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IUBMB Comments The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. It can also act on phenazine-1-carboxylate, converting it into phenazin-1-ol.
The enzyme appears in viruses and cellular organisms
Synonyms
PA4217,
phzS ,
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phzS
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5-methylphenazine-1-carboxylate + NADH + O2 = pyocyanin + NAD+ + CO2 + H2O
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5-methylphenazine-1-carboxylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. It can also act on phenazine-1-carboxylate, converting it into phenazin-1-ol.
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
additional information
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phenazine-1-carboxylic acid is a poor substrate
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
additional information
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phenazine-1-carboxylic acid is a poor substrate
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
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5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
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FAD
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NADH
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UniProt
brenda
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UniProt
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UniProt
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PHZS_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
402
0
43645
Swiss-Prot
A0A5E8CEW1_9BRAD
413
0
44513
TrEMBL
A0A5E7Z232_9RHIZ
427
0
45751
TrEMBL
PHZM_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
334
0
36357
Swiss-Prot
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Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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43600
x * 43600, calculated from amino acid sequence
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homodimer
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2 * 43600, calculated from amino acid sequence
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x * 43600, calculated from amino acid sequence
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x * 42650, laser light scattering; x * 43926, calculated from amino acid sequence
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native and seleno-L-methionine-labelled enzyme, hanging drop vapor diffusion method, using 0.7-1.0 M lithium sulfate, 0.1 M sodium citrate pH 5.0–5.5, 0.5 M ammonium sulfate or 14-17% (w/v) PEG 10 000, 0.1 M ammonium acetate, 0.1 M Bis-Tris pH 5.5 and 23-26% (w/v) PEG 3350, 0.1 M Bis-Tris pH 5.8-6.0, 0.2 M ammonium sulfate
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Ni-NTA affinity resin column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)Gold cells
expressed in Escherichia coli Rosetta pLysS cells
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Mavrodi, D.V.; Bonsall, R.F.; Delaney, S.M.; Soule, M.J.; Phillips, G.; Thomashow, L.S.
Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1
J. Bacteriol.
183
6454-6465
2001
Pseudomonas aeruginosa (Q9HWG9)
brenda
Gohain, N.; Thomashow, L.S.; Mavrodi, D.V.; Blankenfeldt, W.
The purification, crystallization and preliminary structural characterization of FAD-dependent monooxygenase PhzS, a phenazine-modifying enzyme from Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
62
989-992
2006
Pseudomonas aeruginosa
brenda
Parsons, J.F.; Greenhagen, B.T.; Shi, K.; Calabrese, K.; Robinson, H.; Ladner, J.E.
Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa
Biochemistry
46
1821-1828
2007
Pseudomonas aeruginosa (Q9HWH2)
brenda
Greenhagen, B.T.; Shi, K.; Robinson, H.; Gamage, S.; Bera, A.K.; Ladner, J.E.; Parsons, J.F.
Crystal structure of the pyocyanin biosynthetic protein PhzS
Biochemistry
47
5281-5289
2008
Pseudomonas aeruginosa (Q9HWG9)
brenda
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Enzyme Nomenclature
1.14.13.218 5-methylphenazine-1-carboxylate 1-monooxygenase
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