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Enzyme Nomenclature
Information on EC 2.5.1.B25 - 2,7-dihydroxynaphthalene 3-dimethylallyltransferase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.5.1.B25
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
2,7-dihydroxynaphthalene 3-dimethylallyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene = diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene = diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
Friedel-Crafts alkylation
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene = diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
Friedel-Crafts alkylation
-
-
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene = diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl diphosphate:2,7-dihydroxynaphthalene 3-dimethylallyltransferase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
the enzyme is specific for dimethylallyl diphosphate. No activity with geranyl diphosphate or isopentenyl diphosphate
-
-
?
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
the enzyme is specific for dimethylallyl diphosphate. No activity with geranyl diphosphate or isopentenyl diphosphate
-
-
?
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
-
the enzyme is specific for dimethylallyl diphosphate. No activity with geranyl diphosphate or isopentenyl diphosphate
-
-
?
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
-
the enzyme is specific for dimethylallyl diphosphate. No activity with geranyl diphosphate or isopentenyl diphosphate
-
-
?
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
-
the enzyme is specific for dimethylallyl diphosphate. No activity with geranyl diphosphate or isopentenyl diphosphate
-
-
?
dimethylallyl diphosphate + 2,7-dihydroxynaphthalene
diphosphate + 2,7-dihydroxy-3-dimethylallylnaphthalene
-
the enzyme is specific for dimethylallyl diphosphate. No activity with geranyl diphosphate or isopentenyl diphosphate
-
-
?
additional information
?
-
significantly lower level of prenylation activity with dihydrophenazine-1-carboxylic acid as aromatic substrate, and only traces of products are detected with aspulvinone E, flaviolin, or 4-hydroxybenzoic acid. No product is formed with L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate
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-
-
additional information
?
-
significantly lower level of prenylation activity with dihydrophenazine-1-carboxylic acid as aromatic substrate, and only traces of products are detected with aspulvinone E, flaviolin, or 4-hydroxybenzoic acid. No product is formed with L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate
-
-
-
additional information
?
-
-
significantly lower level of prenylation activity with dihydrophenazine-1-carboxylic acid or 4-hydroxybenzoate as aromatic substrate, and only traces of products are detected with aspulvinone E, flaviolin. No product is formed with L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate
-
-
-
additional information
?
-
-
significantly lower level of prenylation activity with dihydrophenazine-1-carboxylic acid or 4-hydroxybenzoate as aromatic substrate, and only traces of products are detected with aspulvinone E, flaviolin. No product is formed with L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate
-
-
-
additional information
?
-
-
significantly lower level of prenylation activity with dihydrophenazine-1-carboxylic acid as aromatic substrate, and only traces of products are detected with aspulvinone E, flaviolin, or 4-hydroxybenzoic acid. No product is formed with L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate
-
-
-
additional information
?
-
-
significantly lower level of prenylation activity with dihydrophenazine-1-carboxylic acid as aromatic substrate, and only traces of products are detected with aspulvinone E, flaviolin, or 4-hydroxybenzoic acid. No product is formed with L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
addition of MgCl2 to the incubation mixture increases the reaction velocity. The optimal concentration of MgCl2 is 10 mM, leading to a 2.4-fold increase of product formation. The enzyme shows catalytic activity in the complete absence of Mg2+ or any other divalent cation
Mg2+
-
the enzyme is active in the absence of Mg2+, but addition of 10 mM MgCl2 increases reaction velocity by a factor of 2.6
Mg2+
-
the enzyme is active in the absence of Mg2+, but addition of 10 mM MgCl2 increases reaction velocity by a factor of 2.6
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.1 - 9.4
pH 8.1: about 50% of maximal activity, pH 9.4: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a His8-tagged protein
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LINKS TO OTHER DATABASES (specific for EC-Number 2.5.1.B25)
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