng,ng-dimethylarginine
- homocysteine
- medicine
- huvecs
-
endothelium-derived
- hyperhomocysteinemia
- nnos
-
l-nmma
-
ii-induced
- ng-monomethyl-l-arginine
-
monomethylarginine
-
ox-ldl
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
ddah1, dimethylarginine dimethylaminohydrolase, ddah2, ddah-1, ddah-2, dimethylaminohydrolase, dimethylarginine dimethylaminohydrolase 1, dimethylargininase, human ddah-1, ddah-i, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DDAH
DDAH-1
DDAH-2
DDAH1
DDAH2
DDAHI
-
-
-
-
DDAHII
-
-
-
-
Dimethylargininase
-
-
-
-
dimethylarginine dimethylaminohydrolase
dimethylarginine dimethylaminohydrolase 1
dimethylarginine dimethylaminohydrolase-2
G6a
-
-
-
-
DDAH
-
-
-
-
DDAH-2
isozyme, mainly present in vascular tissues that co-express endothelial nitric oxide synthases
dimethylarginine dimethylaminohydrolase
-
-
-
-
dimethylarginine dimethylaminohydrolase
-
-
dimethylarginine dimethylaminohydrolase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Nomega,Nomega'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of linear amidines
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Nomega,Nomega'-dimethyl-L-arginine dimethylamidohydrolase
Also acts on Nomega-methyl-L-arginine.
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CAS REGISTRY NUMBER
COMMENTARY
123644-75-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N5-(methoxycarbamimidoyl)-L-ornithine + H2O
L-citrulline + ?
-
assay at 37°C, 30 min, pH 7.4
-
-
?
N5-(methylcarbamimidoyl)-L-ornithine + H2O
L-citrulline + ?
-
assay at 37°C, 30 min, pH 7.4
-
-
?
N5-[2,5-dihydro-1H-pyrrol-1-yl(imino)methyl]-L-ornithine + H2O
L-citrulline + ?
-
assay at 37°C, 30 min, pH 7.4
-
-
?
NG,NG-dimethyl-L-homoarginine + H2O
?
-
at 2.8% of the activity with NG,NG-dimethyl-L-arginine
-
-
?
Nomega,Nomega'-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
?
Nomega,Nomega-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
?
Nomega-monomethyl-L-arginine + H2O
L-citrulline + methylamine
-
-
-
?
dimethyl-L-arginine + H2O
L-citrulline + dimethylamine
-
4 mM, pH 6.5, 37°C, 2 h incubation time
-
-
?
dimethyl-L-arginine + H2O
L-citrulline + dimethylamine
-
-
-
?
N,N-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
37°C, 2 h, pH 6.0
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme is involved in regulation of the levels of the natural occuring free arginine derivatives L-Nomega,Nomega-dimethylarginine and L-Nomega-methylarginine, which are reversible inhibitors of nitric oxide synthase
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the key role of dimethylarginine dimethylaminohydrolase may be to ensure that under normal conditions the levels of methylarginines are kept low throughout the whole cell
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays an integral role in arginine handling
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the enzyme plays a functional role in the regulation of nitric oxide synthase
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the enzyme might play a role as a regulator of nitric oxide generation in human tissues
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays an integral role in arginine handling
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
ir
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays an integral role in arginine handling
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays a role in metabolism of NG,NG-dimethyl-L-arginine
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the enzyme plays a functional role in the regulation of nitric oxide synthase
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
L-citrulline + dimethylamine
-
-
-
-
?
NG-monomethyl-L-arginine + H2O
citrulline + methylamine
-
at 61% of the activity with NG,NG-dimethyl-L-arginine
-
-
?
Ngamma-monomethyl-L-arginine + H2O
L-citrulline + methylamine
-
-
-
?
Ngamma-monomethyl-L-arginine + H2O
L-citrulline + methylamine
-
-
-
?
Ngamma-monomethyl-L-arginine + H2O
L-citrulline + methylamine
-
-
-
-
?
Ngamma-monomethyl-L-arginine + H2O
L-citrulline + methylamine
-
-
-
?
S-methyl-L-thiocitrulline + H2O
L-citrulline + methanethiol
-
-
-
?
S-methyl-L-thiocitrulline + H2O
L-citrulline + methanethiol
-
-
-
?
S-methyl-L-thiocitrulline + H2O
L-citrulline + methanethiol
-
-
-
?
additional information
?
-
no hydrolysis of NG,NG-dimethyl-L-arginine
-
-
?
additional information
?
-
-
incapable of hydrolyzing peptide incorporated methylarginines
-
-
?
additional information
?
-
no substrate: S-ethyl-2-thiopseudourea, S-ethyl-N-phenylisothiourea and phenylene-1,3-bis(ethane-2-isothiourea)
-
-
?
additional information
?
-
-
no substrate: S-ethyl-2-thiopseudourea, S-ethyl-N-phenylisothiourea and phenylene-1,3-bis(ethane-2-isothiourea)
-
-
?
additional information
?
-
bad substrates are creatine, creatinine, argininosuccinate, guanidinoacetate, L-homoarginine, L-canvanine
-
-
?
additional information
?
-
-
bad substrates are creatine, creatinine, argininosuccinate, guanidinoacetate, L-homoarginine, L-canvanine
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Nomega,Nomega'-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme is involved in regulation of the levels of the natural occuring free arginine derivatives L-Nomega,Nomega-dimethylarginine and L-Nomega-methylarginine, which are reversible inhibitors of nitric oxide synthase
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the key role of dimethylarginine dimethylaminohydrolase may be to ensure that under normal conditions the levels of methylarginines are kept low throughout the whole cell
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays an integral role in arginine handling
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the enzyme plays a functional role in the regulation of nitric oxide synthase
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the enzyme might play a role as a regulator of nitric oxide generation in human tissues
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays an integral role in arginine handling
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays an integral role in arginine handling
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
enzyme plays a role in metabolism of NG,NG-dimethyl-L-arginine
-
-
?
NG,NG-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
the enzyme plays a functional role in the regulation of nitric oxide synthase
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
Zn2+ binding to DDAH-1 protects the enzyme from S-nitrosylation by free nitric oxide
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-chloroacetamidine
irreversible inhibition in a time- and concentration-dependent manner
2-hydroxymethyl-4-chloropyridine
-
solution studies support an inactivation mechanismin in which the active site Asp66 residue stabilizes the pyridinium form of the inactivator, which has enhanced reactivity toward the active site Cys, resulting in covalent bond formation, loss of the halide, and irreversible inactivation
4-hydroxy-nonenal
-
dose-dependently inhibits DDAH activity with 15% inhibition at 0.01 mM and complete inhibition at 0.5 mM
angiotensin II
1 microM, about 55% relative activity; 1 microM, about 55% relative activity
aprotinin inhibitor
-
NG,NG-dimethyl-L-arginine release from freeze-thaw whole blood 34% inhibited
-
darbepoetin alpha
-
inhibits DDAH in a dose dependent manner, inhibition of DDAH is abolished by incubation with EPO antibody or with antioxidant pyrrolidine dithiocarbamate
-
epoetin beta
-
inhibits DDAH in a dose dependent manner, inhibition of DDAH is abolished by incubation with EPO antibody or with antioxidant pyrrolidine dithiocarbamate
-
erythropoetin
200 units/ml, about 75% relative activity; 200 units/ml, about 75% relative activity
-
iodoacetamide
-
pH dependent DDAH inactivation, addition of 2.5 mM NG-methyl-L-arginine at pH 8.5 can prevent inactivation by idoacetamide, inactivation may be due to modification at the active site of DDAH, inactivation increases at higher pH values
leupeptin
-
NG,NG-dimethyl-L-arginine release from freeze-thaw whole blood 55% inhibited
lipopolysaccharide
1 microg/ml, 24 h, about 55% relative activity; 1 microg/ml, about 55% relative activity
monocrotaline
-
DDAH activity and DDAH1, but not DDAH2, protein expression are significantly reduced after 60mg/kg monocrotaline treatment
N-(2-methoxyethyl)-L-arginine
complete inhibition at 100 microM; complete inhibition at 100 microM
N-(but-3-yn-1-yl)-2-chloroethanimidamide
-
click chemistry mediated in vivo activity probe that labels the active fraction of DDAH-1 in intact mammalian cells and that can be blocked by the presence of competitive reversible and irreversible inhibitors
N5-(1-iminopropyl)-L-ornithine
crystallization data. Reversible competitive inhibition, consistent with a reversible covalent mode of DDAH inhibition by alkylamidine inhibitors
nitroglycerine
10 microM, 16 h, about 55% relative activity; 10 microM, about 55% relative activity
PD 404182
i.e. 6H-6-imino-(2,3,4,5-tetrahydropyrimido)[1,2-c]-[1,3]benzothiazine, potent active-site competitive inhibitor, about 75% inhibition at 0.05 mM
pentafluorophenyl sulfonates
-
between 30-76% DDAH inhibition depending on molecular structure of the pentafluoropenyl sulfonate
-
PMSF
-
NG,NG-dimethyl-L-arginine release from freeze-thaw whole blood 57% inhibited
protease inhibitor
-
NG,NG-dimethyl-L-arginine release from freeze-thaw whole blood 25-85% inhibited
-
S-2-amino-4-[N-(2-methoxyethyl)guanidino]butanoic acid benzyl ester
-
S-nitroso-L-cysteine
9-15% inhibition of the zinc-free enzyme at 0.5 mM, S-nitrosylation of the active site Cys273 in DDAH-1
2-(N,N-dimethylamino)-diazenolate-2-oxide
-
S-nitrosylation of apo-enzyme, holo-enzyme resists, reaction with two of five Cys-residues
2-(N,N-dimethylamino)-diazenolate-2-oxide
-
i.e. DEANONOate, inhibition by S-nitrosylation, reversed by dithiothreitol
2-(N,N-dimethylamino)-diazenolate-2-oxide
-
i.e. DEANONOate, inhibition by S-nitrosylation, reversed by dithiothreitol
2-(N,N-dimethylamino)diazenolate-2-oxide
1 mM, 50% inhibition of DDAH-1
2-(N,N-dimethylamino)diazenolate-2-oxide
1 mM, 50% inhibition of DDAH-1; 1 mM, 50% inhibition of DDAH-1
2-(N,N-dimethylamino)diazenolate-2-oxide
1 mM, 50% inhibition of DDAH-1
2-amino-4-(NG-methyl-guanidino)butanoic acid
-
incubation of lysed red blood cells, dose dependent inhibition of NG,NG-dimethyl-L-arginine degradation with the highest dose (1 mM) reversing the pattern to a net increase in NG,NG-dimethyl-L-arginine concentration for the 1- and 3h time points
2-amino-4-(NG-methyl-guanidino)butanoic acid
-
a series of analogues designed, reversible DDAH inhibitors
homocysteine
-
inhibition of the expression of DDAH-2 reduces the NO production induced by IL-1beta
L-arginine
-
0.1 mM L-arginine competitively inhibits DDAH enzyme activity to 5.6%
lysophosphatidylcholine
-
activity is significantly decreased in cells treated with lysophosphatidylcholine (0.005 mg/ml) for 48 h, 0.001-0.005 mM probucol or 0.001 mM pyrrolidindithiocarbamate significantly attenuate inhibition of DDAH activity by lysophosphatidylcholine
N-nitro-L-arginine methylester
1 mM, 1 h, 47.1% relative activity; 1mM, 1 h, 47.1% relative activity
oxidized-low density lipoprotein
-
activity is significantly decreased in cells treated with oxidized-low density lipoprotein (0.1 mg/ml) for 48 h, 0.001-0.005 mM probucol or 0.001 mM pyrrolidindithiocarbamat significantly attenuate inhibition of DDAH activity by oxidized-low density lipoprotein
-
peroxynitrite
-
inhibition of 15% after exposure to peroxynitrite at concentrations ranging from 0.01-0.1 mM, 25% inhibition at 1 mM
S-nitroso-L-homocysteine
96% inhibition of the zinc-free enzyme at 0.5 mM, leads to the unique formation of an N-thiosulfoximide
Zn2+
-
one mol per mol of enzyme, apo-enzyme is active, holoenzyme is activated by removal of Zn2+
Zn2+
-
incubation of lysed red blood cells, diminished hydrolyis of NG,NG-dimethyl-L-arginine by addition of physiologically relevant concentrations (0.02 mM)
additional information
5 mM of L-cysteine, L-homocysteine, glutathione, dithiothreitol, or Tris(2-carboxyethyl)phosphine-HCl for 30 min at 37°C cannot restore inhibited activity, suggesting that the covalent product N-thiosulfoximide will remain stable under the reducing conditions present in the cytosol
-
additional information
-
exposure to pathophysiological levels of reactive oxygen has little to no effect on the activity of the enzyme
-
additional information
S-ethyl-2-thiopseudourea, S-ethyl-N-phenylisothiourea and phenylene-1,3-bis(ethane-2-isothiourea) do not inhibit DDAH-1 at concentrations below 1 mM
-
additional information
-
S-ethyl-2-thiopseudourea, S-ethyl-N-phenylisothiourea and phenylene-1,3-bis(ethane-2-isothiourea) do not inhibit DDAH-1 at concentrations below 1 mM
-
additional information
-
tissue-specific decrease of levels of Ddah1 and Ddah2 RNA after feeding a high-methionine/low-folate diet for 5 to 11 month
-
additional information
-
incubation of lysed red blood cells with EDTA or glucose failed to attenuate the degradation of NG,NG-dimethyl-L-arginine, incubation of whole blood cells with arginine methyltransferase inhibitors does not reduce NG,NG-dimethyl-L-arginine release
-
additional information
-
probucol or pyrrolidindithiocarbamate itself have no effect on the activity of DDAH
-
additional information
-
decrease of DDAH-2 mRNA level induced by 10% serum, ionomycin or endothelial growth factors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
all-trans-retinoic acid
1.9fold increase in DDAH-2 mRNA and protein expression
D-histidine
-
activating ability in decreasing order: histamine, imidazole, L-histidine, D-histidine
histamine
-
activating ability in decreasing order: histamine, imidazole, L-histidine, D-histidine
imidazole
-
activating ability in decreasing order: histamine, imidazole, L-histidine, D-histidine
L-histidine
-
activating ability in decreasing order: histamine, imidazole, L-histidine, D-histidine
pioglitazone
2-3fold increase of DDAH-2 mRNA and protein levels
SNAP
-
increase of DDAH-2 mRNA and protein level, time and concentration dependent
-
visfatin
-
mRNA and protein expression of DDAH2 upregulated after 24 h stimulation of visfatin
-
interleukin-1beta
2fold increase in DDAH-1 protein expression
-
additional information
-
type of buffer dramatically influences enzyme activity, activity in imidazole/HCl buffer is about 25% higher than in phosphate buffer
-
additional information
-
probucol and the intracellular antioxidant pyrrolidine dithiocarbamate significantly attenuate inhibition of endothelial DDAH activity by oxidized-low density lipoprotein or lysophosphatidylcholine, but probucol or PDTC itself had no effect on the activity of DDAH
-
additional information
-
mRNA expression levels of DDAH-I are not changed in pioglitazone-treated rats
-
additional information
-
increase of DDAH-2 mRNA and protein level induced by SNAP, NOR, 8-bromo-cGMP or CNP
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.161
N5-[2,5-dihydro-1H-pyrrol-1-yl(imino)methyl]-L-ornithine
-
37°C, 30 min, pH 7.4
0.11
Nomega,Nomega-dimethyl-L-arginine
wild-type, pH 7.3, temperature not specified in the publication
0.75
Nomega,Nomega-dimethyl-L-arginine
mutant L271G, pH 7.3, temperature not specified in the publication
1.4
Nomega,Nomega-dimethyl-L-arginine
mutant L30A, pH 7.3, temperature not specified in the publication
13.7
Nomega,Nomega-dimethyl-L-arginine
mutant E78A, pH 7.3, temperature not specified in the publication
0.0014
S-methyl-L-thiocitrulline
mutant L271G, pH 7.3, temperature not specified in the publication
0.0031
S-methyl-L-thiocitrulline
wild-type, pH 7.3, temperature not specified in the publication
0.0036
S-methyl-L-thiocitrulline
mutant L30A, pH 7.3, temperature not specified in the publication
0.019
S-methyl-L-thiocitrulline
mutant E78AA, pH 7.3, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
Nomega,Nomega-dimethyl-L-arginine
mutant E78A, pH 7.3, temperature not specified in the publication
0.0087
Nomega,Nomega-dimethyl-L-arginine
mutant L271G, pH 7.3, temperature not specified in the publication
0.014
Nomega,Nomega-dimethyl-L-arginine
wild-type, pH 7.3, temperature not specified in the publication
0.0163
Nomega,Nomega-dimethyl-L-arginine
mutant L30A, pH 7.3, temperature not specified in the publication
0.0097
S-methyl-L-thiocitrulline
mutant L271G, pH 7.3, temperature not specified in the publication
0.03
S-methyl-L-thiocitrulline
mutant E78AA, pH 7.3, temperature not specified in the publication
0.042
S-methyl-L-thiocitrulline
mutant L30A, pH 7.3, temperature not specified in the publication
0.042
S-methyl-L-thiocitrulline
wild-type, pH 7.3, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00012
Nomega,Nomega-dimethyl-L-arginine
mutant E78A, pH 7.3, temperature not specified in the publication
0.0115
Nomega,Nomega-dimethyl-L-arginine
mutant L271G, pH 7.3, temperature not specified in the publication
0.0116
Nomega,Nomega-dimethyl-L-arginine
mutant L30A, pH 7.3, temperature not specified in the publication
0.127
Nomega,Nomega-dimethyl-L-arginine
wild-type, pH 7.3, temperature not specified in the publication
1.58
S-methyl-L-thiocitrulline
mutant E78AA, pH 7.3, temperature not specified in the publication
6.83
S-methyl-L-thiocitrulline
mutant L271G, pH 7.3, temperature not specified in the publication
11.7
S-methyl-L-thiocitrulline
mutant L30A, pH 7.3, temperature not specified in the publication
13.55
S-methyl-L-thiocitrulline
wild-type, pH 7.3, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.606
(2S)-2-amino-5-[N'-(3,3,3-trifluoropropyl)carbamimidamido]pentanoic acid
-
pH 7.4, 37°C
0.013
(2S)-2-amino-5-[N'-(3-methoxypropyl)carbamimidamido]pentanoic acid
-
pH 7.4, 37°C, inhibitor is selective over NOS and over arginase
0.764
(2S)-2-amino-5-[N'-(4-amino-4-oxobutyl)carbamimidamido]pentanoic acid
-
pH 7.4, 37°C
0.058
(2S)-2-amino-5-[N'-(but-3-en-1-yl)carbamimidamido]pentanoic acid
-
pH 7.4, 37°C
0.017
(2S)-2-amino-5-[N'-(but-3-yn-1-yl)carbamimidamido]pentanoic acid
-
pH 7.4, 37°C
1.968
(2S)-2-amino-5-[N'-(nitromethyl)carbamimidamido]pentanoic acid
-
pH 7.4, 37°C
0.057
(2S)-2-amino-5-[N'-(pent-4-en-1-yl)carbamimidamido]pentanoic acid
-
pH 7.4, 37°C
0.69
S-nitroso-L-homocysteine
in the presence of 5 mM EDTA, at pH 7.3 and 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
N-(but-3-yn-1-yl)-2-chloroethanimidamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.99
N5-(1-iminoethyl)-L-ornithine
Homo sapiens
pH 7.3, temperature not specified in the publication
0.11
N5-(1-iminohexyl)-L-ornithine
Homo sapiens
pH 7.3, temperature not specified in the publication
0.0075
N5-(1-iminopentyl)-L-ornithine
Homo sapiens
pH 7.3, temperature not specified in the publication
0.052
N5-(1-iminopropyl)-L-ornithine
Homo sapiens
pH 7.3, temperature not specified in the publication
0.075
S-nitroso-L-homocysteine
Bos taurus
in 50 mM HEPES/NaOH (pH 7.3), 150 mM KCl, and 5 mM EDTA for 30 min at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.9
-
mice fed the high-methionine/low folate diet, heterozygous cystathionine beta-synthase
1.1
-
mice fed the high-methionine/low folate diet, homozygous cystathionine beta-synthase
additional information
additional information
-
different values in different tissues: value between 10 and 12 micromol/min/mg in myocardium, value between 1.9 and 2.3 micromol/min/mg in skeletal muscle, value between 25 and 40 micromol/min/mg in kidney, value between 4.5 and 9.5 in liver
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
6.5
additional information
-
type of buffer dramatically influences enzymatic activity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
288967, 288968, 288970, 288972, 653681, 667155, 667355, 668175, 669059, 685205, 686018, 686991, 687644
-
-
brenda
transgenic mouse model with oxerexpressed human dimethylarginine dimethylaminohydrolase
-
-
brenda
C57BL/6J, after tretmend with an NOS inhibitor used as a model of chronic nitric oxide expression
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
both DDAHI and DDAHII proteins are detected in peri-infarct cardiomyocytes, while DDAHII immunoreactivity is additionally localized to infiltrating inflammatory cells and blood vessels in the healing infarct. Both plasma and left ventricular concentrations of the DDAH substrate, ADMA, are increased post-myocardial infarction
brenda
-
DDAH-2 protein expression is higher in osteoarthritic cartilage than in normal cartilage
brenda
-
in healthy hearts, DDAHI is absent, and DDAHII is localized to endothelium and endocardium with a similar distribution to that of eNOS
brenda
-
DDAHII immunoreactivity is localized to infiltrating inflammatory cells and blood vessels in the healing infarct
brenda
-
normal human chondrocytes are isolated from knee cartilage obtained
brenda
-
both DDAH1 and 2 are expressed in the developing limb buds in patterns overlapping areas with high nitric oxide synthase activity
brenda
additional information
-
DDAHII immunoreactivity is localized to infiltrating inflammatory cells and blood vessels in the healing infarct
brenda
-
entire ventricular zone and tegmentum, ciliarly ganglion, inferior olive, interpeduncular nucleus, red nucleus, dorsal tegmental nucleus and nuclues of the lateral lemniscus
brenda
-
human microvascular and ubilical vein endothelial cells
brenda
-
coronary microvessels, arteries and veins, strong staining
brenda
-
in healthy hearts, DDAHI is absent, and DDAHII is localized to endothelium and endocardium with a similar distribution to that of eNOS
brenda
-
DDAH1 RNA is expressed in the left ventricle, cardiac outflow tract and developing vasculature. DDAH2 expression is seen in the developing left ventricle and cardiac outflow tract, and additionally in the peripheral nervous system
brenda
-
in healthy hearts, DDAHI is absent, and DDAHII is localized to endothelium and endocardium with a similar distribution to that of eNOS
brenda
-
in the serosa of and in the boundary between the smooth muscle and submucosa
brenda
expression of mRNA for DDAH-1 is 7fold higher in the liver compared to DDAH-2
brenda
DDAH I is highly expressed, low level expression of DDAH II
brenda
expression of mRNA for DDAH-1 is 2fold higher in the renal cortex compared to DDAH-2
brenda
-
DDAH-1 mRNA expression is especially strong in the ventral horn and dorsal root ganglion, and also localized in cervical, thoracic and lumbar spinal cord and sympathetic ganglion
brenda
-
in the gray matter, especially in the ventral portion and sympathetic ganglion
brenda
-
overexpression in the immortalized cell line
brenda
additional information
DDAH I predominates in tissues that express neuronal nitric oxide synthase, DDAH II predominates in tissues expressing endothelial nitric oxide synthase
brenda
additional information
-
DDAH I predominates in tissues that express neuronal nitric oxide synthase, DDAH II predominates in tissues expressing endothelial nitric oxide synthase
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
conventional immunofluorescence and confocal microscopy reveal the presence of DDAH-2 in the mitochondria of IL-1beta-stimulated chondrocytes. Blocking the translocation to mitochondria reduces the NO production induced by IL-1beta
brenda
-
no specific association with organelles or with plasma membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
DDAH1 knockout impairs endothelial sprouting from cultured aortic rings, and overexpression of constitutively active Akt or DDAH1 rescues endothelial sprouting in the aortic rings from these mice
malfunction
-
plasma and tissue asymmetrical dimethylarginine (ADMA) and N-monomethyl-L-arginine (L-NMMA) levels in DDAH1-/- mice are several folds higher than in wild-type mice, but growth and development of these knockout mice are similar to wild-type. Although the expression of DDAH2 is unaffected, DDAH activity is undetectable in all tissues tested. Results indicate that DDAH1 is the critical enzyme for ADMA and L-NMMA degradation
malfunction
-
using selective gene silencing of DDAH1 with small interfering RNA and overexpression of DDAH1 in HUVEC, it is shown that DDAH1 acts to promote endothelial cell proliferation, migration and tube formation both by Akt phosphorylation as well as through the traditional role of degrading ADMA. DDAH1 overexpression increases Ras activity
physiological function
-
heterozygous DDAH1 embryos express DDAH1 RNA and protein at approximately 50% of wild-type levels, while circulating plasma asymmetric dimethylarginine levels of heterozygotes are about 20% higher than those of wild-type mice. Homozygous DDAH1 null embryos are generated at low frequency, and do not progress through embryonic development. Mice carrying an inactivated DDAH2 locus have reduced DDAH2 expression at both the RNA and protein levels in all tissues studied. Breeding of these mice indicates that both heterozygous and homozygous inactivation of the DDAH2 locus does not impact on embryonic survival, with wild type, heterozygous and null mice produced in Mendelian ratios
physiological function
overexpression of DDAH-1 increases endothelial nitric oxide by 24%. Small interfering RNA-mediated down-regulation of DDAH-1 reduces nitric oxide bioavailability by 27%. The reduction in nitric oxide production following DDAH-1 gene silencing is associated with a 48% reduction in L-Arg/asymmetric dimethylarginine and is partially restored with L-Arg supplementation
physiological function
overexpression of DDAH-2 increases endothelial nitric oxide by 18%. Small interfering RNA-mediated down-regulation of DDAH-2 reduces nitric oxide bioavailability by 57%. L-Arg and asymmetric dimethylarginine are unchanged in the DDAH-2-silenced cells, and L-Arg supplementation has no effect on nitric oxide
physiological function
-
results from this animal model of prolonged critical illness show that DDAH activities in several organs in concert determine plasma levels of ADMA, confirming that DDAH is an important player in the regulation of circulatory ADMA
physiological function
human DDAH1 overexpression does not protect against hypertension-induced cardiac fibrosis and hypertrophy. In addition, the hypertension-induced impairment of the endothelium-dependent vasorelaxation of aortic segments ex vivo is not significantly attenuated by DDAH1 overexpression. However, human DDAH1 overexpressing mice display an attenuated hypertensive inflammatory response in renal tissue, resulting in less hypertensive renal injury
physiological function
DDAH2 increases expression of endothelial nitric oxide synthase (eNOS), inducing proliferation and capillary-like tube formation of vascular endothelial cells. eNOS shows higher expression in invasive adenocarcinoma than in adenocarcinoma in situ and normal lung, similarly to DDAH2
physiological function
global knockout of Ddah2 results in elevated blood pressure during periods of activity and changes in vascular responsiveness mediated by changes in methylarginine concentration, and systemic nitric oxide concentrations. In a model of severe polymicrobial sepsis, Ddah2 knockout affects outcome. Monocyte-specific deletion of Ddah2 results in a similar pattern of increased severity to that seen in globally deficient animals
physiological function
in mice specifically lacking Ddah1 expression in endothelial cells, plasma asymmetrical dimethylarginine level is unchanged, and cultured aortas release amounts of asymmetrical dimethylarginine to similar to controls. Vasoreactivity ex vivo and hemodynamics in vivo are unaltered in endothelial DDAH1 mutant mice, while angiogenic responses both ex vivo and in vivo are significantly impaired
physiological function
Pseudomonas aeruginosa can utilize asymmetric dimethyl-L-arginine as a sole source of nitrogen but not carbon. Expression of the DdaH gene is induced in the presence of methylarginines, including NG-monomethyl-L-arginine and asymmetric dimethyl-L-arginine. Induction of the DdaH gene is achieved via the putative enhancer-binding protein PA1196 and the alternative sigma factor RpoN. Both PA1196 and RpoN are essential for the expression of the DdaH gene in response to methylarginines
Show AA Sequence and Transmembrane Helices (2707 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30500
34000
40000
30500
calculated from the protein sequence of wild-type DDAH, after removal of the N-terminal methionine residue
30500
deconvoluted mass spectrum of a control reaction mixture that included wild-type DDAH but no inactivator
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 29000, dynamic equilibrium between monomer and homodimer, hydrodynamic measurements
homodimer
PaDDAH exists in dynamic equilibrium between symmetric homodimer and monomer states
monomer
monomer
1 * 29000, dynamic equilibrium between monomer and homodimer, hydrodynamic measurements
monomer
PaDDAH exists in dynamic equilibrium between monomer and symmetric homodimer states
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by sitting drop vapor diffusion, at 1.08-2.0 A resolution and at pH 6.3 and pH 9.0
N5-(1-iminopropyl)-L-ornithine:DDAH-1 complex, to 1.9 A resolution, covalent bond formation between the inhibitors amidino carbon and the active-site Cys274, and solution studies show reversible competitive inhibition, consistent with a reversible covalent mode of DDAH inhibition by alkylamidine inhibitors
A 2.18 A resolution X-ray crystal structure of the inactivated complex elucidates the orientation of the inactivator and its covalent attachment to the active site Cys
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C274A
C249S
D244N
-
wild type and D244N DDAH variants both form covalent adducts upon incubation with 2-hydroxymethyl-4-chloropyridine, showing mass additions that are consistent with covalent attachment of one equivalent of hydroxymethylpyridine to each enzyme. These results also indicate that Asp244 is not essential for covalent modification to occur
D66N
-
the C249S mutant and D66N mutant are both incapable of forming a covalent adduct when incubated with 2-hydroxymethyl-4-chloropyridine
E33H
weakening of the homodimer interaction observed for wild type protein, expressed in Escherichia coli at levels similar to the wild type
E33Q
weakening of the homodimer interaction observed for wild type protein, expressed in Escherichia coli at levels similar to the wild type
H162G
N36D
expressed in Escherichia coli at levels similar to the wild type
N36H
weakening of the homodimer interaction observed for wild type protein, expressed in Escherichia coli at levels similar to the wild type
N36W
more stable homodimer than the wild type protein, expressed in Escherichia coli at levels similar to the wild type
Q43H
weakening of the homodimer interaction observed for wild type protein, expressed in Escherichia coli at levels similar to the wild type
Q43R
weakening of the homodimer interaction observed for wild type protein, expressed in Escherichia coli at levels similar to the wild type
R40E
weakening of the homodimer interaction observed for wild type protein, expressed in Escherichia coli at levels similar to the wild type
R40E-R98H
exclusively monomeric, expressed in Escherichia coli at levels similar to the wild type
R40W
not expressed in Escherichia coli at levels similar to the wild type
R98H
weakening of the homodimer interaction observed for wild type protein, expressed in Escherichia coli at levels similar to the wild type
R98N
not expressed in Escherichia coli at levels similar to the wild type
S248N
-
mutant is still capable of substrate turnover and is still inactivated by 2-hydroxymethyl-4-chloropyridine with a second order inactivation rate constant that is approximately 2fold less than wild type DDAH
C274A
-
inactive and is not labeled by inhibitor N-(but-3-yn-1-yl)-2-chloroethanimidamide
C249S
Cys249 as the catalytic nucleophile required for intermediate formation
C249S
-
the C249S mutant and D66N mutant are both incapable of forming a covalent adduct when incubated with 2-hydroxymethyl-4-chloropyridine
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
2 h, holo-enzyme retains ca. 56% of the original activity, no residual activity of the apoenzyme. Thermal denaturation of both protein forms is irreversible
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, 0.1 M sodium phosphate buffer, pH 7.0, 10% glycerol, 1 mM 2-mercaptoethanol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by immobilized nickel-affinity chromatography and gel filtration
Ni-NTA affinity resin chromatography and phenyl-Sepharose column chromatography
-
recombinant enzyme, partial
wild type to more than 98% homogeneity, by Ni-NTA affinity chromatography, mutant required additional purification step, ion-exchange chromatography followed by affinity chromatography, mutant purified to more than 95% homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into a pET-28a expression vector, N-terminal His6-tagged protein overexpressed in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-lipoic acid increases the gene expression and activity of DDAH, and signal transducer and activator of transcription STAT3 phosphorylation. Transfection of STAT3 increases DDAH II promoter activity, and alpha-lipoic acid amplifies it. alpha-Lipoic acid-induced increase in DDAH II promoter activity is attenuated in the promoter that has a mutation in the putative STAT3-binding site
-
DDAH isoforms are expressed in a dynamic,overlapping pattern during embryonic development
-
DDAH-2 protein expression is higher in osteoarthritic cartilage than in normal cartilage
-
during growth on asymmetric dimethyl-L-arginine, induction of the DdaH gene is achieved via the putative enhancer-binding protein PA1196 and the alternative sigma factor RpoN. Both PA1196 and RpoN are essential for the expression of the DdaH gene in response to methylarginines
following myocardial infarction, left ventricular DDAH activity is increased to 210% of control
-
in chondrocyte mitochondria extracts, DDAH-2 expression is significantly increased after exposure to IL-1beta
-
resveratrol activates silent information regulator SIRT1 and inhibits upregulates the expression of DDAH2
treatment of mice with farnesoid X receptor agonist 3-(2,6-dichlorophenyl)-4-(3'-carboxy-2-chlorostilben-4-yl)oxymethyl-5-isopropylisoxazole, i.e. GW4064, leads to increased expression of DDAH-1 and cationic amino acid transporter CAT-1 in both liver and kidney
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inhibition by 2-(N,N-dimethylamino)-diazenolate-2-oxide is reversed by dithiothreitol
inhibition by 2-(N,N-dimethylamino)-diazenolate-2-oxide is reversed by dithiothreitol
-
inhibition by 2-(N,N-dimethylamino)-diazenolate-2-oxide is reversed by dithiothreitol
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
use of inhibitor N-(but-3-yn-1-yl)-2-chloroethanimidamide as a broad-specificity probe for labeling endogenous DDAH isoforms and enzymes with similar pharmacophores. Inhibitor labels the active fraction of DDAH-1 in intact mammalian cells and can be blocked by the presence of competitive reversible and irreversible inhibitors. Incorporation of the alkyne tag allows to derivatize with a variety of reagents after in vivo tagging
medicine
additional information
medicine
2-chloroacetamidine may potentially find wide applicability as a general pharmacophore, useful in delineating characteristics of the amidinotransferase superfamily
medicine
-
DDAH activity and elevated endogenous asymmetric dimethylarginine is implicated in endothelial dysfunction exposed to glycosylated bovine serum albumin, aminoguanidine can protect endothelium against injury induced by glycosylated bovine serum albumin both in vitro and in vivo
medicine
-
decreased DDAH-1 expression may cause accumulation of endogenous inhibitors of enothelial NO synthase, thereby contributing to endothelial dysfunction in the failing heart
medicine
-
decreased DDAH-1 expression may cause accumulation of endogenous inhibitors of enothelial NO synthase, thereby contributing to endothelial dysfunction in the failing heart
medicine
-
endogenous nitric oxide synthase inhibitor asymmetrical dimethylarginine (hydrolyzed by DDAH) is elevated in many patients and may contribute to the initiation and progression of their disease
medicine
-
epoetin beta and darbepoetin alpha posttranslationally impair DDAH activity via increased oxidative stress, causing NG,NG-dimethyl-L-arginine as an important cardiovascular risk factor to accumulate and inhibit NO-synthesis
medicine
-
expression and secretion of the vascular endothelial growth factor is not increased in DDAH1-transfected cells
medicine
-
expression and secretion of the vascular endothelial growth factor is not increased in DDAH1-transfected cells
medicine
-
in vivo administration of DDAH inhibitors (2-amino-4-(NG-methyl-guanidino)butanoic acid and its analogues) increases plasma NG,NG-dimethyl-L-arginine levels, giving proof of concept that these can be used to probe the physiological effects of DDAH inhibition, with potential for pharmaceutical use of DDAH inhibitors in diseases where excess NO production is implicated
medicine
-
protective effect of probucol on endothelium related to enhancement of DDAH activity
medicine
structure-based development of specific DDAH-1 inhibitors that might be useful in the therapeutic treatment of NOS dysfunction-related diseases
medicine
-
placental dysfunction of dimethylarginine dimethylaminohydrolase has been suggested as one of the initiating events in the development of preeclampsia
medicine
-
DDAH influences insulin sensitivity by regulating the endogenous nitric oxide synthase inhibitor asymmetrical dimethylarginine
medicine
influence on atherosclerosis in experimental models by increased ADMA concentrations and reduced NO synthesis
medicine
-
influence on atherosclerosis in experimental models by increased ADMA concentrations and reduced NO synthesis
medicine
influence on atherosclerosis in experimental models by increased ADMA concentrations and reduced NO synthesis
medicine
influence on atherosclerosis in experimental models by increased ADMA concentrations and reduced NO synthesis
medicine
influence on atherosclerosis in experimental models by increased ADMA concentrations and reduced NO synthesis
medicine
-
novel therapeutic strategy for the treatment of chronic kidney disease
medicine
-
hyperhomocysteinemia is induced in human DDAH1 transgenic mice and wild-type littermates using a high methionine/low folate diet. Plasma total homocysteine is elevated approximately 3fold in both wild-type and DDAH1 transgenic mice fed the high methionine/low folate diet compared with the control diet. Plasma asymmetrical dimethylarginine is approximately 40% lower in DDAH1 transgenic mice compared with wild-type mice irrespective of diet. Responses to 10 microM papaverine, a direct smooth muscle dilator, are impaired with the high methionine/low folate diet in wild-type mice but not DDAH1 transgenic mice. DDAH1 transgenic mice also are protected from hypertrophy of cerebral arterioles but not from accelerated carotid artery thrombosis induced by the high methionine/low folate diet
medicine
-
seven days after coronary artery ligation, L-Arg and methylated arginine content, as well as DDAH activity are determined in homogenates of left ventricular infarct and border. In healthy hearts, DDAHI is absent, and DDAHII is localized to endothelium and endocardium with a similar distribution to that of eNOS. Following myocardial infarction, left ventricular DDAH activity is increased to 210% of control. Both DDAHI and DDAHII proteins are detected in peri-infarct cardiomyocytes, while DDAHII immunoreactivity is additionally localized to infiltrating inflammatory cells and blood vessels in the healing infarct. Both plasma and left ventricular concentrations of the DDAH substrate, ADMA, are increased post-myocardial infarction, although the ratio of Arg:ADMA is retained in the left ventricular post-myocardial infarction relative to sham operated controls
medicine
global knockout of Ddah2 results in elevated blood pressure during periods of activity and changes in vascular responsiveness mediated by changes in methylarginine concentration, and systemic nitric oxide concentrations. In a model of severe polymicrobial sepsis, Ddah2 knockout affects outcome. Monocyte-specific deletion of Ddah2 results in a similar pattern of increased severity to that seen in globally deficient animals
medicine
in a mouse model of severe malaria, Plasmodium berghei ANKA infection inactivates hepatic DDAH1 via a post-transcriptional mechanism as evidenced by stable mRNA transcript number, decreased DDAH1 protein concentration, decreased enzyme activity, elevated tissue asymmetric dimethylarginine, elevated asymmetric dimethylarginine/arginine ratio in plasma, and decreased whole blood nitrite concentration
medicine
in lung adenocarcinoma, isoform DDAH2 is expressed in fibroblasts of stroma of malignancies, with higher expression in minimally invasive adenocarcinoma and invasive adenocarcinoma than in adenocarcinoma in situ. Tumors with high stromal expression of DDAH2 have a poorer prognosis than those without
medicine
in patients with type 2 diabetes mellitus, the percentage of senescent endothelial progenitor cells increases while the expression of DDAH2 decreases concomitantly with an increase in the plasma levels of asymmetric dimethylarginine. Exogenous application of asymmetric dimethylarginine accelerates the senescence of cultured endothelial progenitor cells in a dose-dependent manner, and overexpression of DDAH2 inhibits high glucose-induced endothelial progenitor cells senescence. Resveratrol (activating silent information regulator SIRT1) inhibits high glucose-induced endothelial progenitor cells senescence by upregulating the expression of DDAH2 and decreasing the levels of asymmetric dimethylarginine
medicine
plasma asymmetric dimethylarginine/arginine ratios are elevated in children with acute severe malaria compared to 28-day follow-up values and compared to children with uncomplicated malaria or healthy children
additional information
dimerization is not critical for the maintenance of the biological function of the protein
additional information
-
dimerization is not critical for the maintenance of the biological function of the protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leiper, J.M.; Santa Maria, J.; Chubb, A.; MacAllister, R.J.; Charles, I.G.
Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases
Biochem. J.
343
209-214
1999
Homo sapiens (O95865), Homo sapiens
brenda
Kimoto, M.; Sasakawa, T.; Tsuji, H.; Miyatake, S.; Oka, T.
Cloning and sequencing of cDNA encoding NG,NG-dimethylarginine dimethylaminohydrolase from rat kidnes
Biochim. Biophys. Acta
1337
6-10
1997
Rattus norvegicus
brenda
Santa Maria, J.; Vallance, P.; Charles, I.G.; Leiper, J.M.
Identification of microbial dimethylarginine dimethylaminohydrolase enzymes
Mol. Microbiol.
33
1278-1279
1999
Homo sapiens, Mycobacterium tuberculosis, Mus musculus, Pseudomonas aeruginosa, Rattus norvegicus, Streptomyces coelicolor
brenda
Birdsey, G.M.; Leiper, J.M.; Vallance, P.
Intramolecular localization of dimethylarginine dimethylaminohydrolase overexpressed in an endothelial cell line
Acta Physiol. Scand.
168
73-79
2000
Homo sapiens
brenda
Bogumil, R.; Knipp, M.; Fundel, S.M.; Vasak, M.
Characterization of dimethylargininase from bovine brain: evidence for a zinc binding site
Biochemistry
37
4791-4798
1998
Bos taurus
brenda
MacAllister, R.J.; Parry, H.; Kimoto, M.; Ogawa, T.; Russell, R.J.; Hodson, H.; Whiteley, G.St.J.; Vallance, P.
Regulation of nitric oxide synthesis by dimethylarginine dimethylaminohydrolase
Br. J. Pharmacol.
119
1533-1540
1996
Homo sapiens, Rattus norvegicus
brenda
Ogawa, T.; Kimoto, M.; Sasaoka, K.
Purification and properties of a new enzyme, NG,NG-dimethylarginine dimethylaminohydrolase from rat kidney
J. Biol. Chem.
264
10205-10209
1989
Rattus norvegicus
brenda
Kimoto, M.; Whiteley, G.St.J.; Tsuji, H.; Ogawa, T.
Detection of NG,NG-dimethylarginine dimethylaminohydrolase in human tissue using a monoclonal antibody
J. Biochem.
117
237-238
1995
Homo sapiens
brenda
Kimoto, M.; Tsuji, H.; Ogawa, T.; Sasaoka, K.
Detection of NG,NG-dimethylarginine dimethylaminohydrolase in the nitric oxide-generating systems of rats using monoclonal antibody
Arch. Biochem. Biophys.
300
657-662
1993
Rattus norvegicus
brenda
Knipp, M.; Charnock, J.M.; Garner, C.D.; Vasak, M.
Structural and functional characterization of the Zn(II) site in dimethylargininase-1 (DDAH-1) from bovine brain. Zn(II) release activates DDAH-1
J. Biol. Chem.
276
40449-40456
2001
Bos taurus
brenda
Knipp, M.; Braun, O.; Gehrig, P.M.; Sack, R.; Vasak, M.
Zn(II)-free dimethylargininase-1 (DDAH-1) is inhibited upon specific Cys-S-nitrosylation
J. Biol. Chem.
278
3410-3416
2003
Bos taurus
brenda
Plevin, M.J.; Magalhaes, B.S.; Harris, R.; Sankar, A.; Perkins, S.J.; Driscoll, P.C.
Characterization and manipulation of the Pseudomonas aeruginosa dimethylarginine dimethylaminohydrolase monomer--dimer equilibrium
J. Mol. Biol.
341
171-184
2004
Pseudomonas aeruginosa (Q9I4E3), Pseudomonas aeruginosa
brenda
Leiper, J.; Murray-Rust, J.; McDonald, N.; Vallance, P.
S-nitrosylation of dimethylarginine dimethylaminohydrolase regulates enzyme activity: further interactions between nitric oxide synthase and dimethylarginine dimethylaminohydrolase
Proc. Natl. Acad. Sci. USA
99
13527-13532
2002
Homo sapiens, Pseudomonas aeruginosa
brenda
Stone, E.M.; Schaller, T.H.; Bianchi, H.; Person, M.D.; Fast, W.
Inactivation of two diverse enzymes in the amidinotransferase superfamily by 2-chloroacetamidine: dimethylargininase and peptidylarginine deiminase
Biochemistry
44
13744-13752
2005
Pseudomonas aeruginosa (Q9I4E3), Pseudomonas aeruginosa
brenda
Chen, Y.; Li, Y.; Zhang, P.; Traverse, J.H.; Hou, M.; Xu, X.; Kimoto, M.; Bache, R.J.
Dimethylarginine dimethylaminohydrolase and endothelial dysfunction in failing hearts
Am. J. Physiol. Heart Circ. Physiol.
289
H2212-2219
2005
Canis lupus familiaris, Homo sapiens
brenda
Billecke, S.S.; Kitzmiller, L.A.; Northrup, J.J.; Whitesall, S.E.; Kimoto, M.; Hinz, A.V.; D'Alecy, L.G.
Contribution of whole blood to the control of plasma asymmetrical dimethylarginine
Am. J. Physiol. Heart Circ. Physiol.
291
H1788-1796
2006
Rattus norvegicus
brenda
Hasegawa, K.; Wakino, S.; Tanaka, T.; Kimoto, M.; Tatematsu, S.; Kanda, T.; Yoshioka, K.; Homma, K.; Sugano, N.; Kurabayashi, M.; Saruta, T.; Hayashi, K.
Dimethylarginine dimethylaminohydrolase 2 increases vascular endothelial growth factor expression through Sp1 transcription factor in endothelial cells
Arterioscler. Thromb. Vasc. Biol.
26
1488-1494
2006
Bos taurus, Homo sapiens
brenda
Yin, Q.; Fu, S.; He, P.; Xiong, Y.
Dimethylarginine dimethylaminohydrolase inhibition and asymmetric dimethylarginine accumulation contribute to endothelial dysfunction in rats exposed to glycosylated protein: Effects of aminoguanidine
Atherosclerosis
190
53-61
2006
Rattus norvegicus
brenda
Stone, E.M.; Person, M.D.; Costello, N.J.; Fast, W.
Characterization of a transient covalent adduct formed during dimethylarginine dimethylaminohydrolase catalysis
Biochemistry
44
7069 - 7078
2005
Pseudomonas aeruginosa (Q9I4E3), Pseudomonas aeruginosa
brenda
Stone, E.M.; Costello, A.L.; Tierney, D.L.; Fast, W.
Substrate-assisted cysteine deprotonation in the mechanism of dimethylargininase (DDAH) from Pseudomonas aeruginosa
Biochemistry
45
5618-5630
2006
Pseudomonas aeruginosa
brenda
Mishima, T.; Hamada, T.; Ui-Tei, K.; Miyata, Y.; Imaki, J.; Suzuki, H.; Yamashita K.
Expression of DDAH1 in chick and rat embryos
Brain Res. Dev. Brain Res.
148
223-232
2004
Gallus gallus, Rattus norvegicus
brenda
Jiang, J.L.; Zhang, X.H.; Li, N.S.; Rang, W.Q; Feng-Ye, W.Q.; Hu, C.P.; Li, Y.J.; Deng, H.W.
Probucol decreases asymmetrical dimethylarginine level by alternation of protein arginine methyltransferase I and dimethylarginine dimethylaminohydrolase activity
Cardiovasc. Drugs Ther.
20
281-294
2006
Homo sapiens, Rattus norvegicus
brenda
Vallance, P.; Bush, H.D.; Mok, B.J.; Hurtado-Guerrero, R.; Gill, H.; Rossiter, S.; Wilden, J.D.; Caddick, S.
Inhibition of dimethylarginine dimethylaminohydrolase (DDAH) and arginine deiminase (ADI) by pentafluorophenyl (PFP) sulfonates
Chem. Commun. (Camb.)
2005
5563-5565
2005
Pseudomonas sp.
brenda
Wakino, S.; Hayashi, K.; Tatematsu, S.; Hasegawa, K.; Takamatsu, I.; Kanda, T.; Homma, K.; Yoshioka, K.; Sugano, N.; Saruta, T.
Pioglitazone lowers systemic asymmetric dimethylarginine by inducing dimethylarginine dimethylaminohydrolase in rats
Hypertens. Res.
28
255-262
2005
Rattus norvegicus
brenda
Scalera, F.; Kielstein, J.T.; Martens-Lobenhoffer, J.; Postel, S.C.; Tager, M.; Bode-Boger, S.M.
Erythropoietin increases asymmetric dimethylarginine in endothelial cells: role of dimethylarginine dimethylaminohydrolase
J. Am. Soc. Nephrol.
16
892-898
2005
Homo sapiens
brenda
Rossiter, S.; Smith, C.L.; Malaki, M.; Nandi, M.; Gill, H.; Leiper, J.M.; Vallance, P.; Selwood, D.L.
Selective substrate-based inhibitors of mammalian dimethylarginine dimethylaminohydrolase
J. Med. Chem.
48
4670-4678
2005
Rattus norvegicus
brenda
Frey, D.; Braun, O.; Briand, C.; Vak, M.; Grtter, M.G.
Structure of the mammalian NOS regulator dimethylarginine dimethylaminohydrolase: a basis for the design of specific inhibitors
Structure
14
901-911
2006
Bos taurus (P56965), Bos taurus
brenda
Braun, O.; Knipp, M.; Chesnov, S.; Vasak, M.
Specific reactions of S-nitrosothiols with cysteine hydrolases: A comparative study between dimethylargininase-1 and CTP synthetase
Protein Sci.
16
1522-1534
2007
Bos taurus (P56965)
brenda
Sasaki, A.; Doi, S.; Mizutani, S.; Azuma, H.
Roles of accumulated endogenous nitric oxide synthase inhibitors, enhanced arginase activity, and attenuated nitric oxide synthase activity in endothelial cells for pulmonary hypertension in rats
Am. J. Physiol. Lung Cell Mol. Physiol.
292
L1480-L1487
2007
Rattus norvegicus
brenda
Forbes, S.P.; Druhan, L.J.; Guzman, J.E.; Parinandi, N.; Zhang, L.; Green-Church, K.B.; Cardounel, A.J.
Mechanism of 4-HNE mediated inhibition of hDDAH-1: implications in no regulation
Biochemistry
47
1819-1826
2008
Homo sapiens
brenda
Wang, J.; Sim, A.S.; Wang, X.L.; Wilcken, D.E.
L-arginine regulates asymmetric dimethylarginine metabolism by inhibiting dimethylarginine dimethylaminohydrolase activity in hepatic (HepG2) cells
Cell. Mol. Life Sci.
63
2838-2846
2006
Homo sapiens
brenda
Wang, D.; Gill, P.S.; Chabrashvili, T.; Onozato, M.L.; Raggio, J.; Mendonca, M.; Dennehy, K.; Li, M.; Modlinger, P.; Leiper, J.; Vallance, P.; Adler, O.; Leone, A.; Tojo, A.; Welch, W.J.; Wilcox, C.S.
Isoform-specific regulation by N(G),N(G)-dimethylarginine dimethylaminohydrolase of rat serum asymmetric dimethylarginine and vascular endothelium-derived relaxing factor/NO
Circ. Res.
101
627-635
2007
Rattus norvegicus (Q6MG60)
brenda
Siroen, M.P.; Teerlink, T.; Bolte, A.C.; van Elburg, R.M.; Richir, M.C.; Nijveldt, R.J.; van der Hoven, B.; van Leeuwen, P.A.
No compensatory upregulation of placental dimethylarginine dimethylaminohydrolase activity in preeclampsia
Gynecol. Obstet. Invest.
62
7-13
2006
Homo sapiens
brenda
Hong, L.; Fast, W.
Inhibition of human dimethylarginine dimethylaminohydrolase-1 by S-nitroso-L-homocysteine and hydrogen peroxide. Analysis, quantification, and implications for hyperhomocysteinemia
J. Biol. Chem.
282
34684-34692
2007
Homo sapiens
brenda
Slaghekke, F.; Dekker, G.; Jeffries, B.
Endogenous inhibitors of nitric oxide and preeclampsia: a review
J. Matern. Fetal. Neonatal. Med.
19
447-452
2006
Homo sapiens (O95865), Homo sapiens
brenda
Tain, Y.L.; Baylis, C.
Determination of dimethylarginine dimethylaminohydrolase activity in the kidney
Kidney Int.
72
886-889
2007
Rattus norvegicus
brenda
Mizuno, Y.; Isotani, E.; Ohno, K.; Nagai, A.; Imamura, M.; Azuma, H.
Involvement of accumulated NOS inhibitors and endothelin-1, enhanced arginase, and impaired DDAH activities in pulmonary dysfunction following subarachnoid hemorrhage in the rabbit
Vascul. Pharmacol.
48
21-31
2008
Oryctolagus cuniculus
brenda
Dayal, S.; Rodionov, R.N.; Arning, E.; Bottiglieri, T.; Kimoto, M.; Murry, D.J.; Cooke, J.P.; Faraci, F.M.; Lentz, S.R.
Tissue-specific downregulation of dimethylarginine dimethylaminohydrolase in hyperhomocysteinemia
Am. J. Physiol. Heart Circ. Physiol.
295
H816-H825
2008
Mus musculus
brenda
Sydow, K.; Mondon, C.E.; Schrader, J.; Konishi, H.; Cooke, J.P.
Dimethylarginine dimethylaminohydrolase overexpression enhances insulin sensitivity
Arterioscler. Thromb. Vasc. Biol.
28
692-697
2008
Homo sapiens
brenda
Kotthaus, J.; Schade, D.; Muschick, N.; Beitz, E.; Clement, B.
Structure-activity relationship of novel and known inhibitors of human dimethylarginine dimethylaminohydrolase-1: alkenyl-amidines as new leads
Bioorg. Med. Chem.
16
10205-10209
2008
Homo sapiens
brenda
Xiao, J.; Xiao, Z.J.; Liu, Z.G.; Gong, H.Y.; Yuan, Q.; Wang, S.; Li, Y.J.; Jiang, D.J.
Involvement of dimethylarginine dimethylaminohydrolase-2 in visfatin-enhanced angiogenic function of endothelial cells
Diabetes Metab. Res. Rev.
25
242-249
2009
Homo sapiens
brenda
Ellger, B.; Richir, M.C.; van Leeuwen, P.A.; Debaveye, Y.; Langouche, L.; Vanhorebeek, I.; Teerlink, T.; Van den Berghe, G.
Glycemic control modulates arginine and asymmetrical-dimethylarginine levels during critical illness by preserving dimethylarginine-dimethylaminohydrolase activity
Endocrinology
149
3148-3157
2008
Oryctolagus cuniculus
brenda
Wadham, C.; Mangoni, A.A.
Dimethylarginine dimethylaminohydrolase regulation: a novel therapeutic target in cardiovascular disease
Expert. Opin. Drug Metab. Toxicol.
5
303-319
2009
Bos taurus, Bos taurus (Q3SX44), Oryctolagus cuniculus, Rattus norvegicus (O08557), Rattus norvegicus (Q6MG60), Homo sapiens (O94760), Homo sapiens (O95865), Mus musculus (Q99LD8), Mus musculus (Q9CWS0)
brenda
Sakurada, M.; Shichiri, M.; Imamura, M.; Azuma, H.; Hirata, Y.
Nitric oxide upregulates dimethylarginine dimethylaminohydrolase-2 via cyclic GMP induction in endothelial cells
Hypertension
52
903-909
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Wang, S.; Hu, C.P.; Jiang, D.J.; Peng, J.; Zhou, Z.; Yuan, Q.; Nie, S.D.; Jiang, J.L.; Li, Y.J.; Huang, K.L.
All-trans retinoic acid inhibits cobalt chloride-induced apoptosis in PC12 cells: role of the dimethylarginine dimethylaminohydrolase/asymmetric dimethylarginine pathway
J. Neurosci. Res.
87
1938-1946
2009
Homo sapiens
brenda
Ueda, S.; Yamagishi, S.I.; Matsumoto, Y.; Kaida, Y.; Fujimi-Hayashida, A.; Koike, K.; Tanaka, H.; Fukami, K.; Okuda, S.
Involvement of asymmetric dimethylarginine (ADMA) in glomerular capillary loss and sclerosis in a rat model of chronic kidney disease (CKD)
Life Sci.
84
853-860
2009
Homo sapiens
brenda
Gray, G.A.; Patrizio, M.; Sherry, L.; Miller, A.A.; Malaki, M.; Wallace, A.F.; Leiper, J.M.; Vallance, P.
Immunolocalisation and activity of DDAH I and II in the heart and modification post-myocardial infarction
Acta Histochem.
112
413-423
2010
Rattus norvegicus
brenda
Lee, W.J.; Kim, S.H.; Kim, G.H.; Han, S.M.; Won, J.C.; Jung, C.H.; Park, H.S.; Choi, d.o..S.; Lee, K.U.; Park, J.Y.
Alpha-lipoic acid activates dimethylarginine dimethylaminohydrolase in cultured endothelial cells
Biochem. Biophys. Res. Commun.
398
653-658
2010
Mus musculus
brenda
Wang, Y.; Monzingo, A.F.; Hu, S.; Schaller, T.H.; Robertus, J.D.; Fast, W.
Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide
Biochemistry
48
8624-8635
2009
Homo sapiens (O94760), Homo sapiens
brenda
Rodionov, R.N.; Dayoub, H.; Lynch, C.M.; Wilson, K.M.; Stevens, J.W.; Murry, D.J.; Kimoto, M.; Arning, E.; Bottiglieri, T.; Cooke, J.P.; Baumbach, G.L.; Faraci, F.M.; Lentz, S.R.
Overexpression of dimethylarginine dimethylaminohydrolase protects against cerebral vascular effects of hyperhomocysteinemia
Circ. Res.
106
551-558
2010
Homo sapiens
brenda
Breckenridge, R.A.; Kelly, P.; Nandi, M.; Vallance, P.J.; Ohun, T.J.; Leiper, J.
A role for dimethylarginine dimethylaminohydrolase 1 (DDAH1) in mammalian development
Int. J. Dev. Biol.
54
215-220
2010
Mus musculus
brenda
Wang, Y.; Hu, S.; Fast, W.
A click chemistry mediated in vivo activity probe for dimethylarginine dimethylaminohydrolase
J. Am. Chem. Soc.
131
15096-15097
2009
Homo sapiens
brenda
Pope, A.J.; Karrupiah, K.; Kearns, P.N.; Xia, Y.; Cardounel, A.J.
Role of dimethylarginine dimethylaminohydrolases in the regulation of endothelial nitric oxide production
J. Biol. Chem.
284
35338-35347
2009
Bos taurus (P56965), Bos taurus (Q3SX44)
brenda
Li, J.; Wilson, A.; Gao, X.; Kuruba, R.; Liu, Y.; Poloyac, S.; Pitt, B.; Xie, W.; Li, S.
Coordinated regulation of dimethylarginine dimethylaminohydrolase-1 and cationic amino acid transporter-1 by farnesoid X receptor in mouse liver and kidney and its implication in the control of blood levels of asymmetric dimethylarginine
J. Pharmacol. Exp. Ther.
331
234-243
2009
Mus musculus
brenda
Hu, X.; Atzler, D.; Xu, X.; Zhang, P.; Guo, H.; Lu, Z.; Fassett, J.; Schwedhelm, E.; Boeger, R.H.; Bache, R.J.; Chen, Y.
Dimethylarginine dimethylaminohydrolase-1 is the critical enzyme for degrading the cardiovascular risk factor asymmetrical dimethylarginine
Arterioscler. Thromb. Vasc. Biol.
31
1540-1546
2011
Mus musculus
brenda
Zhang, P.; Hu, X.; Xu, X.; Chen, Y.; Bache, R.J.
Dimethylarginine dimethylaminohydrolase 1 modulates endothelial cell growth through nitric oxide and Akt
Arterioscler. Thromb. Vasc. Biol.
31
890-897
2011
Homo sapiens, Mus musculus
brenda
Cillero-Pastor, B.; Mateos, J.; Fernandez-Lopez, C.; Oreiro, N.; Ruiz-Romero, C.; Blanco, F.J.
Dimethylarginine dimethylaminohydrolase 2, a newly identified mitochondrial protein modulating nitric oxide synthesis in normal human chondrocytes
Arthritis Rheum.
64
204-212
2012
Homo sapiens
brenda
Johnson, C.M.; Linsky, T.W.; Yoon, D.W.; Person, M.D.; Fast, W.
Discovery of halopyridines as quiescent affinity labels: inactivation of dimethylarginine dimethylaminohydrolase
J. Am. Chem. Soc.
133
1553-1562
2011
Pseudomonas aeruginosa
brenda
Kotthaus, J.; Schade, D.; Kotthaus, J.; Clement, B.
Designing modulators of dimethylarginine dimethylaminohydrolase (DDAH): a focus on selectivity over arginase
J. Enzyme Inhib. Med. Chem.
27
24-28
2012
Homo sapiens
brenda
Davids, M.; Richir, M.C.; Visser, M.; Ellger, B.; van den Berghe, G.; van Leeuwen, P.A.; Teerlink, T.
Role of dimethylarginine dimethylaminohydrolase activity in regulation of tissue and plasma concentrations of asymmetric dimethylarginine in an animal model of prolonged critical illness
Metab. Clin. Exp.
61
482-490
2012
Oryctolagus cuniculus
brenda
Ghebremariam, Y.T.; Erlanson, D.A.; Cooke, J.P.
A novel and potent inhibitor of dimethylarginine dimethylaminohydrolase: a modulator of cardiovascular nitric oxide
J. Pharmacol. Exp. Ther.
348
69-76
2014
Homo sapiens (O94760), Homo sapiens
brenda
Sydow, K.; Schmitz, C.; von Leitner, E.C.; von Leitner, R.; Klinke, A.; Atzler, D.; Krebs, C.; Wieboldt, H.; Ehmke, H.; Schwedhelm, E.; Meinertz, T.; Blankenberg, S.; Boeger, R.H.; Magnus, T.; Baldus, S.; Wenzel, U.
Dimethylarginine dimethylaminohydrolase1 is an organ-specific mediator of end organ damage in a murine model of hypertension
PLoS ONE
7
e48150
2012
Homo sapiens (O94760)
brenda
Lambden, S.; Kelly, P.; Ahmetaj-Shala, B.; Wang, Z.; Lee, B.; Nandi, M.; Torondel, B.; Delahaye, M.; Dowsett, L.; Piper, S.; Tomlinson, J.; Caplin, B.; Colman, L.; Boruc, O.; Slaviero, A.; Zhao, L.; Oliver, E.; Khadayate, S.; Singer, M.; Arrigoni, F.; Leiper, J.
Dimethylarginine dimethylaminohydrolase 2 regulates nitric oxide synthesis and hemodynamics and determines outcome in polymicrobial sepsis
Arterioscler. Thromb. Vasc. Biol.
35
1382-1392
2015
Mus musculus (Q99LD8)
brenda
Yuan, Q.; Hu, C.P.; Gong, Z.C.; Bai, Y.P.; Liu, S.Y.; Li, Y.J.; Jiang, J.L.
Accelerated onset of senescence of endothelial progenitor cells in patients with type 2 diabetes mellitus role of dimethylarginine dimethylaminohydrolase 2 and asymmetric dimethylarginine
Biochem. Biophys. Res. Commun.
458
869-876
2015
Homo sapiens (O95865), Homo sapiens
brenda
Dowsett, L.; Piper, S.; Slaviero, A.; Dufton, N.; Wang, Z.; Boruc, O.; Delahaye, M.; Colman, L.; Kalk, E.; Tomlinson, J.; Birdsey, G.; Randi, A.M.; Leiper, J.
Endothelial dimethylarginine dimethylaminohydrolase 1 is an important regulator of angiogenesis but does not regulate vascular reactivity or hemodynamic homeostasis
Circulation
131
2217-2225
2015
Mus musculus (Q9CWS0), Mus musculus
brenda
Lundgren, B.; Bailey, F.; Moley, G.; Nomura, C.
DdaR (PA1196) regulates expression of dimethylarginine dimethylaminohydrolase for the metabolism of methylarginines in Pseudomonas aeruginosa PAO1
J. Bacteriol.
199
e00001-17
2017
Pseudomonas aeruginosa (Q9I4E3), Pseudomonas aeruginosa
brenda
Chertow, J.H.; Alkaitis, M.S.; Nardone, G.; Ikeda, A.K.; Cunnington, A.J.; Okebe, J.; Ebonyi, A.O.; Njie, M.; Correa, S.; Jayasooriya, S.; Casals-Pascual, C.; Billker, O.; Conway, D.J.; Walther, M.; Ackerman, H.
Plasmodium infection is associated with impaired hepatic dimethylarginine dimethylaminohydrolase activity and disruption of nitric oxide synthase inhibitor/substrate homeostasis
PLoS Pathog.
11
e1005119
2015
Homo sapiens (O94760), Homo sapiens, Mus musculus (Q9CWS0), Mus musculus
brenda
Shiozawa, T.; Iyama, S.; Toshima, S.; Sakata, A.; Usui, S.; Minami, Y.; Sato, Y.; Hizawa, N.; Noguchi, M.
Dimethylarginine dimethylaminohydrolase 2 promotes tumor angiogenesis in lung adenocarcinoma
Virchows Arch.
468
179-190
2016
Homo sapiens (O95865), Homo sapiens
brenda
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