Enzymes ordered

Enzymes are classified in terms of the reactions which they catalyse and were formerly named by adding the suffix ase to the substrate or to the process of the reaction. In order to clarify the confusing nomenclature a system has been developed by the International Union of Biochemistry and the International Union of Pure and Applied Chemistry (see Enzyme Nomenclature , Elsevier, 1973). The enzymes are classified into divisions based on the type of reaction catalysed and the particular substrate. The suffix ase is retained and recommended trivial names and systematic names for classification are usually given when quoting a particular enzyme. Any one particular enzyme has a specific code number based upon the new classification. 

Most reactions in cells are carried out by enzymes [1], In many instances the rates of enzyme-catalysed reactions are enhanced by a factor of a million. A significantly large fraction of all known enzymes are proteins which are made from twenty naturally occurring amino acids. The amino acids are linked by peptide bonds to fonn polypeptide chains. The primary sequence of a protein specifies the linear order in which the amino acids are linked. To carry out the catalytic activity the linear sequence has to fold to a well defined tliree-dimensional (3D) stmcture. In cells only a relatively small fraction of proteins require assistance from chaperones (helper proteins) [2]. Even in the complicated cellular environment most proteins fold spontaneously upon synthesis. The detennination of the 3D folded stmcture from the one-dimensional primary sequence is the most popular protein folding problem. 

The contents of B, which act as a control, are treated with mercuric chloride in order to inhibit the action of the enzyme, and then 10 ml. of urease solution are added. The solution is diluted with water and ammonium chloride added (in order to balance the ammonium chloride subsequently formed in A). Meth) l-red is then added and the solution is titrated with Mj 10 HCl from a second burette B until a bright red colour is obtained. 

Interestingly, at very low concentrations of micellised Qi(DS)2, the rate of the reaction of 5.1a with 5.2 was observed to be zero-order in 5.1 a and only depending on the concentration of Cu(DS)2 and 5.2. This is akin to the turn-over and saturation kinetics exhibited by enzymes. The acceleration relative to the reaction in organic media in the absence of catalyst, also approaches enzyme-like magnitudes compared to the process in acetonitrile (Chapter 2), Cu(DS)2 micelles accelerate the Diels-Alder reaction between 5.1a and 5.2 by a factor of 1.8710 . This extremely high catalytic efficiency shows how a combination of a beneficial aqueous solvent effect, Lewis-acid catalysis and micellar catalysis can lead to tremendous accelerations. 

Peptides and proteins are formed by linking successive amino acids into chains or rings. The order (sequence) and types of amino acids (read from the sequence of codons) determine the chemical and physical properties of peptides and proteins (and enzymes). 

Enzymes not only produce characteristic and desirable flavor (79) but also cause flavor deterioration (80,81) (see Enzyme Applications, Industrial). The latter enzyme types must be inactivated in order to stabilize and preserve a food. Freezing depresses enzymatic action. A more complete elimination of enzymatic action is accompHshed by pasteurization. 

Sucrose polyesters, which are made by esterilying sucrose with long-chain fatty acids, have the physical properties of fat, but are resistant to digestive enzymes (40). Olestra, a sucrose polyester developed by Procter Gamble, was submitted for regulatory approval in May 1987. In order to faciUtate the approval process, Procter Gamble has since narrowed the scope of its food additive petition to include olestra s use only in savory and extmded snacks. 

When mapping longer DNA species such as those on the order of a whole chromosome, other techniques are used. A few enzymes are known which have recognition sequences of 8 bp in length. These longer sequences occur relatively more rarely in a chromosome than do 6-bp sequences. In... 

In the normal process ( ), step (J) occurs very rapidly and step (/) is the rate-determining step, whereas in the inhibition process (B), step (3) occurs very slowly, generally over a matter of days, so that it is rate determining. Thus it has been demonstrated with AChE that insecticides, eg, tetraethyl pyrophosphate and mevinphos, engage in first-order reactions with the enzyme the inhibited enzyme is a relatively stable phosphorylated compound containing one mole of phosphoms per mole of enzyme and as a result of the reaction, an equimolar quantity of alcohoHc or acidic product HX is hberated. 

Assays using equiUbrium (end point) methods are easy to do but the time requited to reach the end point must be considered. Substrate(s) to be measured reacts with co-enzyme or co-reactant (C) to produce products (P and Q) in an enzyme-catalyzed reaction. The greater the consumption of S, the more accurate the results. The consumption of S depends on the initial concentration of C relative to S and the equiUbrium constant of the reaction. A change in absorbance is usually monitored. Changes in pH and temperature may alter the equiUbrium constant but no serious errors are introduced unless the equihbrium constant is small. In order to complete an assay in a reasonable time, for example several minutes, the amount and therefore the cost of the enzyme and co-factor maybe relatively high. Sophisticated equipment is not requited, however. 

In order for the cyclooxygenase to function, a source of hydroperoxide (R—O—O—H) appears to be required. The hydroperoxide oxidizes a heme prosthetic group at the peroxidase active site of PGH synthase. This in turn leads to the oxidation of a tyrosine residue producing a tyrosine radical which is apparendy involved in the abstraction of the 13-pro-(5)-hydrogen of AA (25). The cyclooxygenase is inactivated during catalysis by the nonproductive breakdown of an active enzyme intermediate. This suicide inactivation occurs, on average, every 1400 catalytic turnovers. 

The primary disadvantage of the conjugate addition approach is the necessity of performing two chiral operations (resolution or asymmetric synthesis) ia order to obtain exclusively the stereochemicaHy desired end product. However, the advent of enzymatic resolutions and stereoselective reduciag agents has resulted ia new methods to efficiently produce chiral enones and CO-chain synthons, respectively (see Enzymes, industrial Enzymes in ORGANIC synthesis). Eor example, treatment of the racemic hydroxy enone (70) with commercially available porciae pancreatic Hpase (PPL) ia vinyl acetate gave a separable mixture of (5)-hydroxyenone (71) and (R)-acetate (72) with enantiomeric excess (ee) of 90% or better (204). 

The principal route of macroHde excretion is by way of the Hver. Effects of macrohdes on hepatic metaboHc enzymes, particularly cytochrome P-450, have been studied in order to identify and reduce potential interference with metaboHsm of other dmgs (21—23,444—447). Several macrohdes are initially... 

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