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dimethylargininase activity

Known as: N(G),N(G)-dimethylarginine dimethylaminohydrolase activity, NG,NG-dimethyl-L-arginine dimethylamidohydrolase activity, dimethylarginine dimethylaminohydrolase activity 
Catalysis of the reaction: N(G),N(G)-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline. [EC:3.5.3.18]
National Institutes of Health

Papers overview

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Highly Cited
2008
Highly Cited
2008
OBJECTIVE—The nitric oxide (NO) synthase inhibitor asymmetric dimethylarginine (ADMA) is generated by protein arginine N… Expand
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Highly Cited
2007
Highly Cited
2007
Asymmetric dimethylarginine (ADMA), which inhibits NO synthase, is inactivated by NG,NG-dimethylarginine dimethylaminohydrolase… Expand
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Highly Cited
2006
Highly Cited
2006
Recent studies suggested that endothelium is a main source of reactive oxygen species (ROS) and the major source was via NADPH… Expand
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Highly Cited
2003
Highly Cited
2003
Background—Experimental evidence suggests that estrogens stimulate the production of nitric oxide (NO) by vascular endothelial… Expand
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Highly Cited
2002
Highly Cited
2002
The enzyme dimethylarginine dimethylaminohydrolase (DDAH) hydrolyses asymmetrically methylated arginine residues that are… Expand
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Highly Cited
2001
Highly Cited
2001
Background—Hyperhomocysteinemia is a putative risk factor for cardiovascular disease, which also impairs endothelium-dependent… Expand
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Highly Cited
2001
Highly Cited
2001
Nitric oxide synthase is inhibited by asymmetric NG-methylated derivatives of arginine whose cellular levels are controlled in… Expand
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Highly Cited
2000
Highly Cited
2000
l-Citrulline constitutes a product of a number of enzymatic reactions. In the past a number of colorimetric methods for the… Expand
Highly Cited
2000
Highly Cited
2000
Endogenously produced asymmetrically methylated arginine residues are competitive inhibitors of all three isoforms of nitric… Expand
Highly Cited
1996
Highly Cited
1996
1 Dimethylarginine dimethylaminohydrolase (DDAH), an enzyme that metabolizes the endogenous nitric oxide synthase inhibitors NG… Expand