Several proteins contain citrulline as a result of a posttranslational modification. These citrulline residues are generated by a family of enzymes called peptidylarginine deiminases (PADs), which convert arginine into citrulline in a process called citrullination or deimination. Proteins that normally contain citrulline residues include myelin basic protein (MBP), filaggrin, and several histone proteins, whereas other proteins, such as fibrin and vimentin are susceptible to citrullination during cell death and tissue inflammation.

Patients with rheumatoid arthritis often have detectable antibodies against proteins containing citrulline. Although the origin of this immune response is not known, detection of antibodies reactive with citrulline (anti-citrullinated protein antibodies) containing proteins or peptides is now becoming an important help in the diagnosis of rheumatoid arthritis.[5]

Circulating citrulline concentration is, in humans, a biomarker of intestinal functionality.

(2S)-5-(aminocarbonylamino)-2-azanyl-pentanoic acid

Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase.

Psuedomonas aeruginosa Dimethylarginine Dimethylaminohydrolase DDAH

The methylarginines ADMA and MMA inhibit the production of nitric oxide synthase.DDAH is important in removing methylarginines, generated by protein degradation, from accumulating and inhibiting the generation of nitric oxide in mammals.

Ddah From Pseudomonas Aeruginosa. C249s Mutant Complexed With Citrulline

Crystal Structure Of The Dimethylarginine Dimethylaminohydrolase H162g Adduct With S-Methyl-L- Thiocitrulline

Crystal Structure Of The Dimethylarginine Dimethylaminohydrolase Adduct With 4-Chloro-2-Hydroxymethylpyridine

hypothetical protein NCGM2_2069 [Pseudomonas aeruginosa NCGM2.S1]

hypothetical protein NCGM1900_1389 [Pseudomonas aeruginosa]

hypothetical protein NCGM1984_4129 [Pseudomonas aeruginosa]

hypothetical protein PA257_4611 [Pseudomonas aeruginosa]

N(G),N(G)-dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa]

putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa LESB58]

NG,NG-dimethylarginine dimethylaminohydrolase 1 [Pseudomonas aeruginosa 18A]

N(G), N(G)-dimethylargininedimethylaminohydrolase [Pseudomonas aeruginosa MH38]

N(G), N(G)-dimethylargininedimethylaminohydrolase [Pseudomonas aeruginosa MH27]

putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa PA38182]

hypothetical protein PA1195 [Pseudomonas aeruginosa PAO1]

putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa UCBPP-PA14]

putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa M18]

N-Dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa DK2]

N-Dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa B136-33]

MULTISPECIES: N(G),N(G)-dimethylarginine dimethylaminohydrolase [Pseudomonas]

RecName: Full=N(G),N(G)-dimethylarginine dimethylaminohydrolase; Short=DDAH; Short=Dimethylarginine dimethylaminohydrolase; Alt

The methylarginines ADMA and MMA inhibit the production of nitric oxide synthase.[3] As such, DDAH is important in removing methylarginines, generated by protein degradation, from accumulating and inhibiting the generation of nitric oxide.

Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase

The CCPN NMR assignment and data analysis application

Department of Biochemistry, Cambridge CB2 1GA, UK