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EC Tree
IUBMB Comments 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.
The expected taxonomic range for this enzyme is: Pseudomonas putida
Reaction Schemes
+
+
=
+
a 4a-hydroxy-5,6,7,8-tetrahydropteridine
Synonyms
L-mandelate-4-hydroxylase, mandelic acid 4-hydroxylase, oxygenase, mandelate 4-mono-,
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L-mandelate-4-hydroxylase
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mandelic acid 4-hydroxylase
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-
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oxygenase, mandelate 4-mono-
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-
-
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(S)-2-hydroxy-2-phenylacetate + a 5,6,7,8-tetrahydropteridine + O2 = (S)-4-hydroxymandelate + a 4a-hydroxy-5,6,7,8-tetrahydropteridine
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-
-
-
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(S)-2-hydroxy-2-phenylacetate,tetrahydropteridine:oxygen oxidoreductase (4-hydroxylating)
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.
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(S)-2-hydroxy-2-phenylacetate + tetrahydropteridine
(S)-4-hydroxymandelate + dihydropteridine + H2O
(S)-2-hydroxy-2-phenylacetate + tetrahydropteridine + O2
?
-
i.e. L-mandelate, first step of oxidative degradation of L-mandelate by Pseudomonas convexa
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-
?
(S)-2-hydroxy-2-phenylacetate + tetrahydropteridine
(S)-4-hydroxymandelate + dihydropteridine + H2O
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-
-
?
(S)-2-hydroxy-2-phenylacetate + tetrahydropteridine
(S)-4-hydroxymandelate + dihydropteridine + H2O
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-
-
?
(S)-2-hydroxy-2-phenylacetate + tetrahydropteridine
(S)-4-hydroxymandelate + dihydropteridine + H2O
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i.e. L-mandelate, highly substrate specific, D-mandelate is not hydroxylated
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?
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(S)-2-hydroxy-2-phenylacetate + tetrahydropteridine + O2
?
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i.e. L-mandelate, first step of oxidative degradation of L-mandelate by Pseudomonas convexa
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-
?
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NADPH
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-
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Fe2+
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required
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1,10-phenanthroline
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0.5 mM, 88% inhibition
2,2'-bipyridyl
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0.5 mM, 83% inhibition
2-amino-4-hydroxy-6,7-dimethyl-tetrahydropteridine
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above 0.000025 mM, slight inhibition
4-hydroxymercuribenzoate
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partially reversible by thiol compounds
8-hydroxyquinoline
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0.5 mM, 60% inhibition
Ag2+
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0.0001 mM, 42% inhibition
Cd2+
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0.0001 mM, 66% inhibition
Cu2+
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0.0001 mM, 40% inhibition
diethyldithiocarbamate
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0.5 mM, 16% inhibition
EDTA
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0.5 mM, 64% inhibition
guanidine hydrochloride
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2.0 mM, 95% inhibition
Hg2+
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0.0001 mM, 56% inhibition
SDS
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0.1 mM, complete inhibition
Thiourea
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1.0 mM, complete inhibition
Urea
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2.0 mM, complete inhibition
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2-amino-4-hydroxy-6,7-dimethyl-tetrahydropteridine
tetrahydrofolic acid
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pteridine cofactor required, 50% of the activity of 2-amino-4-hydroxy-6,7-dimethyl-tetrahydropteridine
tetrahydropteridine
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required
2-amino-4-hydroxy-6,7-dimethyl-tetrahydropteridine
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-
2-amino-4-hydroxy-6,7-dimethyl-tetrahydropteridine
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pteridine cofactor required, 2-amino-4-hydroxy-6,7-dimethyl-tetrahydropteridine is most effective, optimal concentration is 0.000025 mM
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0.1
(S)-2-Hydroxy-2-phenylacetate
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-
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5.4
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5.4
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citrate-phosphate buffer
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4.6 - 7.4
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half-maximal activity at pH 4.6 and pH 7.4
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brenda
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brenda
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55
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5 min, no loss of activity
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-20°C, partially purified enzyme is stable for 36-40 h
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Bhat, S.G.; Vaidyanathan, C.S.
Involvement of 4-hydroxymandelic acid in the degradation of mandelic acid by Pseudomonas convexa
J. Bacteriol.
127
1108-1118
1976
Pseudomonas putida
brenda
Bhat, S.G.; Ramanarayanan, M.; Vaidyanathan, C.S.
Mandelic acid-4-hydroxylase, a new inducible enzyme from Pseudomonas convexa
Biochem. Biophys. Res. Commun.
52
834-842
1973
Pseudomonas putida
brenda
Bhat, S.G.; Vaidyanathan, C.S.
Purifications and properties of L-mandelate-4-hydroxylase from Pseudomonas convexa
Arch. Biochem. Biophys.
176
314-323
1976
Pseudomonas putida
brenda
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1.14.16.6 mandelate 4-monooxygenase
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