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Literature summary for 4.2.99.21 extracted from

  • Luo, Q.; Meneely, K.M.; Lamb, A.L.
    Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB (2011), J. Am. Chem. Soc., 133, 7229-7233.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics and thermodynamics, overview Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
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-
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Pseudomonas aeruginosa
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gene pchB
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Reaction

Reaction Comment Organism Reaction ID
isochorismate = salicylate + pyruvate a reactive substrate conformation is formed upon loop closure of the active site and ordering of the loop contributes to the entropic penalty for converting the enzyme substrate complex to the transition state. The thermodynamic parameters of the physiological lyase activity of PchB show that the reaction is clearly enthalpically driven, and has a very large entropic penalty of 24.3 cal/(mol K), which is more than 1.5-fold greater than that of the uncatalyzed reaction of 15.77 cal/(mol K) Pseudomonas aeruginosa
isochorismate = salicylate + pyruvate kinetic mechanism and transition state of the elimination reaction, overview Pseudomonas aeruginosa

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isochorismate isochorismate undergoes elimination to form salicylate and pyruvate and rearrangement to form isoprephenate in the absence of enzyme Pseudomonas aeruginosa salicylate + pyruvate
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Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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assay at Pseudomonas aeruginosa