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

Citrulline residues are generated in proteins as a result of a posttranslational
modification reaction conducted by a family of enzymes called peptidylarginine
deiminases (PADs), which convert arginine into citrulline. Proteins that
normally contain citrulline residues include myelin basic protein (MBP),
filaggrin, and several histone proteins.
Patients with rheumatoid arthritis often have detectable antibodies against
proteins containing citrulline. Therefore, application of antibodies reactive
with citrulline, containing proteins is now becoming an important tool to
diagnose the rheumatoid arthritis.Whereas, the circulating citrulline
concentration in humans,is used as distinctive bio-marker for examining the
intestinal functionality.

Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase

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

In mammals, the enzyme dimethylarginine dimethylaminohydrolase (DDAH) is implicated in the regulation of the cellular levels of asymmetric methylarginines, small molecule metabolites that themselves represent a family of endogenous inhibitors of nitric oxide synthase (NOS). The involvement of DDAH function in the regulation of NOS makes this enzyme a potentially attractive therapeutic target.

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

Dimethylarginine Dimethylaminohydrolase, Asymmetric Dimethyarginine, Nitric Oxide, Nitric Oxide Synthases

Psuedomonas aeruginosa Dimethylarginine Dimethylaminohydrolase

The CCPN NMR assignment and data analysis application

Department of Biochemistry, Cambridge CB2 1GA, UK