Information on EC 2.5.1.121 - 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces anulatus

EC NUMBER
COMMENTARY hide
2.5.1.121
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RECOMMENDED NAME
GeneOntology No.
5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + 5,10-dihydrophenazine-1-carboxylate = diphosphate + 9-(dimethylallyl)-5,10-dihydrophenazine-1-carboxylate
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl diphosphate:5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
The enzyme is involved in the biosynthesis of prenylated phenazines by the bacterium Streptomyces anulatus. It is specific for both dimethylallyl diphosphate and 5,10-dihydrophenazine-1-carboxylate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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 + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
show the reaction diagram
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 + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
100 mM MgCl2 increases product formation 1.5fold
Mg2+
the enzyme is independent of the presence of magnesium or other divalent cations. 50 mM MgCl2 increases product formation 1.5fold
Na+
500 mM, NaCl increases product formation 3fold
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FeSO4
10 mM, completely abolishes the formation of endophenazine A
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
10 mM, increases reaction velocity 1.5fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
5,10-dihydrophenazine 1-carboxylate
pH 7.5, 30C
0.116
dimethylallyl diphosphate
pH 7.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.435
5,10-dihydrophenazine 1-carboxylate
Streptomyces anulatus
C4PWA1
pH 7.5, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.4
5,10-dihydrophenazine 1-carboxylate
Streptomyces anulatus
C4PWA1
pH 7.5, 30C
29156
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
pH 5.0: about 50% of maximal activity, ph 9.5: about 50% of maximal activity
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heterologous expression in Streptomyces coelicolor M512