1.13.11.46: 4-hydroxymandelate synthase
This is an abbreviated version!
For detailed information about 4-hydroxymandelate synthase, go to the full flat file.
Word Map on EC 1.13.11.46
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1.13.11.46
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benzyl
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dioxygenation
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orientalis
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amycolatopsis
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homogentisate
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oxygenases
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cosmetic
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deuterium
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l-phenylalanine
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benzaldehyde
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charge-transfer
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heterolytic
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nonheme
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vancomycin
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aceto
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carbon-carbon
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biradical
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phenylglyoxylate
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substructure
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ferryl
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1,2-shift
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s-mandelate
- 1.13.11.46
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benzyl
-
dioxygenation
- orientalis
-
amycolatopsis
- homogentisate
- oxygenases
-
cosmetic
- deuterium
- l-phenylalanine
- benzaldehyde
-
charge-transfer
-
heterolytic
-
nonheme
- vancomycin
-
aceto
-
carbon-carbon
-
biradical
- phenylglyoxylate
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substructure
-
ferryl
-
1,2-shift
- s-mandelate
Reaction
Synonyms
(S)-hydroxymandelate synthase, 4-(S) hydroxymandelate synthase, 4-hydroxyphenylpyruvate dioxygenase II, HMS, HPDL, hydroxymandelate synthase, hydroxyphenylpyruvate dioxygenase-like
ECTree
1.13.11.46 4-hydroxymandelate synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.13.11.46 - 4-hydroxymandelate synthase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylpyruvate + O2
4-hydroxymandelate + CO2
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?
4-hydroxyphenylpyruvate + O2
4-hydroxymandelate + CO2
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?
4-hydroxyphenylpyruvate + O2
4-hydroxymandelate + CO2
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alpha-keto acid dependent dioxygenase reaction
substrate of non-ribosomal peptide antibiotics such as vancomycin and chloroeremomycin
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?
4-hydroxyphenylpyruvate + O2
4-hydroxymandelate + CO2
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active site structure and 4-hydroxymandelate binding structure, overview
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?
4-hydroxyphenylpyruvate + O2
4-hydroxymandelate + CO2
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?
additional information
?
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substrate specificity, overview, Hms accepts a range of 2-oxo acids, whereby the presence of an aromatic substituent is crucial for efficient substrate turnover. A hydrophobic substrate binding pocket is identified as the likely determinant of substrate specificity. The enzyme shows high regioselectivity of oxygenation and a strong coupling efficiency of C-C bond cleavage and subsequent hydroxylation. The turnover number of Hms strongly correlates with substrate hydrophobicity. Quantitative structure activity relationship and in silico docking analyses, e.g. with (S)-mandelate and (R)-mandelate, overview
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?
additional information
?
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substrate specificity, overview, Hms accepts a range of 2-oxo acids, whereby the presence of an aromatic substituent is crucial for efficient substrate turnover. A hydrophobic substrate binding pocket is identified as the likely determinant of substrate specificity. The enzyme shows high regioselectivity of oxygenation and a strong coupling efficiency of C-C bond cleavage and subsequent hydroxylation. The turnover number of Hms strongly correlates with substrate hydrophobicity. Quantitative structure activity relationship and in silico docking analyses, e.g. with (S)-mandelate and (R)-mandelate, overview
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?
