Information on EC 1.13.11.46 - 4-hydroxymandelate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.46
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RECOMMENDED NAME
GeneOntology No.
4-hydroxymandelate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative decarboxylation
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of vancomycin group antibiotics
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Monobactam biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
Requires Fe2+. Involved in the biosynthesis of the vancomycin group of glycopeptide antibiotics.
CAS REGISTRY NUMBER
COMMENTARY hide
280566-04-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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4-hydroxyphenylpyruvate dioxygenase, HPPD, EC 1.13.11.27, and hydroxymandelate synthase catalyze similar reactions using the same substrates, 4-hydroxyphenylpyruvate and dioxygen. Initially, both enzymes reduce and activate dioxygen in order to decarboxylate 4-hydroxyphenylpyruvate, yielding 4-hydroxyphenylacetate, CO2, and an activated oxo intermediate. Both enzymes then hydroxylate 4-hydroxyphenylacetate but do so in different positions
malfunction
additional information
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molecular docking and modeling, molecular dynamics and simulations by classical molecular dynamics simulations, simulated HMS-Fe(IV)-O-HPA species, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-4-phenylbutanoic acid + O2
?
show the reaction diagram
4-fluorophenylpyruvic acid + O2
?
show the reaction diagram
4-hydroxyphenylpyruvate + O2
4-hydroxymandelate + CO2
show the reaction diagram
4-methoxyphenylpyruvic acid + O2
?
show the reaction diagram
4-methylphenylpyruvic acid + O2
?
show the reaction diagram
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-
-
-
?
4-nitrophenylpyruvic acid + O2
?
show the reaction diagram
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-
-
-
?
phenylpyruvic acid + O2
?
show the reaction diagram
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-
-
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylpyruvate + O2
4-hydroxymandelate + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[2-nitro-4-(triflouromethyl)benzoyl]-1,3-cyclohexanedione
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anaerobic conditions, complex with Fe2+ and enzyme, a herbicide/therapeutic that inhibits 4-hydroxyphenylpyruvate dioxygenase in a similar manner
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
2-oxo-4-phenylbutanoic acid
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pH 7.5, 25C
0.0143 - 0.22
4-hydroxyphenylpyruvate
0.16
4-methoxyphenylpyruvic acid
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pH 7.5, 25C
0.353
phenylpyruvic acid
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pH 7.5, 25C
additional information
additional information
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steady-state kinetic analysis, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
2-oxo-4-phenylbutanoic acid
Streptomyces coelicolor
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pH 7.5, 25C
0.077
4-fluorophenylpyruvic acid
Streptomyces coelicolor
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pH 7.5, 25C
1.2 - 4.5
4-hydroxyphenylpyruvate
0.96
4-methoxyphenylpyruvic acid
Streptomyces coelicolor
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pH 7.5, 25C
0.13
4-methylphenylpyruvic acid
Streptomyces coelicolor
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pH 7.5, 25C
0.035
4-nitrophenylpyruvic acid
Streptomyces coelicolor
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pH 7.5, 25C
0.88
phenylpyruvic acid
Streptomyces coelicolor
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pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
57.5 - 108
4-hydroxyphenylpyruvate
423
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40368
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alpha,alpha, 2 * 40368, gel filtration, electrospray mass spectrometry
80000
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gel filtration, electrospray mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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alpha,alpha, 2 * 40368, gel filtration, electrospray mass spectrometry
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
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hanging drop method, the crystal structure of the hydroxymandelate synthase/Co2+/hydroxymandelate complex determined to a resolution of 2.3 A
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally strep-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
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recombinant His-tagged protein, Ni-NTA resin
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recombinant wild-type and mutant enzymes by ammonium sulfate fractionation, anion echange chromatography, and gel filtration
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recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expression of C-terminally strep-tagged enzyme in Escherichia coli strain BL21(DE3)
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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recombinant expression of wild-type and mutant enzymes
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I216N
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site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme, the mutant produces 90% 4-hydroxmandelate and 10% 4-hydroxyphenylacetate from 4-hydroxyphenylpyruvate, which differs from the wild-type, that does not produce any 4-hydroxyphenylacetate
T214P
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site-directed mutagenesis, mutant shows decreased catalytic efficiency compared to the wild-type enzyme