622-54-8Relevant articles and documents
Characterization of a newly identified mycobacterial tautomerase with promiscuous dehalogenase and hydratase activities reveals a functional link to a recently diverged cis -3-chloroacrylic acid dehalogenase
Baas, Bert-Jan,Zandvoort, Ellen,Wasiel, Anna A.,Quax, Wim J.,Poelarends, Gerrit J.
, p. 2889 - 2899 (2011)
The enzyme cis-3-chloroacrylic acid dehalogenase (cis-CaaD) is found in a bacterial pathway that degrades a synthetic nematocide, cis-1,3-dichloropropene, introduced in the 20th century. The previously determined crystal structure of cis-CaaD and its prom
A thermodynamic investigation of some reactions involving prephenic acid
Kishore, Nand,Holden, Marcia J.,Tewari, Yadu B.,Goldberg, Robert N.
, p. 211 - 227 (2007/10/03)
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.
