Melilotate 3-monooxygenase
| Melilotate 3-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.4 | ||||||||
| CAS no. | 37256-72-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Melilotate 3-monooxygenase (EC 1.14.13.4) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are melilotic acid, reduced nicotinamide adenine dinucleotide (NADH), oxygen. and a proton. Its products are 2,3-dihydroxyphenylpropionic acid, oxidised NAD+, and water.[1][2][3]
The enzyme is a flavin-containing monooxygenase that uses molecular oxygen as oxidant and incorporates one of its atoms into the starting material. 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. It participates in phenylalanine metabolism. It uses flavin adenine dinucleotide as a cofactor.[4][5][6]
References
- ↑ Enzyme 1.14.13.4 at KEGG Pathway Database.
- ↑ Levy CC (1967). "Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group". J. Biol. Chem. 242 (4): 747–53. doi:10.1016/S0021-9258(18)96268-X. PMID 6017743.
- ↑ Levy CC, Frost P (1966). "The metabolism of coumarin by a microorganism. V. Melilotate hydroxylase". J. Biol. Chem. 241 (4): 997–1003. doi:10.1016/S0021-9258(18)96862-6. PMID 4285850.
- ↑ Strickland S, Massey V (1973). "The purification and properties of the flavoprotein melilotate hydroxylase". J. Biol. Chem. 248 (8): 2944–52. doi:10.1016/S0021-9258(19)44099-4. PMID 4348920.
- ↑ Strickland S, Massey V (1973). "The mechanism of action of the flavoprotein melilotate hydroxylase". J. Biol. Chem. 248 (8): 2953–62. doi:10.1016/S0021-9258(19)44100-8. PMID 4348921.
- ↑ Montersino, Stefania; Tischler, Dirk; Gassner, George T.; Van Berkel, Willem J. H. (2011). "Catalytic and Structural Features of Flavoprotein Hydroxylases and Epoxidases". Advanced Synthesis & Catalysis. 353 (13): 2301–2319. doi:10.1002/adsc.201100384.