The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. The enzyme is active in vitro only in the presence of EC 1.14.13.218, 5-methylphenazine-1-carboxylate 1-monooxygenase.
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The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. The enzyme is active in vitro only in the presence of EC 1.14.13.218, 5-methylphenazine-1-carboxylate 1-monooxygenase.
purified PhzM alone has little or no ability to methylate phenzine-1-carboxylic acid. When the putative hydroxylase PhzS, EC 1.14.13.218, is included, pyocyanin is readily produced
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.8 A crystal structure of PhzM. PhzM is a dimer in solution. The polypeptide folds into three domains. The C-terminal domain exhibits the alpha/beta-hydrolase fold typical of small molecule methyltransferases. Two smaller N-terminal domains form much of the dimer interface. PhzM is most similar to the plant O-methyltransferases that are characterized by an unusual intertwined dimer interface. The structure of PhzM contains no ligands and the active site is open and solvent exposed
to 2.3 A resolution. Space group P1, with unit-cell parameters a = 46.1, b = 61.8, c = 69.6 A, alpha = 96.3, beta = 106.6, gamma = 106.9, one dimer in the asymmetric unit
detection of mutations in these genes by sequencing. Pseudomonas isolates have 9 mutations in 8 Iraqi isolates in the phzM gene. It is proposed that the mutations have no role in the pathogenesis
Gohain, N.; Thomashow, L.S.; Mavrodi, D.V.; Blankenfeldt, W.
The purification, crystallization and preliminary structural characterization of PhzM, a phenazine-modifying methyltransferase from Pseudomonas aeruginosa
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History
Enzyme Nomenclature
2.1.1.327 phenazine-1-carboxylate N-methyltransferase
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