Enzymes catalytic action

Many biomolecules are Lewis adducts with central metal ions. Most often, O and N atoms of organic groups, with their lone pairs, serve as the Lewis bases. Chlorophyll is a Lewis adduct of a Mg " ion and four N atoms in an organic ring system. Vitamin B12 has a similar structure with a central Co, and so does heme, but with a central Fe ". Several other metal ions, such as Zn ", Mo ", and Cu ", are bound at the active sites of enzymes and function as Lewis acids in the enzymes catalytic action. 

The mechanisms of enzyme catalytic actions are much more complex than those used to describe traditional catalysis, since enzyme configuration itself is strongly affected by the reaction environment and by the presence of specific substrates. 

Figure 18.9 shows the pH-activity profiles of the native and complexed enzymes using BANA as the low molecular weight substrate. The complexed BT is found to have an appreciable retention of enzymatic activity. This finding indicates that one imidazolyl group (histidine), which cooperates with both COOH (aspartic acid) and OH (serine) in acylation-deacylation as an intermediate step in the enzyme catalytic action [22], is free of salt linkages with KPVS. 

Enzymatic Process. Chemically synthesized substrates can be converted to the corresponding amino acids by the catalytic action of an enzyme or the microbial cells as an enzyme source, t - Alanine production from L-aspartic acid, L-aspartic acid production from fumaric acid, L-cysteine production from DL-2-aminothiazoline-4-catboxyhc acid, D-phenylglycine (and D-/> -hydtoxyphenylglycine) production from DL-phenyUiydantoin (and DL-/)-hydroxyphenylhydantoin), and L-tryptophan production from indole and DL-serine have been in operation as commercial processes. Some of the other processes shown in Table 10 are at a technical level high enough to be useful for commercial production (24). Representative chemical reactions used ia the enzymatic process are shown ia Figure 6. 

The most frequent of the domain structures are the alpha/beta (a/P) domains, which consist of a central parallel or mixed P sheet surrounded by a helices. All the glycolytic enzymes are a/p structures as are many other enzymes as well as proteins that bind and transport metabolites. In a/p domains, binding crevices are formed by loop regions. These regions do not contribute to the structural stability of the fold but participate in binding and catalytic action. 

Figure S.l The enzyme superoxide dismutase (SOD). SOD is a P structure comprising eight antiparallel P strands (a). In addition, SOD has two metal atoms, Cu and Zn (yellow circles), that participate in the catalytic action conversion of a superoxide radical to hydrogen peroxide and oxygen. The eight p strands are arranged around the surface of a barrel, which is viewed along the barrel axis in (b) and perpendicular to this axis in (c). [(a) Adapted from J.S. Richardson. The stmcture of SOD was determined in the laboratory of J.S. and D.R. Richardson, Duke University.)...

The catalytic action is specific and may be affected by the presence of other substances both as inhibitors and as coenzymes. Most enzymes are named in terms of the reactions they catalyze (see Chapter 1). There are three major types of enzyme reactions, namely ... 

Kinetics is the branch of science concerned with the rates of chemical reactions. The study of enzyme kinetics addresses the biological roles of enzymatic catalysts and how they accomplish their remarkable feats. In enzyme kinetics, we seek to determine the maximum reaction velocity that the enzyme can attain and its binding affinities for substrates and inhibitors. Coupled with studies on the structure and chemistry of the enzyme, analysis of the enzymatic rate under different reaction conditions yields insights regarding the enzyme s mechanism of catalytic action. Such information is essential to an overall understanding of metabolism. 

In addition to the catalytic action served by the snRNAs in the formation of mRNA, several other enzymatic functions have been attributed to RNA. Ribozymes are RNA molecules with catalytic activity. These generally involve transesterification reactions, and most are concerned with RNA metabofism (spfic-ing and endoribonuclease). Recently, a ribosomal RNA component was noted to hydrolyze an aminoacyl ester and thus to play a central role in peptide bond function (peptidyl transferases see Chapter 38). These observations, made in organelles from plants, yeast, viruses, and higher eukaryotic cells, show that RNA can act as an enzyme. This has revolutionized thinking about enzyme action and the origin of life itself. 

Enzymes are highly active catalysts in many biological processes. A very important feature in the catalytic action of enzymes is their high selectivity. Any enzyme that is active toward a particular reaction involving a particular substrate is entirely inactive toward other reactions and toward other substrates. (Note that in biochemistry, a substrate is the substance undergoing reaction under the catalytic effect of the enzyme.)... 

The enzymes are protein molecules having globular structure, as a rule. The molecular masses of the different enzymes have values between ten thousands and hundred thousands. The enzyme s active site, which, as a rule, consists of a nonproteinic organic compound containing metal ions of variable valency (iron, copper, molybdenum, etc.) is linked to the protein globule by covalent or hydrogen bonds. The catalytic action of the enzymes is due to electron transfer from these ions to the substrate. The protein part of the enzyme secures a suitable disposition of the substrate relative to the active site and is responsible for the high selectivity of catalytic action. 

Syntheses of aliphatic polyesters by fermentation and chemical processes have been extensively studied from the viewpoint of biodegradable materials science. Recently, another approach to their production has been made by using an isolated lipase or esterase as catalyst via non-biosynthetic pathways under mild reaction conditions. Lipase and esterase are enzymes which catalyze hydrolysis of esters in an aqueous environment in living systems. Some of them can act as catalyst for the reverse reactions, esterifications and transesterifications, in organic media [1-5]. These catalytic actions have been expanded to... 

In addition to labeling immunoglobulins with enzymes to provide detectability through their catalytic action on a substrate, antibody molecules also can be labeled or tagged with small... 

Enzymes are metabolic products of cells that have highly specific catalytic action. They are proteins with molecular weights in the range of 15,000-1,000,000 or so. 

Many chemical changes occurring in living processes are catalyzed by enzymes which are complex protein substances produced by living cells. Enzymes are often present in colloidal state and are very specific in their catalytic action. Zymase obtained from yeast catalyses the fermentation of dextrose but is ineffective in breakdown of cane sugar. 

In this review, we first attempt briefly to discuss the structure of various aqueous aggregates. The catalytic action of these aggregates will then be presented in relation to enzyme catalysis. The underlying theme is the hydrophobic effect. 

Since the first two approaches are very well known and exploited, and excellent reviews and books on the topic are available [1], we will deal only with some of the most recent findings in chemical catalysis -excluding the Sharpless asymmetric epoxidation and dihydroxylation, to which the whole of Chapter 10 is devoted. Synthetic catalysts which mimic the catalytic action of enzymes, known as chemzymes, will be also considered. 

The "lock-and-key" description of the catalytic action of enzymes given by Emil Fischer [13] one hundred years ago, put more emphasis on the enzyme-substrate specificity than on stereospecificity, suggesting the idea of ... 

The best way to combine all these parameters is to trace back the catalytic action of enzymes to intramolecularity. It is generally accepted that when van der Waals distances (contact distances) are imposed for definite times upon reactive groups, intramolecular reactions occur then at enzyme-like rates (accelerations of 10 to 10 0 are associated to enzyme-catalysed reactions). On the other hand, according to the Page-Jencks theory [17] the fast rates of intramolecular reaction "are merely an entropic consequence of converting a bimolecular reaction into a unimolecular reaction". 

The catalytic action of an enzyme, its activity, is measured by determining the increase in the reaction rate under precisely defined conditions—i.e., the difference between the turnover (violet) of the catalyzed reaction (orange) and uncatalyzed reaction (yellow) in a specific time interval. Normally, reaction rates are expressed as the change in concentration per unit of time (mol 1 s see p. 22). Since the catalytic activity of an enzyme is independent of the volume, the unit used for enzymes is usually turnover per unit time, expressed in katal (kat, mol s ). However, the international unit U is still more commonly used (pmol turnover min 1 U = 16.7 nkat). 

Figure 2. Behavior of membrane-associated lipases. From left to right (a) catalytic action of an enzyme that first requires attachment to the substrate at the water-membrane interface (b) action of an integral membrane enzyme that remains attached to the membrane where the enzyme finds its substrate (c) action of a membrane-bound enzyme on substrates in the aqueous medium and (d) action of an enzyme in the aqueous phase on a substrate that must first desorb from the membrane before it can interact with enzyme. From Jain et al. with permission of the authors.

---