KEGG   ENZYME: 1.14.16.6
Entry
EC 1.14.16.6                Enzyme                                 

Name
mandelate 4-monooxygenase;
L-mandelate 4-hydroxylase;
mandelic acid 4-hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
(S)-2-hydroxy-2-phenylacetate,tetrahydropteridine:oxygen oxidoreductase (4-hydroxylating)
Reaction(IUBMB)
(S)-2-hydroxy-2-phenylacetate + a 5,6,7,8-tetrahydropteridine + O2 = (S)-4-hydroxymandelate + a 4a-hydroxy-5,6,7,8-tetrahydropteridine [RN:R03794]
Reaction(KEGG)
R03794
Substrate
(S)-2-hydroxy-2-phenylacetate [CPD:C01984];
5,6,7,8-tetrahydropteridine [CPD:C05650];
O2 [CPD:C00007]
Product
(S)-4-hydroxymandelate [CPD:C03198];
4a-hydroxy-5,6,7,8-tetrahydropteridine [CPD:C22239]
Comment
Requires Fe2+. The enzyme has been characterized from the bacterium Pseudomonas putida. The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, 6,7-dihydropteridine reductase, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine.
History
EC 1.14.16.6 created 1984, modified 2020
Pathway
ec00627  Aminobenzoate degradation
ec01120  Microbial metabolism in diverse environments
Reference
1  [PMID:9909]
  Authors
Bhat SG, Vaidyanathan CS.
  Title
Purifications and properties of L-mandelate- 4-hydroxylase from Pseudomonas convexa.
  Journal
Arch Biochem Biophys 176:314-23 (1976)
DOI:10.1016/0003-9861(76)90170-3
Other DBs
ExplorEnz - The Enzyme Database: 1.14.16.6
IUBMB Enzyme Nomenclature: 1.14.16.6
ExPASy - ENZYME nomenclature database: 1.14.16.6
BRENDA, the Enzyme Database: 1.14.16.6
CAS: 39459-82-0

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