97645-23-3

Upstream product

• 620-76-8 phenylpyruvate^- 
• 622-54-8 4-hydroxyphenylpyruvate^- 
• 617-12-9 (+/-)-chorismate 
• 159700-65-9 (-)-chorismate 

Downstream Products

• 620-76-8 phenylpyruvate^- 

Relevant academic research and scientific papers

Is chorismate mutase a prototypic entropy trap? - Activation parameters for the Bacillus subtilis enzyme

Chorismate mutase is thought to accelerate the chorismate-to-prephenate rearrangement in part by significantly lowering the entropy barrier for the reaction. We have determined the activation parameters for the well-characterized Bacillus subtilis chorism

Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor

Citrulline was incorporated via chemical semisynthesis at position 90 in the active site of the AroH chorismate mutase from Bacillus subtilis. The wild-type arginine at this position makes hydrogen-bonding interactions with the ether oxygen of chorismate.

PH dependence of catalysis by pseudomonas aeruginosa isochorismate - Pyruvate lyase: Implications for transition state stabilization and the role of lysine 42

An isochorismate - pyruvate lyase with adventitious chorismate mutase activity from Pseudomonas aerugionsa (PchB) achieves catalysis of both pericyclic reactions in part by the stabilization of reactive conformations and in part by electrostatic transitio

A thermodynamic investigation of some reactions involving prephenic acid

Calorimetric enthalpies of reaction have been measured for the following enzyme-catalysed reactions at the temperature 298.15 K: prephenate(aq) = phenylpyruvate(aq) + carbon dioxide(aq), prephenate(aq) + NADox(aq) + H2O(1) = 4-hydroxyphenylpyruvate(aq) + NADred(aq) + carbon dioxide (aq). Here, NADox and NADred are, respectively, the oxidized and reduced forms of β-nicotinamide adenine dinucleotide. The enzymes that catalyse these respective reactions, prephenate dehydratase and prephenate dehydrogenase, were prepared by expression of the appropriate plasmids using the techniques of molecular biology. The calorimetric measurements together with the equilibrium modeling calculations lead to a standard molar enthalpy change ΔrHom = -(126 ± 5) kJ·mol-1 for the reference reaction: prephenate2-(aq) = phenylpyruvate-(aq) + HCO-3(aq). Similarly, ΔrHom = -(74 ± 3) kJ·mol-1 for the reference reaction: prephenate2-(aq) + NAD-ox(aq) + H2O(1) = 4-hydroxyphenylpyruvate- (aq) + NAD2red(aq) + HCO-3(aq) + H+aq). Both results pertain to T = 298.15 K and ionic strength I = 0. Benson estimates for the entropies lead to approximate values of the equilibrium constants K ≈ 1·1026 and K ≈ 1·1012, respectively, for the above two reference reactions.

The Conformational Equilibrium of Chorismate in Solution: Implications for the Mechanism of the Non-Enzymic and the Enzyme-Catalyzed Rearrangement of Chorismate to Prephenate

The temperature variation of the 1H NMR coupling constants of chorismic acid and of the bis(tetra-n-butylammonium) salts of chorismate and of 4-O-methylchorismate in water and in methanol has been studied.The results show that 10-40percent of each of thes