MitoProteome Database

MT000897

UniProt Annotations

Entry Information
Gene Namedimethylarginine dimethylaminohydrolase 1
Protein EntryDDAH1_HUMAN
UniProt IDO94760
SpeciesHuman
Comments
Comment typeDescription
Alternative Products Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O94760-1; Sequence=Displayed; Name=2; IsoId=O94760-2; Sequence=VSP_043813;
Biophysicochemical Properties Kinetic parameters: KM=69 uM for asymmetric dimethylarginine (ADMA) {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; KM=54 uM for monomethyl-L-arginine (MMA) {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; KM=3.1 uM for S-methyl-L-thiocitrulline {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; Vmax=356 nmol/min/mg enzyme with ADMA {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; Vmax=154 nmol/min/mg enzyme with NMA {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506};
Catalytic Activity N(omega),N(omega)-dimethyl-L-arginine + H(2)O = dimethylamine + L-citrulline. {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}.
Enzyme Regulation Inhibited by zinc ions (By similarity). Enzyme purified in the absence of 1,10-phenanthroline contains on average 0.4 zinc atoms per subunit. Inhibited by 4-hydroxy-nonenal through the formation of a covalent adduct with His-173. Competitively inhibited by N(5)-iminopropyl-ornithine. {ECO:0000250, ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}.
Function Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Similarity Belongs to the DDAH family. {ECO:0000305}.
Subunit Monomer. {ECO:0000269|PubMed:19663506}.
Tissue Specificity Detected in brain, liver, kidney and pancreas, and at low levels in skeletal muscle. {ECO:0000269|PubMed:10493931}.