Enzymatic reaction involving

The simplest type of enzymatic reaction involves only a single reactant or substrate. The substrate forms an unstable complex with the enzyme that decomposes to give the product species or, alternatively, to generate the substrate. 

The response characteristics of enzyme electrodes depend on many variables, and an understanding of the theoretical basis of their function would help to improve their performance. Enzymatic reactions involving a single substrate can be formulated in a general way as... 

It is interesting that some of the enzymatic reactions involve the rearrangement of diols to aldehydes (see below). 

Carloni et al.91 applied the DFT(PZ) calculations to investigate the electronic structure of various models of oxydized and reduced Cu, Zn superoxide dismutase. The first stage of the enzymatic reaction involves the electron transfer from Cu" ion to superoxide. The theoretical investigations provided a detailed description of the electronic structure of the molecules involved in the electron transfer process. The effect of charged groups, present in the active center, on the electron transfer process were analyzed and the Argl41 residue was shown to play a crucial role. 

One of the best known enzymatic reactions involving glucose is the following oxidation reaction catalysed by glucose oxidase (GOD) ... 

As the enzymatic reaction involves H2, H+, and electrons and the active sites are deeply buried in the protein, the X-ray crystallographers have... 

Both in nature and in test tubes many complicated reactions take place with apparent ease. Highly specific enzymatic reactions involving complementarity of substrate and receptor both with respect to their spatial structure and electrostatic fields lie outside the scope of this book. Here we would like only to mention a few... 

Selectivity is an intrinsic properly of enzymatic catalysis. [3] Following the nomenclature proposed by Cleland [24, 25], the pseudo second-order rate constant for the reaction of a substrate with an enzyme, kml/KM, is known as the specificity constant, ksp. [26] To express the relative rates of competing enzymatic reactions, involving any type of substrates, the ratio of the specificity constants appears to be the parameter of choice [3]. Since the authoritative proposition by Sih and coworkers [27], the ratio of specificity constants for the catalytic conversion of enantiomeric substrates, R and S, is commonly known as the enantiomeric ratio or E -value (Equation 1) ... 

Enzymatic reactions involving addition to a C = C bond adjacent to a carbonyl group (or in which elimination occurs a,P to a carbonyl) are numerous. Except for some enzymes acting by free radical mechanisms, the nucleophilic group always adds at the P position suggesting that the mechanism portrayed by Eq. 13-7 is probable. It is noteworthy that frequently in a metabolic sequence a carbonyl group is deliberately introduced to... 

Structures of Thiamin-Dependent Enzymes 4. The Variety of Enzymatic Reactions Involving Thiamin 5. Oxidative Decarboxylation and 2-Acetylthiamin Diphosphate. 6. Thiamin Coenzymes in Nerve Action 753. .. Table 14-4 Some Pyruvoyl Enzymes... 

Most of the genetic information of bacteria is contained in a single structure of fixed DNA content, a giant circular DNA molecule that replicates semi-conservatively. The enzymatic reactions involved in the biologically fundamental processes of DNA biosynthesis and genetic recombination are being elucidated in studies with bacterial systems. 

Biochemically, PLP is the coenzyme form of vitamin B6. As such it participates in many enzymatic reactions involved in amino acid biosynthesis and catabolism. Specific examples include ... 

The Henri-Michaelis-Menten Treatment Assumes That the Enzyme-Substrate Complex Is in Equilibrium with Free Enzyme and Substrate Steady-State Kinetic Analysis Assumes That the Concentration of the Enzyme-Substrate Complex Remains Nearly Constant Kinetics of Enzymatic Reactions Involving Two Substrates... 

The suggestion that Co—C bond dissociation energies lie in the range 84-125 kJ mol-1 is appropriate for the known rates of enzymatic reactions involving such dissociations. It is clear, too, from these model studies, that electronic and steric effects produced in the coenzyme by changes in the interactions in the coenzyme-enzyme complex could be significant in enhancing Co—C bond homolysis. 

Bronsted acid/base catalysis is the most common enzymatic mechanism, since nearly all enzymatic reactions involve a proton transfer. This means that nearly all enzymes have acidic and/or basic groups in their active site. In add catalysis, the substrate is protonated by one of the amino add residues at the active site (typically aspartic acid, glutamic acid, histidine, cysteine, lysine, or tyrosine). This residue itself must therefore be protonated at the readion pH (typically between pH 5 and 9), with a pKa just above this value. Conversely, in base catalysis, the pJCa of the deprotonating residue must be just below the physiological pH. Some enzymes can even carry out bifunctional catalysis, by protonating and deprotonating two different sites on the same substrate molecule simultaneously. 

Bioreactions are exothermic. The net heat released during growth represents the sum of the many enzymatic reactions involved. Reasonably, this measure depends on both the biomass concentration and the metabolic state of the cells. Its general use in biotechnology has been reviewed by von Stockar and Marison [415]. A theoretical thermodynamic derivation for aerobic growth gives a prediction for the heat yield coefficient YQ/0 of 460 kj (mol 02) 1 and it was ex-... 

Siegbahn PEM, Borowski T. Modeling enzymatic reactions involving transition metals. Acc Chem Res. 2006 39 729-38. 

Many enzymatic reactions involve transfer protons, hydrides or hydrogen atoms (Alhambra et al 2000 Allison, 1998 Backgren et al 2000 Blum et al., 2001 Cha et al.,... 

For many enzymatic reactions involving hydrogen transfer, experimental data on KIF and its temperature dependence are roughly consistent with a classical (nontunneling) theory (Eq. 2.32) (Bruno and Bialik, 1992 and references therein). Nevertheless, anomalies... 

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