Melilotate 3-monooxygenase

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In enzymology, a melilotate 3-monooxygenase (EC 1.14.13.4) is an enzyme that catalyzes the chemical reaction

3-(2-hydroxyphenyl)propanoate + NADH + H⁺ + O₂ $\rightleftharpoons$ 3-(2,3-dihydroxyphenyl)propanoate + NAD⁺ + H₂O

The 4 substrates of this enzyme are 3-(2-hydroxyphenyl)propanoate, NADH, H⁺, and O₂, whereas its 3 products are 3-(2,3-dihydroxyphenyl)propanoate, NAD⁺, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 3-(2-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include 2-hydroxyphenylpropionate hydroxylase, melilotate hydroxylase, 2-hydroxyphenylpropionic hydroxylase, and melilotic hydroxylase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, FAD.

[edit] References

IUBMB entry for 1.14.13.4
BRENDA references for 1.14.13.4 (Recommended.)
PubMed references for 1.14.13.4
PubMed Central references for 1.14.13.4
Google Scholar references for 1.14.13.4
Levy CC (1967). "Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group". J. Biol. Chem. 242: 747–53. PMID 6017743.
Levy CC, Frost P (1966). "The metabolism of coumarin by a microorganism. V. Melilotate hydroxylase". J. Biol. Chem. 241: 997–1003. PMID 4285850.
Strickland S, Massey V (1973). "The purification and properties of the flavoprotein melilotate hydroxylase". J. Biol. Chem. 248: 2944–52. PMID 4348920.
Strickland S, Massey V (1973). "The mechanism of action of the flavoprotein melilotate hydroxylase". J. Biol. Chem. 248: 2953–62. PMID 4348921.