Enzymes are the biological molecules, generally made up of proteins that substantially speed up the rate of practically all the biochemical processes occurring inside the cells. These are important to cell processes and perform a broad range of essential functions in the body, such as digestive aid and cell metabolism (Daniel & Danson, 2010). Enzymes are involved in all types of biochemical processes involved in development, blood clotting, regeneration, illness, respiration, digestion, reproduction, and several other bioactivities. Enzymes are functional materials on biological aspects of several roles of living organisms. Many enzymes enable the splitting of big molecules into smaller molecules that get readily absorbed in the body. Many enzymes functions to join two molecules together to form a new molecule to shape. The enzymes function as very specific catalysts, which mean that a particular enzyme only speeds up one specific reaction in the cellular processes (Ramirez & Tolmasky, 2010).
The molecules in which the enzymes bind are known as substrates. The region on the substrate where the enzymes bind is known as the active site. There have been two theories that describe the relationship between the enzymes and the substrates. The first one is the lock-and-key model where the enzyme perfectly fits in the active site of the substrate. In the second model which is the induced fit model the active site and substrate bind and they align and alter the shape of the substrate for the attachment (Secundo, 2013). Whatever the case, the reactions which occur help speed more than a million times as soon as the substrates bind to the active position of the enzyme. The chemical processes lead to a new product or molecule, which separates further from the enzyme, catalyzing further reactions. Enzymes are classified into six categories according to the type of reaction catalyzed (Ricca et al., 2011):
Oxidoreductases catalyze intracellular reduction and oxidation reactions. The reactions involves the cofactors like NAD+/NADH and FAD / FADH2.
Transferases catalyze the transfer by a nucleophilic substitution reaction of the functional groups like phosphate, sulfate, methyl, glycosyl, formal, alkyl, acyl, and hydroxymethyl.
Hydrolases are the group of enzymes that catalyze cleavages of the bond by water reaction. Most hydrolases' normal role is digestive in breaking down the nutrients into smaller digestive units.
Lyases are the enzymes that catalyze the addition and reduction reactions.
DNA ligases are involved in any process involving the sealing from the DNA backbone of phosphodiester bonds.
Isomerases catalyze reactions to isomerization, such as racemization and epimerization.
Daniel, R. M., & Danson, M. J. (2010). A new understanding of how temperature affects the catalytic activity of enzymes. Trends in Biochemical Sciences, 35(10), 584-591.
Ramirez, M. S., & Tolmasky, M. E. (2010). Aminoglycoside modifying enzymes. Drug Resistance Updates, 13(6), 151-171.
Ricca, E., Brucher, B., & Schrittwieser, J. H. (2011). Multi‐enzymatic cascade reactions: Overview and perspectives. Advanced Synthesis & Catalysis, 353(13), 2239-2262.
Secundo, F. (2013). Conformational changes of enzymes upon immobilisation. Chemical Society Reviews, 42(15), 6250-6261.
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