3,4-dihydroxyphenylalanine oxidative deaminase

3,4-dihydroxyphenylalanine oxidative deaminase (EC 1.13.12.15, 3,4-dihydroxy-L-phenylalanine: oxidative deaminase, oxidative deaminase, DOPA oxidative deaminase, DOPAODA) is an enzyme with systematic name 3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating).^[1] This enzyme catalyses the following chemical reaction

2 L-dopa + O₂

\rightleftharpoons

2 3,4-dihydroxyphenylpyruvate + 2 NH₃

This enzyme is one of the three enzymes involved in L-dopa (3,4-dihydroxy-L-phenylalanine) catabolism in the bacterium Rubrivivax benzoatilyticus.

References

↑ Ranjith, N.K., Ramana, Ch.V. and Sasikala, Ch. (2008). "Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase from Rhodobacter sphaeroides OU5". Can. J. Microbiol. 54 (10): 829–834. doi:10.1139/w08-071. PMID 18923551.

External links

3,4-dihydroxyphenylalanine oxidative deaminase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: monooxygenases (EC 1.13)

1.13.11: two atoms of oxygen	lipoxygenase: Arachidonate 5-lipoxygenase Arachidonate 12-lipoxygenase/ALOX12 Arachidonate 8-lipoxygenase Arachidonate 15-lipoxygenase/ALOX15 Linoleate 11-lipoxygenase other dioxygenase: Catechol dioxygenase Homogentisate 1,2-dioxygenase Cysteine dioxygenase 4-Hydroxyphenylpyruvate dioxygenase Indoleamine 2,3-dioxygenase Chlorite dismutase

1.13.12: one atom of oxygen	Firefly luciferase

1.13.99: other	Inositol oxygenase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.