Enzymatic reactions involving the heteroatoms from organic substrates

Enzymatic transamination reactions involving arginine and ornithine.

Recent research has resulted in considerable modification of the earlier concept that enzymatic transamination was limited to reactions between alanine, aspartate, glutamate, and their or-keto analogues. Reactions leading to the reversible amination of the cY-keto analogues of many of the natural amino acids have been described (l-5), and there is also evidence that aldehyde groups may particip...

Kinetics of diffusion-controlled enzymatic reactions with charged substrates

The Debye-Hückel limiting law (DHL) has often been used to estimate rate constants of diffusion-controlled reactions under different ionic strengths. Two main approximations are adopted in DHL: one is that the solution of the linearized Poisson-Boltzmann equation for a spherical cavity is used to estimate the excess electrostatic free energy of a solution; the other is that details of electrost...

Ultranicro Analysis of Enzymes and Substrates by Enzymatic Amplification Reactions

The principle and kinetics of enzymatic cycling are described. The enzymatic cycling reaction is catalyzed by a couple of enzymes and amplifies stoichiometrically a pair of substrates participating in the reaction. Many biological substances can be converted quantitatively to substrates that can be amplified and measured by cycling reactions. Three cyclings in routine use (NAD, NADP and CoA cyc...

Adsorption and Desorption Reactions Involving Phosphate and Organic Acids

Enzymatic Reactions

It has been argued that a substrate-induced conformational change involving the orientation of catalytic groups cannot affect the specificity for two substrates in an enzymatic system where the chemical step is rate limiting, because such an induced fit would alter the catalytic efficiency for both to an equal extent. To the contrary, the generalized induced-fit treatment described here shows t...