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Literature summary for 4.2.99.21 extracted from

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
isochorismate Pseudomonas aeruginosa
-
salicylate + pyruvate
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
gene pchB
-

Reaction

Reaction Comment Organism Reaction ID
isochorismate = salicylate + pyruvate reaction mechanism with catalytic residue Lys42, modeling, overview Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isochorismate
-
Pseudomonas aeruginosa salicylate + pyruvate
-
?
isochorismate elimination of pyruvate Pseudomonas aeruginosa salicylate + pyruvate
-
?
additional information PchB can also perform a nonphysiological role as a chorismate mutase, EC 4.1.3.40, albeit with considerably lower catalytic efficiency Pseudomonas aeruginosa ?
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?

Synonyms

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

General Information

General Information Comment Organism
evolution PchB is a structural homologue of the AroQ chorismate mutases Pseudomonas aeruginosa
metabolism the enzyme is involved in siderophore pyochelin via salicylate biosynthesis Pseudomonas aeruginosa
additional information structure-function relationship, biocatalysis of pericyclic reactions, overview. For PchB, the pericyclic reaction is a concerted but asynchronous [1,5]-sigmatropic shift with a quantitative transfer of hydrogen from C2 to C9. Major structural difference between the apo form and the pyruvate-bound or the pyruvate-and salicylate-bound forms of PchB: the active site loop between helix 1 and helix 2 is disordered in the apo structure but fully ordered in the ligand-bound structures. The difference between the open and closed structures is due to a conserved active site lysine 42, which hydrogen bonds to a bound pyruvate molecule. Quantum mechanical/molecular mechanical molecular dynamics simulations, overview Pseudomonas aeruginosa