EC |
1.13.12.15 |
Accepted name: |
3,4-dihydroxyphenylalanine oxidative deaminase |
Reaction: |
2 L-dopa + O2 = 2 3,4-dihydroxyphenylpyruvate + 2 NH3 |
Glossary: |
L-dopa = 3,4-dihydroxy-L-phenylalanine |
Other name(s): |
3,4-dihydroxy-L-phenylalanine: oxidative deaminase; oxidative deaminase; DOPA oxidative deaminase; DOPAODA |
Systematic name: |
3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating) |
Comments: |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ranjith, N.K., Ramana, Ch.V. and Sasikala, Ch. Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase from Rhodobacter sphaeroides OU5. Can. J. Microbiol. 54 (2008) 829–834. [DOI] [PMID: 18923551] |
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[EC 1.13.12.15 created 2008] |
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