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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
Expression of NG,NG-Dimethylarginine Dimethylaminohydrolase and Protein Arginine N-Methyltransferase Isoforms in Diabetic Rat Kidney
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
Isoform-Specific Regulation by NG,NG-Dimethylarginine Dimethylaminohydrolase of Rat Serum Asymmetric Dimethylarginine and Vascular Endothelium-Derived Relaxing Factor/NO
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
Lysophosphatidylcholine-induced elevation of asymmetric dimethylarginine level by the NADPH oxidase pathway in endothelial cells.
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
Estrogen Stimulates Dimethylarginine Dimethylaminohydrolase Activity and the Metabolism of Asymmetric Dimethylarginine
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
S-nitrosylation of dimethylarginine dimethylaminohydrolase regulates enzyme activity: Further interactions between nitric oxide synthase and dimethylarginine dimethylaminohydrolase
The enzyme dimethylarginine dimethylaminohydrolase (DDAH) hydrolyses asymmetrically methylated arginine residues that are… Expand
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Highly Cited
2001
Highly Cited
2001
Homocysteine Impairs the Nitric Oxide Synthase Pathway: Role of Asymmetric Dimethylarginine
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
Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase
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
A colorimetric 96-well microtiter plate assay for the determination of enzymatically formed citrulline.
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
Chromosomal localization, gene structure, and expression pattern of DDAH1: comparison with DDAH2 and implications for evolutionary origins.
Endogenously produced asymmetrically methylated arginine residues are competitive inhibitors of all three isoforms of nitric… Expand
Highly Cited
1996
Highly Cited
1996
Regulation of nitric oxide synthesis by dimethylarginine dimethylaminohydrolase
1 Dimethylarginine dimethylaminohydrolase (DDAH), an enzyme that metabolizes the endogenous nitric oxide synthase inhibitors NG… Expand
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