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Information on EC 3.5.3.18 - dimethylargininase and Organism(s) Homo sapiens
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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 taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, ddah-i, human ddah-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DDAH
DDAH-1
DDAH-2
DDAH1
DDAH2
DDAHI
-
-
-
-
DDAHII
-
-
-
-
Dimethylargininase
-
-
-
-
dimethylarginine dimethylaminohydrolase
G6a
-
-
-
-
DDAH
-
-
-
-
DDAH-2
isozyme, mainly present in vascular tissues that co-express endothelial nitric oxide synthases
dimethylarginine dimethylaminohydrolase
-
-
-
-
dimethylarginine dimethylaminohydrolase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of linear amidines
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Nomega,Nomega'-dimethyl-L-arginine dimethylamidohydrolase
Also acts on Nomega-methyl-L-arginine.
CAS REGISTRY NUMBER
COMMENTARY
123644-75-7
-
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
-
-
?
Ngamma-monomethyl-L-arginine + H2O
L-citrulline + methylamine
-
-
-
?
Nomega,Nomega'-dimethyl-L-arginine + H2O
dimethylamine + L-citrulline
-
-
-
?
Nomega,Nomega-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
-
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
-
-
?
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)
-
-
?
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
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
-
lipopolysaccharide
1 microg/ml, 24 h, about 55% relative activity; 1 microg/ml, about 55% relative activity
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
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%
peroxynitrite
-
inhibition of 15% after exposure to peroxynitrite at concentrations ranging from 0.01-0.1 mM, 25% inhibition at 1 mM
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
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
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
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
288967, 288968, 288970, 288972, 653681, 667155, 667355, 668175, 669059, 685205, 686018, 686991, 687644
-
-
transgenic mouse model with oxerexpressed human dimethylarginine dimethylaminohydrolase
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
DDAH-2 protein expression is higher in osteoarthritic cartilage than in normal cartilage
additional information
-
overexpression in the immortalized cell line
additional information
DDAH I predominates in tissues that express neuronal nitric oxide synthase, DDAH II predominates in tissues expressing endothelial nitric oxide synthase
additional information
-
DDAH I predominates in tissues that express neuronal nitric oxide synthase, DDAH II predominates in tissues expressing endothelial nitric oxide synthase
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DDAH1_HUMAN
285
0
31122
Swiss-Prot
Mitochondrion (Reliability: 3)
DDAH2_HUMAN
285
0
29644
Swiss-Prot
other Location (Reliability: 2)
B2R644_HUMAN
285
0
31122
TrEMBL
Mitochondrion (Reliability: 3)
H0Y7N1_HUMAN
188
0
20073
TrEMBL
other Location (Reliability: 2)
A0A140T971_HUMAN
225
0
23512
TrEMBL
other Location (Reliability: 2)
Q5SSV3_HUMAN
226
0
23569
TrEMBL
other Location (Reliability: 2)
B4E3V1_HUMAN
167
0
18418
TrEMBL
other Location (Reliability: 1)
Q5SRR8_HUMAN
236
0
24640
TrEMBL
other Location (Reliability: 2)
B4DYP1_HUMAN
185
0
20535
TrEMBL
other Location (Reliability: 1)
V9HW53_HUMAN
285
0
29644
TrEMBL
other Location (Reliability: 2)
B4DGT0_HUMAN
192
0
21353
TrEMBL
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C274A
C274A
-
inactive and is not labeled by inhibitor N-(but-3-yn-1-yl)-2-chloroethanimidamide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity resin chromatography and phenyl-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
DDAH-2 protein expression is higher in osteoarthritic cartilage than in normal cartilage
-
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
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inhibition by 2-(N,N-dimethylamino)-diazenolate-2-oxide is reversed by dithiothreitol
-
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
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
-
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
-
protective effect of probucol on endothelium related to enhancement of DDAH activity
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
-
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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)
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
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
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
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
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
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
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
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
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
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
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)
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
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
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