Enzyme catalytic properties structure

Biocatalysis refers to catalysis by enzymes. The enzyme may be introduced into the reaction in a purified isolated form or as a whole-cell micro-organism. Enzymes are highly complex proteins, typically made up of 100 to 400 amino acid units. The catalytic properties of an enzyme depend on the actual sequence of amino acids, which also determines its three-dimensional structure. In this respect the location of cysteine groups is particularly important since these form stable disulfide linkages, which hold the structure in place. This three-dimensional structure, whilst not directly involved in the catalysis, plays an important role by holding the active site or sites on the enzyme in the correct orientation to act as a catalyst. Some important aspects of enzyme catalysis, relevant to green chemistry, are summarized in Table 4.3. 

Recently, the distribution of 2,3-dihydroxybenzoate decarboxylase has been found in a variety of fungal strains (unpubhshed data), and the carboxylation activity for catechol is confirmed by the reaction using resting cells (or cell-free extract) in the presence of 3M KHCO3. The detailed comparative studies of enzyme structures and catalytic properties between 2,3-dihydroxybenzoate decarboxylase and 3,4-dihyroxybenzoate decarboxylase might explain how the decarboxylases catalyze the regioselective carboxylation of catechol. 

In general, biomolecules such as proteins and enzymes display sophisticated recognition abilities but their commercial viability is often hampered by their fragile structure and lack of long term stability under processing conditions [69]. These problems can be partially overcome by immobilization of the biomolecules on various supports, which provide enhanced stability, repetitive and continuous use, potential modulation of catalytic properties, and prevention of microbial contaminations. Sol-gel and synthetic polymer-based routes for biomolecule encapsulation have been studied extensively and are now well established [70-72]. Current research is also concerned with improving the stability of the immobilized biomolecules, notably enzymes, to increase the scope for exploitation in various... 

The separation of a reactant system (solute) from its environment with the consequent concept of solvent or surrounding medium effect on the electronic properties of a given subsystem of interest as general as the quantum separability theorem can be. With its intrinsic limitations, the approach applies to the description of specific reacting subsystems in their particular active sites as they can be found in condensed phase and in media including the rather specific environments provided by enzymes, catalytic antibodies, zeolites, clusters or the less structured ones found in non-aqueous and mixed solvents [1,3,6,8,11,12,14-30],... 

The lowered temperature approach has been linked to flow, temperature jump, photolysis, and nmr methods. Cryoenzymology allows the characterization of enzyme intermediates which have life-times of only milliseconds at normal temperatures, but are stable for hours at low temperatures. Mixed aqueous/organic solvents or even concentrated salt solutions are employed and must always be tested for any adverse effects on the catalytic or structural properties of the enzyme. 

Since the discovery that RNA molecules can possess catalytic activities, ribozymes have become a fascinating field both for academic researchers and the pharmaceutical industry. In this review, we emphasize the latest progress made in structure determination of ribozymes as well as the generation of DNA and RNA enzymes with novel catalytic properties by combinatorial approaches. 

Numerous examples of modiflcations to the fundamental cyclodextrin structure have appeared in the literature.The aim of much of this work has been to improve the catalytic properties of the cyclodextrins, and thus to develop so-called artificial enzymes. Cyclodextrins themselves have long been known to be capable of catalyzing such reactions as ester hydrolysis by interaction of the guest with the secondary hydroxyl groups around the rim of the cyclodextrin cavity. The replacement, by synthetic methods, of the hydroxyl groups with other functional groups has been shown, however, to improve remarkably the number of reactions capable of catalysis by the cyclodextrins. For example, Breslow and CO workersreported the attachment of the pyridoxamine-pyridoxal coenzyme group to beta cyclodextrin, and thus found a two hundred-fold acceleration of the conversion of indolepyruvic acid into tryptophan. 

In the absence of structural data for many interesting glycosidases, comparison of their sequences has revealed important structural relationships and similarities of catalytic properties. The database CAZy (Carbohydrate-Active EnZymes) is a sequence-based collection of currently around 100 GH families (currently GH 1 to GH 117, with around 15 families deleted), which are further grouped in 14 clans. It provides family-typical structural and mechanistic details and has become an invaluable tool in GH research.98... 

Schultz, C.P. Ylisastigui-Pons, L. Serina, L. Sakamoto, H. Mantsch, H.H. Neuhard, J. Barzu, 0. Gilles, A.M. Structural and catalytic properties of CMP kinase from Bacillus subtilis a comparative analysis with the homologous enzyme from Escherichia coli. Arch. Biochem. Biophys., 340, 144-153 (1997)... 

Both enzymes and antibodies are proteins. Antibodies consist of subunits with multiple domains, just as do some enzymes. Both enzymes and antibodies have binding sites for small molecules between domains or subunits. In view of such similarities it isn t surprising that some antibodies have catalytic properties. The possibility was suggested in 1969 by Jencks 3 He also proposed that injection of a mouse with a hapten, that resembled a transition state for an enzyme, might induce formation of antibodies complementary to the transition-state structure. These might be catalytic. By the early 1980s such antibodies were discovered.1 d Some of the first catalytic antibodies (also dubbed abzymes) had esterase activity. The haptens used to induce antibody formation were phosphonates such as the following.e f... 

The structure of cytochrome P450cam (CYP101), a soluble bacterial enzyme, has been solved. This enzyme was studied for its catalytic properties in the oxidation of methyl phenyl sulfide and methyl p-tolyl sulfide [117], Molecular dynamics calculations were used to predict the absolute configuration and enantioselectivity of the reaction. 

The catalytic properties of Mn enzyme structural models are not limited to the natural substrates of the enzymes they mimic. One could classify this catalysis based upon the substrates as biological mimetic catalysis or biomimetic catalysis [175] and biologically inspired catalysis or bioinspired catalysis [176], Unlike biomimetic catalysis, its bioinspired counterpart capitalizes on nature s findings to change nonnatural substrates chemically and, perhaps, unravel novel chemistry. 

Schiavo G, Papini E, Genna G, Montecucco C (1990) An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin. Infect Immun 58 4136 11 Scott AB, Magoon EH, McNeer KW, Stager DR (1989) Botulinum treatment of strabismus in children. Trans Am Ophthalmol Soc 87 174-180 discussion 180 1 Scott D (1997) Phospholipase A2 structure and catalytic properties. In Kini R (ed) Venom phospholipase A2 enzymes structure, function and mechanism. John Wiley Sons, Chichester, p 97-128. 

Pepsin (EC 3.4.23.1) is a typical aspartic proteinase produced in the gastric mucosa of vertebrates as a zymogen form [10], This enzyme has been extensively characterized, and its three-dimensional structure has been determined at high resolution. Porcine pepsin, in particular, has been studied as model to analyze the structure-function relationship of the aspartic proteinases. Although the aspartic proteinases including mammalian and fungal enzymes are quite similar in their three-dimentional structures, there are drastic differences in the catalytic properties, especially in substrate specificities. 

---