Literature summary for 4.2.99.21 extracted from

Marti, S.; Andres, J.; Moliner, V.; Silla, E.; Tunon, I.; Bertran, J.
Mechanism and plasticity of isochorismate pyruvate lyase: a computational study (2009), J. Am. Chem. Soc., 131, 16156-16161.

Search for more literature for 4.2.99.21

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations and averaged intermolecular substrate-protein distances, active-site volumes for reactants and transition state	Pseudomonas aeruginosa

Protein Variants

Protein Variants	Comment	Organism
A37I	mutation increases the rate constant for the chorismate mutase activity by a factor of 1000, and also increases the isochorismate pyruvate lyase catalytic efficiency, by a factor of 6	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	enzyme additionally catalyzes the rearrangement of chorismate into prephenate	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme additionally catalyzes the rearrangement of chorismate into prephenate and shows chorismate mutase activity. Both transformation of isochorismate into pyruvate and salicylate and the rearrangement of chorismate into prephenate proceed via a pericyclic reaction mechanism	Pseudomonas aeruginosa	?	-	?

Synonyms

Synonyms	Comment	Organism
IPL	-	Pseudomonas aeruginosa
isochorismate pyruvate lyase	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)