KEGG   ENZYME: 1.13.12.15
Entry
EC 1.13.12.15               Enzyme                                 
Name
3,4-dihydroxyphenylalanine oxidative deaminase;
3,4-dihydroxy-L-phenylalanine: oxidative deaminase;
oxidative deaminase;
DOPA oxidative deaminase;
DOPAODA
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
Sysname
3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating)
Reaction(IUBMB)
2 L-dopa + O2 = 2 3,4-dihydroxyphenylpyruvate + 2 NH3 [RN:R08920]
Reaction(KEGG)
R08920
Substrate
L-dopa [CPD:C00355];
O2 [CPD:C00007]
Product
3,4-dihydroxyphenylpyruvate [CPD:C04045];
NH3 [CPD:C00014]
Comment
This enzyme is one of the three enzymes involved in L-dopa (3,4-dihydroxy-L-phenylalanine) catabolism in the non-oxygenic phototrophic bacterium Rubrivivax benzoatilyticus OU5 (and not Rhodobacter sphaeroides OU5 as had been thought [1]), the other two being EC 4.3.1.22 (dihydroxyphenylalanine reductive deaminase) and EC 2.6.1.49 (3,4-dihydroxyphenylalanine transaminase). In addition to L-dopa, the enzyme can also use L-tyrosine, L-phenylalanine, L-tryptophan and glutamate as substrate, but more slowly. The enzyme is inhibited by NADH and 2-oxoglutarate.
History
EC 1.13.12.15 created 2008
Pathway
ec00350  Tyrosine metabolism
ec01100  Metabolic pathways
Reference
1  [PMID:18923551]
  Authors
Ranjith NK, Ramana ChV, Sasikala Ch
  Title
Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase from Rhodobacter sphaeroides OU5.
  Journal
Can J Microbiol 54:829-34 (2008)
DOI:10.1139/w08-071
Other DBs
ExplorEnz - The Enzyme Database: 1.13.12.15
IUBMB Enzyme Nomenclature: 1.13.12.15
ExPASy - ENZYME nomenclature database: 1.13.12.15
BRENDA, the Enzyme Database: 1.13.12.15
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