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Literature summary for 3.5.3.18 extracted from

  • 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 (2009), J. Biol. Chem., 284, 35338-35347.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Bos taurus P56965 isoform DDAH-1
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Bos taurus Q3SX44 isoform DDAH-2
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Source Tissue

Source Tissue Comment Organism Textmining
endothelial cell aortic endothelial cell Bos taurus
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Synonyms

Synonyms Comment Organism
DDAH-2
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Bos taurus

General Information

General Information Comment Organism
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 Bos taurus
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 Bos taurus