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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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2010
2010
Sequence Variation in DDAH1 and DDAH2 Genes Is Strongly and Additively Associated with Serum ADMA Concentrations in Individuals with Type 2 Diabetes
BACKGROUND Asymmetric dimethylarginine (ADMA), present in human serum, is an endogenous inhibitor of nitric oxide synthase and… Expand
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2008
2008
Expression of NG,NG-dimethylarginine dimethylaminohydrolase and protein arginine N-methyltransferase isoforms in diabetic rat kidney: effects of angiotensin II receptor blockers.
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 N(G),N(G)-dimethylarginine dimethylaminohydrolase of rat serum asymmetric dimethylarginine and vascular endothelium-derived relaxing factor/NO.
Asymmetric dimethylarginine (ADMA), which inhibits NO synthase, is inactivated by N(G),N(G)-dimethylarginine… 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
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
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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
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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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