Entry |
|
Name |
5-methylphenazine-1-carboxylate 1-monooxygenase;
phzS (gene name)
|
Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
|
Sysname |
5-methylphenazine-1-carboxylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
|
Reaction(IUBMB) |
5-methylphenazine-1-carboxylate + NADH + O2 = pyocyanin + NAD+ + CO2 + H2O [RN: R11346]
|
Reaction(KEGG) |
|
Substrate |
|
Product |
|
Comment |
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.
|
History |
EC 1.14.13.218 created 2016
|
Pathway |
ec01110 | Biosynthesis of secondary metabolites |
|
Orthology |
K20940 | 5-methylphenazine-1-carboxylate 1-monooxygenase |
|
Genes |
» show all
|
Reference |
|
Authors |
Mavrodi DV, Bonsall RF, Delaney SM, Soule MJ, Phillips G, Thomashow LS |
Title |
Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. |
Journal |
|
Sequence |
|
Reference |
|
Authors |
Parsons JF, Greenhagen BT, Shi K, Calabrese K, Robinson H, Ladner JE |
Title |
Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa. |
Journal |
|
Reference |
|
Authors |
Greenhagen BT, Shi K, Robinson H, Gamage S, Bera AK, Ladner JE, Parsons JF |
Title |
Crystal structure of the pyocyanin biosynthetic protein PhzS. |
Journal |
|
Sequence |
|
Other DBs |
|
LinkDB |
|