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Literature summary for 2.1.1.327 extracted from

  • 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 (2007), Biochemistry, 46, 1821-1828.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
-
Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HWH2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Pseudomonas aeruginosa ?
-
?
S-adenosyl-L-methionine + phenazine-1-carboxylate
-
Pseudomonas aeruginosa S-adenosyl-L-homocysteine + 5-methyl-phenazine-1-carboxylate
-
?

Synonyms

Synonyms Comment Organism
phzM
-
Pseudomonas aeruginosa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3
-
phenazine-1-carboxylate presence of hydroxylase PhzS, pH 7.8, 22°C Pseudomonas aeruginosa