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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.
Reaction Schemes
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9-prenyl-5,10-dihydrophenazine-1-carboxylate
Synonyms
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5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase
dihydrophenazine-1-carboxylate dimethylallyltransferase
dimethylallyl diphosphate:5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
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5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase
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5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase
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dihydrophenazine-1-carboxylate dimethylallyltransferase
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dihydrophenazine-1-carboxylate dimethylallyltransferase
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Ppzp
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prenyl diphosphate + 5,10-dihydrophenazine-1-carboxylate = diphosphate + 9-prenyl-5,10-dihydrophenazine-1-carboxylate
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prenyl-diphosphate:5,10-dihydrophenazine-1-carboxylate 9-prenyltransferase
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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dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
Substrates: the enzyme is involved in the biosynthesis of prenylated phenazines
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dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
Substrates: the enzyme is specific for both dimethylallyl diphosphate and 5,10-dihydrophenazine 1-carboxylate. No activity with geranyldiphosphate or other phenazine substrates, such as phenazine, phenazine 1-carboxylic acid methyl ester, N-methyl-phenazine, or pyocyanine (1-hydroxy-5-N-methyl-phenazine). No activity with 4-hydroxyphenylpyruvate 1,3-dihydroxynaphthalene, and 1,6-dihydroxynaphthalene. Reaction velocity with flaviolin is 0.5% compared to the activity with 5,10-dihydrophenazine 1-carboxylate
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dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
Substrates: the enzyme is involved in the biosynthesis of prenylated phenazines
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dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
Substrates: the enzyme is specific for both dimethylallyl diphosphate and 5,10-dihydrophenazine 1-carboxylate. No activity with geranyldiphosphate or other phenazine substrates, such as phenazine, phenazine 1-carboxylic acid methyl ester, N-methyl-phenazine, or pyocyanine (1-hydroxy-5-N-methyl-phenazine). No activity with 4-hydroxyphenylpyruvate 1,3-dihydroxynaphthalene, and 1,6-dihydroxynaphthalene. Reaction velocity with flaviolin is 0.5% compared to the activity with 5,10-dihydrophenazine 1-carboxylate
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dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
Substrates: the enzyme is involved in the biosynthesis of prenylated phenazines
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dimethylallyl diphosphate + 5,10-dihydrophenazine 1-carboxylate
diphosphate + 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate
Substrates: the enzyme is involved in the biosynthesis of prenylated phenazines
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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
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FeSO4
10 mM, completely abolishes the formation of endophenazine A
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EDTA
10 mM, increases reaction velocity 1.5fold
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0.035
5,10-dihydrophenazine 1-carboxylate
pH 7.5, 30°C
0.116
dimethylallyl diphosphate
pH 7.5, 30°C
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0.435
5,10-dihydrophenazine 1-carboxylate
pH 7.5, 30°C
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12.4
5,10-dihydrophenazine 1-carboxylate
pH 7.5, 30°C
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5 - 9.5
pH 5.0: about 50% of maximal activity, ph 9.5: about 50% of maximal activity
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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malfunction
after inactivation of ppzP, only nonprenylated phenazine 1-carboxylic acid is formed
malfunction
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after inactivation of ppzP, only nonprenylated phenazine 1-carboxylic acid is formed
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physiological function
the enzyme is involved in the biosynthesis of prenylated phenazines
physiological function
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the enzyme is involved in the biosynthesis of prenylated phenazines
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PPZP_STRAQ
299
0
33012
Swiss-Prot
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37000
x * 37000, SDS-PAGE
37138
x * 37138, calculated from sequence
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x * 37000, SDS-PAGE
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x * 37138, calculated from sequence
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x * 37000, SDS-PAGE
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x * 37138, calculated from sequence
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heterologous expression in Streptomyces coelicolor M512
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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
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