The Etymology of an Enzyme - Essay Example

The human body carries out many metabolic activities to maintain homeostasis as well as provide energy for that given body. To catalyze this energy and organic necessities to uphold the constructs of the body, enzymes are engendered to establish such feats in the body. Enzymes are proliferated out of the sequencing of the amino acids accordingly. Each type of enzyme has a different type arrangement, and therefore, each possess a specific function. In this dissertation, we will examine and discuss the function of enzymes and its proliferation. Then we will utilize acquired information to examine a given experiment. Scientists have explored the concepts of the processes of cells in its rudimentary stage. RNA, ribonucleic acid, is known to be the eldest type of organic molecule that contained gene makeup in biological existence (pg. 50, Barrick, Scientific American). DNA seemed to be an evolved trend later down the centuries. DNA now possesses all information concerning the constructs of the human body, including the structure of enzymes. Enzymes In comparison to DNA, RNA differs in nucleic acid component such as uracil rather than DNA's thymine. In addition, in some species, such as humans, RNA is single stranded. Erstwhile, RNA possessed the role of preserving genetic information and used as messengers to proliferate proteins to accommodate the cell's needs. RNA is composed of four nucleotides arranged in a chain of a five carbon sugar-phosphate molecules. The nucleotides are adenosine, uracil, cytosine, and guanine. The sequencing of these four nucleotides encodes information to regulate processes in the intercellular level as well as address homeostatic regulation outside of that cell and into the human body. In the article, "The Power of Riboswitches" written by Jeffrey E. Barrick and Ronald Breaker, RNA processes were studied through a medium or apparatus of binary fission of bacteria. Their study is purposed to understand the extended role of RNA inthe pre-historic era and use their findings to mitigate the negative effects ofdiseases. To understand the process of creating enzyme RNA proliferation, we have to explore how they are produced and pinpoint theirpurpose in modern cells. The process commences when RNA polymerase, an enzyme, attaches to DNA strands and copies portions of it. RNA polymerase unwinds and opens the double stranded DNA and reads the nucleotides and matched them up with composite nucleotides that fit. After transcription is done, the messenger RNA (mRNA) is released and capped on each side of the strand to prevent the enzymes outside the nucleus from disintegrating it. These mRNA are photocopies of the DNA. Now when the strand reaches outside, it is quickly read by ribosomes. Ribosomes are composed of ribosomal RNA (rRNA) that essentially deals with the synthesis of proteins. The ribosomes read the nucleotides assembled in sets of three called codons. Each codon sequence has a specific amino acid it pairs up with. Each amino acid is distributed tRNA or transfer RNA. After each codon is translated, the appropriated amino acid are assembled in the order of the codons on the mRNA and fused to together through the process of dehydration synthesis. Then that protein will leave the ribosome while the mRNA disintegrates for its extended exposure to the catalytic enzymes outside the nucleus. The components of the disintegrated mRNA are recycled. That protein can be an enzyme fit for metabolic activity. For a catalytic activity, the molecules at the beginning of the process are called substrates, and the enzyme breaks them down into different molecules, the products. Almost all processes in the cell need enzymes in order to occur at significant rates. Since enzymes are extremely selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell. Enzymes work by lowering the activation energy for a reaction, thus dramatically increasing the rate of the reaction. Most enzyme reaction rates are millions of times quicker in comparison to those of uncatalyzed reactions. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts by performing specific tasks. Enzymes are known to catalyze about 4,000 biochemical reactions (www.wikipedia.org). Not all biochemical catalysts are proteins, since some RNA molecules called ribozymes also catalyze reactions (Barrick, pg. 60). Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, pH, and the concentration of substrate. When a specific apparatus containing this activity surpass or decrease the categorical threshold in which the enzyme will effectively operate, this can cause an enzyme to denature and inhibit from doing its job. "Amylase is an enzyme that catalyses the hydrolysis of the polysaccharide starch (Amylose) to the disaccharide maltose. It is readily abundant in saliva, but somewhat unpleasant to obtain in large quantities. It is widely distributed in plant tissues, but is most abundant in seeds, where it apparently functions in initiating the breakdown of stored starch to glucose which is needed in large amounts during germination period. The point of the experiment is to find which seed Amylase is most abundant in, and if the circumstances affect this." Amylase is a name given to glycoside hydrolase enzymes (www.wikipedia.com) that brakes down starch. There are four different types of amylase; each possesses a Greek letter to respectively differentiate them from their functions. These types are the alpha-amylase, beta-amylase, gamma-amylase, and acid a-glycosidase. All of these react to long carbohydrates chains. The alpha-amylases are calcium metallozymes which are completely inert in the absence of calcium ions. During the presence of calcium, the alpha-amylase reacts on long carbohydrate chains to proliferate dextrin and maltose. This enzyme is common in animals because its utilization is seen heavily in the human gastro-intestinal track. Alpha-amylase is a major digestive enzyme in animals. It is said to operate faster than its isomers (i.e. beta and gamma- amylase). In beta-amylase, the catalytic activity yields sweetness in any given apparatus, such as fruit. Bacteria, Fungi, and plants synthesize this type of enzyme. It usually present in cereals containing malt. Microbes utilize this enzyme to break down Animals do not possess this type of enzyme although many mutualistic organisms that reside within the animal (e.g., micro organisms within the digestive track.) may possess it. Furthermore, Gamma-amylase continues the decomposition of starch after alpha-amylase molecules disappear or worn away inept to finish the job. Acid a-glycosidase is a form gamma-amylase that is found in mammalian intestines. Also the amylase is secreted in to areas of the human or animal body. The salivary glands secrete a form of amylase called ptyalin and pancreas. Ptyalin separates long carbohydrates into maltose dextrin. This catalytic activity commences to take place in the mouth and adjourns in the stomach due to the low pH level. Ptyalin's tolerance for working effectively is between pH 5.6 through 6.9. It will also operate effectively in the presence of Bromide and Chlorine at 37 degrees Celsius. If the conditions surpass these parameters, the enzyme will denature. Pancreatic amylase is dispensed by the pancreas via the gall bladder. After the stomach does its regular procedure, it pushes through peristalsis the food into the small intestine through a sphincter. The pancreas secretes the amylase with the appropriate materials to create an ambience for the enzyme to operate effectively. It then continues its hydrolysis of carbohydrates which commenced in the mouth. "Amylase enzymes are used extensively in bread making to break down complex sugars such as starch (found in flour) into simple sugars. Yeast then feeds on these simple sugars and converts it into the waste products of alcohol and CO2 (carbon dioxide). This imparts flavour and causes the bread to rise. While Amylase enzymes are found naturally in yeast cells, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread. This is the reason for long fermented doughs such as sour dough. Modern bread making techniques have included amylase enzymes into bread improver thereby making the bread making process faster and more practical for commercial use..Bacillary amylase is also used in detergents to dissolve starches from fabrics. Workers in factories that work with amylase for any of the above uses are at increased risk of asthma ("occupational asthma"). 5-9% of bakers have a positive skin test, and a fourth to a third to a third of bakers with breathing problems are hypersensitive to amylase." (www.wikipedia.org) There are many uses of amylase other than metabolic digestion. It can be used in baking and washing clothes. In an experiment, we will determine the reactivity of amylase on carbohydrates in a plethora of conditions. We will use seeds or grains to test its reactivity in those given conditions. Corn, wheat, oats and barely are used in this experiment. The apparatus that are used are twelve starch agar plates. The grains will be boiled, dried, or soaked. This will test the reactivity of amylase a given temperature. Procedure: 1. Prepare agar plates of equal quantity of agar to ensure a fair test and valid results. 2. Soak, boil and dry 3 of each of the 4 types of seeds and using one untouched seed. a. boil for 5 minutes b. soak for 18hrs (3pm-9am) 3. Using a 'Sharpe' pen, label the bottom of the plate: "soaked seeds", "boiled seeds" and "dry seeds". 4. Once seeds are ready, cut longitudinally with a sharp razor blade and place 3 of each on different agar plates, labelled as above, spaced at least 3cm apart to avoid clear zones colliding. 5. Incubate agar plates for 18hours 3pm-9pm at 25C. 6. Remove seeds (plates) and rinse plate gently using distilled water. 7. Flood plate with iodine solution, swish around as colour develops, rinse with distilled water. 8. Record results: - cut out clear area of agar and weigh mass on balance. Record results on table and note any difference. Results Seed/Variable Oats Wheat Barley Maize (corn) Dried Very little amount No production No production Very little amount Soaked moderate moderate Substantial amount Substantial amount Boiled Very good amount Very good amount Very good amount Very good amount Amylase present How much/g Overall, there was not a lot. Amylase consumption was apparent in boiled grain only. Overall, there was not a lot. Amylase consumption was apparent in boiled grain only. Amylase was present in this. Amylase consumption was apparent in boiled grain only. Amylase was present in this. Amylase consumption was apparent in boiled grain only. Ostensibly, the enzyme has some parameters that it operates in to work effectively. Placing an iodine solution on the agar to determine amylase consumption will halt any catalysis of the agar. (www.wikipedia.com) Also, as mentioned earlier, amylase functions effectively at 37 degrees Celsius. The boiled grains amylase consumption should very little due to that precept because the enzymes were denatured. However, the incubation of the boiled grain agar plates cooled it so much so that it allowed to reach around 37 degrees Celsius. Therefore, the boiled grain agar plates operated at satisfactory temperatures convenient for agar consumption. In the dried grain agar plates, agar consumption was low because the incubation which was placed 25 degrees Celsius slowed down the effectiveness of the enzyme. Albeit some grains demonstrated some agar consumption, it was very miniscule overall. The time allotted to the enzyme (18 hours) proved too small for the amylase to hydrolyze the agar. In the soaked grains, there seemed to be moderately consumption overall. These results should be similar to the dried grain agar consumption. However, they performed much better than that variable. The moisture may have increased the surface area for amylase to hydrolyze the agar. Under this hypothesis, agar consumption in the soaked grain exceeded that of the dried grain. Throughout this analysis, we have investigated through research the etymology of an enzyme as well as this particular enzyme at issue. Then, we placed this knowledge to the test by experimenting in varying conditions. The requirements and parameters provided by that research were kept. Bibliography: 1) Stuart J. Baum (1982). The introduction to organic and biological chemistry. New York: Macmillan 2) Schwartz, Shires, & Spencer (1989) Principles of Surgery. 5th Edition. New York: McGraw Hill pp.1935 3) Wilson, Braunwald, Isselbacher, Petersdorf, Martin, Fauci, & Root. (1991). Principles of Internal Medicine. 12th Edition. Volume 2. New York: McGraw Hill 4) ASSOCIATION OF ANAESTHETISTS OF GREAT BRITAIN AND IRELAND (2004) Checking Anaesthetic Equipment 3. London: Association of Anaesthetists of Great Britain and Ireland. 5) BURNS, C. & ROSENBERG, L. (2001) Redefining critical incidents: a preliminary report. International Journal of Emergency Mental Health. Vol.3 (1) pp.17-24. 6) Barrick, Jeffrey. (Jan. 2007) Power of Riboswitches. Scientific American pg. 50-56 7) Sinclair, David A. (March 2006) Unlocking the Secretes of Longevity Genes. Scientific American pg.60-67 Electronic sources: 8)http://en.wikipedia.org/wiki/Ribozyme 9) http://en.wikipedia.org/wiki/Enzymes 10) http://en.wikipedia.org/wiki/amylase 11) http://www.medscape.com/viewarticle/481798 Read More

 

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