Future potential enzyme mechanism

Another interesting example of the fission of non-activated C—C bond with the liberation of carbon dioxide is the decarboxylation of oxalate. The enzymes related to degradation of oxalate have a number of potential apphcations especially in relation to diagnosis and human health. Also, the reaction mechanism of this enzyme is interesting. It requires metal ions to activate the substrate and this might give some hints to develop decarboxylation reactions of other types of compounds. In this way, the future extension is expected in this area. 

Lactamases (EC 3.5.2.6) inactivate /3-lactam antibiotics by hydrolyzing the amide bond (Fig. 5.1, Pathway b). These enzymes are the most important ones in the bacterial defense against /3-lactam antibiotics [15]. On the basis of catalytic mechanism, /3-lactamases can be subdivided into two major groups, namely Zn2+-containing metalloproteins (class B), and active-serine enzymes, which are subdivided into classes A, C, and D based on their amino acid sequences (see Chapt. 2). The metallo-enzymes are produced by only a relatively small number of pathogenic strains, but represent a potential threat for the future. Indeed, they are able to hydrolyze efficiently carbape-nems, which generally escape the activity of the more common serine-/3-lac-tamases [16] [17]. At present, however, most of the resistance of bacteria to /3-lactam antibiotics is due to the activity of serine-/3-lactamases. These enzymes hydrolyze the /3-lactam moiety via an acyl-enzyme intermediate similar to that formed by transpeptidases. The difference in the catalytic pathways of the two enzymes is merely quantitative (Fig. 5.1, Pathways a and b). 

To understand the potential of pressure application to enzyme processes and to help elucidate the reaction mechanism as well as a rational design of alcoholysis reactors for future scale-up, we investigated the influence of temperature, pressure, exposure times, and decompression rates on the activity of a commercial immobilized lipase (Novozym 435) activity in high-pressure C02 medium. 

The mysterious behaviour of bio-macromolecules is one of the outstanding problems of molecular biology. The folding of proteins and the replication of DNA transcend all classical mechanisms. At this stage, non-local interaction within such holistic molecules appears as the only reasonable explanation of these phenomena. It is important to note that, whereas proteins are made up of many partially holistic amino-acid units, DNA consists of essentially two complementary strands. Nonlocal interaction in DNA is therefore seen as more prominent, than for proteins. Non-local effects in proteins are sufficient to ensure concerted response to the polarity and pH of suspension media, and hence to direct tertiary folding. The induced fit of substrates to catalytic enzymes could be promoted in the same way. Future analysis of enzyme catalysis, allosteric effects and protein folding should therefore be, more ambitiously, based on an understanding of molecular shape as a quantum potential response. The function of DNA depends even more critically on non-local effects. 

---