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Enoyl-CoA-(∆) isomerase (EC 5.3.3.8, also known as dodecenoyl-CoA-(∆) isomerase, 3,2-trans-enoyl-CoA isomerase, ∆3(cis),∆2(trans)-enoyl-CoA isomerase, or acetylene-allene isomerase, [1] is an enzyme that catalyzes the conversion of cis- or trans-double bonds of coenzyme A (CoA) bound fatty acids at gamma-carbon (position 3) to trans double bonds at beta-carbon (position 2) as below:
The change of Gibbs free energy (ΔG) in an exergonic reaction (that takes place at constant pressure and temperature) is negative because energy is lost (2). In chemical thermodynamics, an exergonic reaction is a chemical reaction where the change in the free energy is negative (there is a net release of free energy). [1]
The enzyme's active site contains two Asp residues. After the substrate binds to the enzyme, the first Asp deprotonates the third carbon from one side of the molecule. This leaves a planar sp 2-hybridized intermediate. The second Asp is located on the opposite side of the active side and it protonates the molecule, effectively adding a proton ...
The and pH of a solution are related by the Nernst equation as commonly represented by a Pourbaix diagram (– pH plot).For a half cell equation, conventionally written as a reduction reaction (i.e., electrons accepted by an oxidant on the left side):
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
Cyanobacterial DesA, [19] an enzyme that can introduce a second cis double bond at the delta-12 position of fatty acid bound to membrane glycerolipids. This enzyme is involved in chilling tolerance; the phase transition temperature of lipids of cellular membranes being dependent on the degree of unsaturation of fatty acids of the membrane lipids.
Using the Eyring equation, there is a straightforward relationship between ΔG ‡, first-order rate constants, and reaction half-life at a given temperature. At 298 K, a reaction with ΔG ‡ = 23 kcal/mol has a rate constant of k ≈ 8.4 × 10 −5 s −1 and a half life of t 1/2 ≈ 2.3 hours, figures that are often rounded to k ~ 10 −4 s ...
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]