Enzymes are considered catalysts; substances that increase the rates of reactions. Enzymes are responsible for thousands of metabolic processes that involve the sustainment of life, one common one is simple food digestion. Without enzymes, digestion would occur too slowly for life to continue. Enzymes maintain a protein structure consisting of one or possibly more than one polypeptide chains of defined primary structure, and take up a characteristic folded form in the native state. Should the structure be modified by an outside entity, the enzyme could be deactivated. Enzymes, because they are specific with the nature of the reactions they catalyze, they are divided into Stereospecific and chemical specificity. These specificificities allows for better research opportunities and understanding the enzyme.
Stereospecificity is a property of a reaction mechanism that allows for a different stereoisomer reaction product from a different stereoisomeric reactant basically, the enzyme is able to act on a steric or optical isomer. Chemical specificity entails three components: Absolute specificity - the enzyme catalyzes with only one enzyme. Group specificity - the enzyme will act only on molecules that have specific functional groups. These are more common and such functional groups include: amino, phosphate and methyl groups. Professor explains this by the example: An enzyme catalyzing the hydrolysis of sugar derivatives, such as ß-galactosidase, may require that the sugar be galactose and that this be joined to an aglycone through a ß-linkage to the first C atom of galactose (section 3.2). Finally, Linkage specificity - this enzyme will act on a particular type of chemical bond regardless of the rest of the molecular structure. It is only concerned with the type of linkage between A and B. For example, an esterase may hydrolyze many esters irrespective of the nature of the alcohol and acid moieties,
References: Tymoczko, J. L., Berg, J. M. and Stryer, L. (2013). Biochemistry: A Short Course (2nd edition). New York, NY: W. H. Freeman and Company. Tymoczko, J. L., Berg, J. M. and Stryer, L. (2006). Biochemistry (6th edition). New York, NY: W. H. Freeman and Company. es. Park,C. & Zipp, E.The effects of Temperature and pH on Enzyme Kinetics. Retrieved from http://www.rpi.edu/dept/chem-eng/Biotech-Environ/Projects00/temph/enzyme.html Lab manual- BCH4053L. Retrieved from http://www.chem.fsu.edu/chemlab/bch4053l/enzymes/activity/index.html Enzymes Retrieved from http://www.biologymad.com/resources/EnzymesRevision.pdf Effect of substrate concentration on the rate of an enzyme catalyzed reaction. Retrieved from http://click4biology.info/c4b/3/Chem3.6.htm#three Introduction to Enzyme. Retrieved from http://www.worthington-biochem.com/introbiochem/enzymeconc.html