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Literature summary for 5.4.99.5 extracted from

  • Lamb, A.L.
    Pericyclic reactions catalyzed by chorismate-utilizing enzymes (2011), Biochemistry, 50, 7476-7483.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
additional information chorismate mutase activity is only detected when the Mg2+ is not present in the wild-type active site Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Chorismate Pseudomonas aeruginosa
-
Prephenate
-
?
additional information Pseudomonas aeruginosa isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform the chorismate mutase reaction ?
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Chorismate = prephenate via near attack conformation and transition state intermediates, reaction mechanism, overview Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
Pseudomonas aeruginosa Prephenate
-
?
additional information isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform the chorismate mutase reaction Pseudomonas aeruginosa ?
-
?

Subunits

Subunits Comment Organism
More enzyme structure comparisons of isochorismate-pyruvate lyase, PchB, with chorismate mutases, overview Pseudomonas aeruginosa

General Information

General Information Comment Organism
additional information structure-function relationships of chorismate-utilizing enzymes, structure comparisons, overview Pseudomonas aeruginosa
physiological function isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency Pseudomonas aeruginosa