Information on EC 2.5.1.111 - 4-hydroxyphenylpyruvate 3-dimethylallyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
2.5.1.111
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RECOMMENDED NAME
GeneOntology No.
4-hydroxyphenylpyruvate 3-dimethylallyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + 4-hydroxyphenylpyruvate = diphosphate + 3-dimethylallyl-4-hydroxyphenylpyruvate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-dimethylallyl-4-hydroxybenzoate biosynthesis
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Novobiocin biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl diphosphate:4-hydroxyphenylpyruvate 3-dimethylallyltransferase
The enzyme is involved in the biosynthesis of the 3-dimethylallyl-4-hydroxyphenylpyruvate moiety of the aminocoumarin antibiotics clorobiocin and novobiocin [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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cloQ-defective mutant of the clorobiocin producer Streptomyces roseochromogenes, which is blocked in the biosynthesis of the prenylated 4-hydroxybenzoic acid moiety of clorobiocin produces three new antibiotics, vanillobiocin, isovanillobiocin and declovanillobiocin. The isolated compounds are similar to clorobiocin, but contain vanillic acid as the acyl component instead of the prenylated 4-hydroxybenzoic acid present in clorobiocin. Isovanillobiocin differs from vanillobiocin by the position of the pyrrole unit attached to the sugar moiety of the antibiotic. Declovanillobiocin lacks the chlorine atom at the aminocoumarin ring. All three compounds have lower antibiotic activity against Bacillus subtilis than clorobiocin
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + 1,6-dihydroxynaphthalene
diphosphate + 1-O-dimethylallyl-1,6-dihydroxynaphthalene
show the reaction diagram
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 1-dimethylallyl-1,6-dihydroxynaphthalene
show the reaction diagram
dimethylallyl diphosphate + 4-coumarate
diphosphate + 3-dimethylallylcoumarate
show the reaction diagram
dimethylallyl diphosphate + 4-coumarate
diphosphate + 4-O-dimethylallylcoumarate
show the reaction diagram
34.4% yield
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-
?
dimethylallyl diphosphate + 4-hydroxyphenylpyruvate
diphosphate + 3-dimethylallyl-4-hydroxyphenylpyruvate
show the reaction diagram
dimethylallyl diphosphate + apigenin
diphosphate + 3'-C-dimethylallyl apigenin
show the reaction diagram
7.6% yield
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?
dimethylallyl diphosphate + caffeate
diphosphate + 3-O,4-O-bis-(dimethylallyl)caffeate
show the reaction diagram
20% yield
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?
dimethylallyl diphosphate + caffeate
diphosphate + 3-O-(dimethylallyl)caffeate
show the reaction diagram
17.3% yield
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?
dimethylallyl diphosphate + caffeate
diphosphate + 4-O-(dimethylallyl)caffeate
show the reaction diagram
26.1% yield
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?
dimethylallyl diphosphate + naringenin
diphosphate + 3'-C-dimethylallyl naringenin
show the reaction diagram
87.2% yield
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?
dimethylallyl diphosphate + naringenin
diphosphate + 4'-O-dimethylallyl naringenin
show the reaction diagram
11.1% yield
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?
dimethylallyl diphosphate + resveratrol
diphosphate + 3'-dimethylallyl resveratrol
show the reaction diagram
12.3% yield
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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
dimethylallyl diphosphate + 4-hydroxyphenylpyruvate
diphosphate + 3-dimethylallyl-4-hydroxyphenylpyruvate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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the addition of Ca2+ (2.5 mM) instead of Mg2+ results in 70% of the activity obtained with Mg2+
Mg2+
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activates, 2.5 mM is the most effecive concentration. In the absence of divalent cations and in the presence of 5 mM EDTA, the enzyme retains 25% of its original activity. The enzyme is not dependent on the presence of Mg2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
even in the presence of 5mM EDTA, NovQ possessed full enzymatic activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0151 - 0.025
4-hydroxyphenylpyruvate
0.025 - 0.035
dimethylallyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.083 - 0.159
4-hydroxyphenylpyruvate
0.253
dimethylallyl diphosphate
Streptomyces roseochromogenus subsp. oscitans
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pH 7.5, 30C, wild-type
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.04 - 9.94
4-hydroxyphenylpyruvate
423
10.12
dimethylallyl diphosphate
Streptomyces roseochromogenus subsp. oscitans
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pH 7.5, 30C, wild-type
157
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging-drop vapor diffusion at 20 C. Structure of of the apoenzyme, of CloQ complexed with 4-hydroxyphenylpyruvate, of mutant enzyme C215S complexed with 4-hydroxyphenylpyruvate and of the mutant enzyme R66S complexed with 4-hydroxyphenylpyruvate. Structure of CloQ complexed with 4-hydroxyphenylpyruvate reveals the formation of a covalent link between the substrate and Cys215 to yield a thiohemiketal species
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crystals are grown by vapour diffusion. The protein crystallizes in space group I4(1)22, with unit-cell parameters a = b = 135.19, c = 98.13 A. Native data from a single crystal are recorded to a resolution of 2.2 A in-house
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli as an N-terminal His8-tagged protein
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C215A
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activity is comparable to that of the wild-type enzyme
C215S
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activity is comparable to that of the wild-type enzyme
E281G
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mutant enzyme shows 1% of wild-type activity
R160A
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mutant enzyme shows 17.3% of wild-type activity
R160Q
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mutant enzyme shows 19.7% of wild-type activity
R66S
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mutant enzyme shows 1.9% of wild-type activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis