KEGG   ENZYME: 1.14.13.4Help
Entry
EC 1.14.13.4                Enzyme                                 

Name melilotate 3-monooxygenase;
2-hydroxyphenylpropionate hydroxylase;
melilotate hydroxylase;
2-hydroxyphenylpropionic hydroxylase;
melilotic hydroxylase
Class Oxidoreductases;
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 of
oxygen into the other donor
BRITE hierarchy
Sysname 3-(2-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase
(3-hydroxylating)
Reaction(IUBMB) 3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 =
3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O [RN:R03369]
Reaction(KEGG) R03369
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Substrate 3-(2-hydroxyphenyl)propanoate [CPD:C01198];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product 3-(2,3-dihydroxyphenyl)propanoate [CPD:C04044];
NAD+ [CPD:C00003];
H2O [CPD:C00001]
Cofactor FAD [CPD:C00016]
Comment A flavoprotein (FAD).
Pathway PATH: ec00360  Phenylalanine metabolism
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:6017743]
Levy CC.
Melilotate hydroxylase. Purification of the enzyme and the nature of
the prosthetic group.
J. Biol. Chem. 242 (1967) 747-53.
Arthrobacter sp.
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:4285850]
Levy CC, Frost P.
The metabolism of coumarin by a microorganism. V. Melilotate
hydroxylase.
J. Biol. Chem. 241 (1966) 997-1003.
Arthrobacter sp.
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:4348920]
Strickland S, Massey V.
The purification and properties of the flavoprotein melilotate
hydroxylase.
J. Biol. Chem. 248 (1973) 2944-52.
Pseudomonas sp.
Reference
  Authors
  Title
  Journal
  Organism
4  [PMID:4348921]
Strickland S, Massey V.
The mechanism of action of the flavoprotein melilotate hydroxylase.
J. Biol. Chem. 248 (1973) 2953-62.
Pseudomonas sp.
Other DBs ExplorEnz - The Enzyme Database: 1.14.13.4
IUBMB Enzyme Nomenclature: 1.14.13.4
ExPASy - ENZYME nomenclature database: 1.14.13.4
BRENDA, the Enzyme Database: 1.14.13.4
CAS: 37256-72-7

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