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Information on EC 2.5.1.121 - 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase and Organism(s) Streptomyces anulatus and UniProt Accession C4PWA1

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IUBMB Comments
The enzyme is involved in the biosynthesis of prenylated phenazines by the bacterium Streptomyces anulatus. It is specific for both prenyl diphosphate and 5,10-dihydrophenazine-1-carboxylate.
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This record set is specific for:
Streptomyces anulatus
UNIPROT: C4PWA1
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The taxonomic range for the selected organisms is: Streptomyces anulatus
The enzyme appears in selected viruses and cellular organisms
Synonyms
5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase, dihydrophenazine-1-carboxylate dimethylallyltransferase, Ppzp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase
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dihydrophenazine-1-carboxylate dimethylallyltransferase
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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 prenyl diphosphate and 5,10-dihydrophenazine-1-carboxylate.
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 SUBSTRATE
NATURAL 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
the enzyme is involved in the biosynthesis of prenylated phenazines
-
-
?
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
INHIBITOR
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, 30°C
0.116
dimethylallyl diphosphate
pH 7.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.435
5,10-dihydrophenazine 1-carboxylate
pH 7.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.4
5,10-dihydrophenazine 1-carboxylate
pH 7.5, 30°C
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
after inactivation of ppzP, only nonprenylated phenazine 1-carboxylic acid is formed
physiological function
the enzyme is involved in the biosynthesis of prenylated phenazines
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPZP_STRAQ
299
0
33012
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37000, SDS-PAGE
37138
x * 37138, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologous expression in Streptomyces coelicolor M512
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saleh, O.; Gust, B.; Boll, B.; Fiedler, H.P.; Heide, L.
Aromatic prenylation in phenazine biosynthesis: dihydrophenazine-1-carboxylate dimethylallyltransferase from Streptomyces anulatus
J. Biol. Chem.
284
14439-14447
2009
Streptomyces anulatus (C4PWA1), Streptomyces anulatus, Streptomyces anulatus 9663 (C4PWA1), Streptomyces anulatus 9663
Manually annotated by BRENDA team