Enzyme system

Enzyme Systems. Carotenoid biosynthesis by crude cell-free preparations from Halobacterium cutirubrum 0-carotene), Phycomyces blakesleeanus mutants (/8-carotene), and a Neurospora crassa mutant (phytoene) has been demonstrated. Detailed studies of carotenogenic enzymes from tomato fruit 

The compounds upon which enzymes act are called substrates. Because the action of a given enzyme is usually specific to one or two substrates, some very special structural fit or lock and key intimate relationship is usually considered to exist between the two components (this idea was first proposed by E. Fischer in 1890). When optically active compounds are involved, enzyme action is invariably specific to the production of one isomer only. 

Enzymes (holoenzymes) consist of two main parts - a pure protein part (apo- enzyme), and a non-protein part (cofactor) Holoenzyme = Apoenzyme -i- Cofactor. 

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Organic chemists often use enantiomencally homogeneous starting materials for the synthe SIS of complex molecules (see Chiral Drugs p 296) A novel preparation of the S enantiomer of compound B has been descnbed using a bacterial cyclohexanone monooxygenase enzyme system... 

Cortisol-Cortisone Conversion. Under normal conditions, this equilibrium slightly favors the oxidized compound. Similarly, the conversion of corticosterone to 11-deoxycorticosterone is also mediated by the liP-hydroxysteroid dehydrogenase enzyme system and requites NAD(P) /NAD(P)H. This conversion is especially important both in the protection of the human fetus from excessive glucocorticoid exposure, and in the protection of distal nephron mineral ocorticoid receptors from glucocorticoid exposure (14). The impairment of this conversion is thought to result in hypertension associated with renal insufficiency (15). 

The extension of the useful storage life of plant and animal products beyond a few days at room temperature presents a series of complex biochemical, physical, microbial, and economic challenges. Respiratory enzyme systems and other enzymes ia these foods continue to function. Their reaction products can cause off-davors, darkening, and softening. Microbes contaminating the surface of plants or animals can grow ia cell exudates produced by bmises, peeling, or size reduction. Fresh plant and animal tissue can be contaminated by odors, dust, iasects, rodents, and microbes. 

Phospholipids. Phospholipids, components of every cell membrane, are active determinants of membrane permeabiUty. They are sources of energy, components of certain enzyme systems, and involved in Hpid transport in plasma. Because of their polar nature, phosphoUpids can act as emulsifying agents (42). The stmcture of most phosphoUpids resembles that of triglycerides except that one fatty acid radical has been replaced by a radical derived from phosphoric acid and a nitrogen base, eg, choline or serine. 

Metabolic Functions. Zinc is essential for the function of many enzymes, either in the active site, ie, as a nondialyzable component, of numerous metahoenzymes or as a dialyzable activator in various other enzyme systems (91,92). WeU-characterized zinc metahoenzymes are the carboxypeptidases A and B, thermolysin, neutral protease, leucine amino peptidase, carbonic anhydrase, alkaline phosphatase, aldolase (yeast), alcohol... 

Fig. 7. The glutathione peroxidase (a selenium enzyme) system where GSH = A -(A -L-7-giutamyi -L-cysteinyi )giycine and G—S—S—G, the disulfide.

Because of its position in the Periodic Table, molybdenum has sometimes been linked to chromium (see Chromiumand chromium alloys) or to other heavy metals. However, unlike those elements, molybdenum and its compounds have relatively low toxicity, as shown in Table 3. On the other hand, molybdenum has been identified as a micronutrient essential to plant life (11,12) (see Fertilizers), and plays a principal biochemical role in animal health as a constituent of several important enzyme systems (see Mineral nutrients). 

Dinitrogen has a dissociation energy of 941 kj/mol (225 kcal/mol) and an ionisation potential of 15.6 eV. Both values indicate that it is difficult to either cleave or oxidize N2. For reduction, electrons must be added to the lowest unoccupied molecular orbital of N2 at —7 eV. This occurs only in the presence of highly electropositive metals such as lithium. However, lithium also reacts with water. Thus, such highly energetic interactions ate unlikely to occur in the aqueous environment of the natural enzymic system. Even so, highly reducing systems have achieved some success in N2 reduction even in aqueous solvents. 

Biomedical Applications. TRIS AMINO is used for a number of purposes in its pure form, it is an acidimetric standard the USP grade can be utilized intraveneously for therapeutic control of blood acidosis TRIS AMINO also is useful in genetic engineering as a buffering agent for enzyme systems, industrial protein purification, and electrophoresis. AMP has found use as a reagent in enzyme-linked immunoassays. The primary appHcation is for alkaline phosphatase assays. 

The enzyme system responsible for the biosynthesis of PGs is widely distributed in mammalian tissues and has been extensively studied (2). It is referred to as prostaglandin H synthase (PGHS) and exhibits both cyclooxygenase and peroxidase activity. In addition to the classical PGs two other prostanoid products, thromboxane [57576-52-0] (TxA ) (3) and prostacyclin [35121 -78-9] (PGI2) (4) are also derived from the action of the enzyme system on arachidonic acid (Fig. 1). 

An important function of certain carotenoids is their provitamin A activity. Vitamin A may be considered as having the stmcture of half of the P-carotene molecule with a molecule of water added at the end position. In general, all carotenoids containing a single unsubstituted P carotene half have provitamin A activity, but only about half the activity of P carotene. Provitamin A compounds are converted to Vitamin A by an oxidative enzyme system present in the intestinal mucosa of animals and humans. This conversion apparendy does not occur in plants (see Vitamins, VITAMIN a). 

Enzyme Inhibition. Some materials produce toxic effects by inhibition of biologically vital enzyme systems, leading to an impairment of normal biochemical pathways. The toxic organophosphates, for example, inhibit the cholinesterase group of enzymes. An important factor in thek acute toxicity is the inhibition of acetylocholinesterase at neuromuscular junctions, resulting in an accumulation of the neurotransmitter material acetylcholine and causing muscle paralysis (29) (see Neuroregulators). 

I. H. Segel, En me Kinetics Behavior andMnalysis of KapidEquilibrium and Steady-State Enzyme Systems, Wiley-Interscience, New York, 1975. 

Figure 3 Some interactions between gastrointestinal bacteria and the xenobiotic metabolizing enzyme system of the host. Solid lines, host XME system reactions dotted lines, classes of reactions mediated by gastrointestinal bacteria. Specific examples of reaction classes 1-5 are cited in the text. (Modified from Rowland and Tanaka " )...

The best computational approach to the study of chemical reactions uses quantum mechanics however, in practice the size of the enzyme system precludes the use of tradi-... 

In a monograph on ephedrine Gaddum has reviewed the differences in the action of adrenaline and ephedrine and has suggested that the latter has the same relation to adrenaline as physostigmine has to acetylcholine, that is, ephedrine inhibits the action of an enzyme system, which normally destroys adrenaline, or the substance closely resembling it, produced by adrenergic nerves. 

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