Information on EC 1.14.13.218 - 5-methylphenazine-1-carboxylate 1-monooxygenase

for references in articles please use BRENDA:EC1.14.13.218
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The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa

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EC NUMBER
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1.14.13.218
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RECOMMENDED NAME
GeneOntology No.
5-methylphenazine-1-carboxylate 1-monooxygenase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
5-methylphenazine-1-carboxylate + NADH + O2 = pyocyanin + NAD+ + CO2 + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyocyanin biosynthesis
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Phenazine biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
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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ORGANISM
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LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
show the reaction diagram
additional information
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phenazine-1-carboxylic acid is a poor substrate
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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
5-methylphenazine-1-carboxylate + NADH + O2
pyocyanin + NAD+ + CO2 + H2O
show the reaction diagram
additional information
?
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Q9HWH2
phenazine-1-carboxylic acid is a poor substrate
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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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MOLECULAR WEIGHT
ORGANISM
UNIPROT
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LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
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LITERATURE
homodimer
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2 * 43600, calculated from amino acid sequence
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity resin column chromatography and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3)Gold cells
expressed in Escherichia coli Rosetta pLysS cells
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.218)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)