Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases

• Published in: Biochemical journal Vol. 343 Pt 1; no. 1; pp. 209 - 214
• Main Authors: Leiper, J M, Santa Maria, J, Chubb, A, MacAllister, R J, Charles, I G, Whitley, G S, Vallance, P
• Format: Journal Article
• Language: English
• Published: England 01-10-1999
• Subjects: Amidohydrolases; Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; DNA, Complementary; Humans; Hydrolases - chemistry; Hydrolases - genetics; Hydrolases - metabolism; Isoenzymes - chemistry; Isoenzymes - genetics; Isoenzymes - metabolism; Molecular Sequence Data; Rats; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Sequence Homology, Amino Acid
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/0264-6021:3430209

Methylarginines inhibit nitric oxide synthases (NOS). Cellular concentrations of methylarginines are determined in part by the activity of dimethylarginine dimethylaminohydrolase (DDAH; EC 3.5.3. 18). We have cloned human DDAH and identified and expressed a second novel DDAH isoform (DDAH I and II respectively). DDAH I predominates in tissues that express neuronal NOS. DDAH II predominates in tissues expressing endothelial NOS. These results strengthen the hypothesis that methylarginine concentration is actively regulated and identify molecular targets for the tissue and cell-specific regulation of methylarginine concentration.