Phenylalanine Essays

obtained exclusively by consumption. The essential amino acids in humans include histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. Phenylalanine, one of the essential amino acids, is used in the body to form tyrosine. An enzyme called phenylalanine hydroxylase is involved in adding a hydroxyl group to phenylalanine in what is called a hydroxylation reaction to form tyrosine (Pratt 485). Since tyrosine can be produced in humans in this way, it is

The phenylalanine/hydroxycinnamte pathway: The phenylalanine/hydroxycinnamte pathway starts with metabolism of Phe and called general phenylpropanoid metabolism. The reactions involving formation of hydroxycinnamates and their activated forms (CoA thoesters and 1-O-acylglucosides) fall under the purview of phenylalanine/hydroxycinnamte pathway [Figure 17.3]. First enzyme of hydroxycinnamte pathway is phenylalanine ammonia lyase (PAL; 4.3.1.24) which catalyses the non-oxidative deamination of Phe

stirrer was prepared through placing it in the fume cupboard. 1 mmol of L-Phenylalanine was placed and weighed in a 5 mL conical vial. After that, a spin vane was inserted into the vial while adding 0.75 mL of 1M H2SO4 solution. During the addition of the sulphuric acid, the solution was stirred at room temperature until the amino acid (L-Phe) completely dissolved. An ice bath was prepared and used for cooling the L-Phenylalanine solution at a temperature of 40C (a selected temperature lower than 50C)

due to deficiency of the enzyme phenylalanine hydroxylase (PAH). This is a rare genetic condition in which occurs inability to metabolise or break down the essential amino acid phenylalanine to tyrosine due to enzyme deficiency. Amino acids are considered as the building blocks of protein and so does this amino acid i.e. phenylalanine. Phenylalanine is an essential amino acid and hence, finds a role in protein synthesis in our body. Certain sources of phenylalanine include most of the proteins and

milestones and would experience developmental delay. If a mother has PKU and it is left untreated her unborn baby can have slow growth which will affect the baby’s physical development. People with the condition also have fairer skin, hair and eyes as phenylalanine is involved in the body’s production of melanin which is the pigment responsible for skin and hair colour. PKU can also affect an individual’s intellectual development as they may develop learning difficulties and have difficulties problem solving

Phenylketonuria, or PKU, is a genetic disorder in which a person’s body is unable to break down an important amino acid found in protein called phenylalanine. This disease can be found in 1 of 10,000 to 15,000 babies across the United States. This disease is mostly found in people of European or Native American heritage. However, PKU can be found the same amount in both women and in men. Phenylketonuria is carried on a recessive allele. As a result, both parents must pass down the same recessive

diagnosed with Phenylketonuria” (Intro): Phenylketonuria, which is commonly known as PKU, is usually caused from an inherited gene, passed down from both parents, that increases the levels of phenylalanine in the bloodstream. Phenylalanine is the building block of proteins that is obtained through the diet. Phenylalanine is found in all protein food sources and even some artificial sweeteners. This disorder is very important because if it is not treated, it could lead up to intellectual disability and other

turn, functional diversity (Bruice). Amino acids can be divided into polar, non-polar, acidic, and basic (Bruice). The amino acids used in this experiment are Phenylalanine, Leucine, Lysine, and Alanine. Phenylalanine, Leucine, and Alanine are all non-polar amino acids; whereas, Lysine is basic (Bruice). Lysine, Leucine, and Phenylalanine are essential for the human body; whereas, Alanine is non-essential (Bruice). Essential amino acids cannot be

(PKU) is an inherited disorder. A Norwegian physician and biochemist Dr. Ivar Asbjorn Folling discovered PKU. It was discovered in 1934, in Norway. It is found in all proteins.PKU can be inherited, it increases the levels of a substance called phenylalanine in the blood stream. Babies are tested with a heel prick to draw blood when they are born. People with Phenylketonuria can live a perfectly normal life if they eat correctly. All of the Possible effects on the body PKU has symptoms like seizures

amylase that hydrolyzes starch after streaking on a starch plate. Next test, inoculation of a urea broth and is used to determine if unknown #398 contains urease that hydrolyzes urea. Last test, inoculation of phenylalanine agar is used to determine if phenylalanine deaminase oxidizes phenylalanine into phenylpyruvic acid and ammonia. Sixth test, is a Multiple Test Media used to determine the physiological characteristics of unknown #398. First test, Inoculation of Kligler 's Iron agar was used to determine

enzyme that helps by breaking down the amino acids tyrosine and phenylalanine. Tyrosine is known as a non-essential amino acid with a polar side group and it has a special role to the phenol functionality. Tyrosine appears in the proteins that are a part of signal transduction processes. Whereas phenylalanine is more of an essential amino

test was performed on Unknown #57 with duplicate conclusions from the SIM test stating that the bacteria is nonmotile. 
 The phenylalanine test is performed to discover if a bacteria posses phenylalanine deaminase which gives it the ability to remove an amino group from the amino acid phenylalanine and metabolize it. A plate of phenylalanine is inoculated and if phenylalanine is broken down, phenylepyruvice acid, amonium ion, and water are formed as end products. Drops of ferric chloride are administrated

irreversible inhibitors. The three types of reversible inhibitors include competitive, noncompetitive and uncompetitive. The type of inhibitor can be identified by the reaction Vmax, Km and Ki. In this experiment, the inhibitor used was 75 mM phenylalanine. The results in this experiment were used to study the effects of enzyme concentration, inhibitor presence and substrate concentration in a biochemical reaction. The enzyme and substrate concentrations were calculated in part 1 along with the Vmax

negative result for urea hydrolysis. PHENYLALANINE Deaminase Test: This test looked for the enzyme, phenylalanine deaminase, which removed an NH2 group from cysteine to produce pyruvic acid, ammonia, and hydrogen sulfide. Next, five drops of ferric chloride was added to the tube. A positive test would turn a green color due to the reaction phenylpyruvic acid with the reagent, ferric chloride. A negative test stayed a yellow color indicating the absence of phenylalanine deaminase. 5 NITRATE REDUCTION

manual). The first will be the Absorbance at 280 nm which is a quick method that is used to find protein peaks. Proteins that contain tyrosine, phenylalanine, and tryptophan have a strong absorbance for UV light at 280 nm. According to the Material Safety Data Sheet, tyrosine can be slightly hazardous in the case of skin contact. In addition, phenylalanine can be hazardous if it comes into contact with eyes, if it is ingested, or if it is inhaled. Additionally, tryptophan may cause skin or eye irritation

ALKAPTONURIC ARTHROPATHY:- A RARE ENTITY Hemant Kumar†, Sagar Tyagi†, Parveen Hans†, Prof .Virinder Mohan* Department of Radiodiagnosis, Rohilkhand Medical college, Bareilly, (U.P.) India ABSTRACT Alkaptonuria is a metabolic disorder of tyrosine and phenylalanine metabolism in which there is absence of homogentisic acid oxidase whose deficiency leads to excessive accumulation of homogentisic acid in urine resulting in black color of urine on standing.[1] The disease is usually diagnosed in adults but a

The process of chemical digestion in the breaking down of food with enzymes so that they can become molecules such as nutrients, salts and water , so that way they are easily absorbed and utilized. The process of absorption involves moving such molecules through the GI epithelium and into the blood or lipids. Ingested food is initially broken down mechanically by your mouth into pieces that are easier to swallow, and then broken down again into even smaller pieces so that in can continue its journey

Chemistry Internal Assessment An Investigation into the Effects of Types of Leaves on Rf Values and Their Corresponding Amino Acids gwy287 Chemistry HL Word Count: Personal Engagement Statement Nature is a fascinating part of this world and discovering the inner parts makes it ever more interesting. Plants function through photosynthesis and because of proteins. These proteins are created by amino acids. Since I find nature so interesting, finding the different amino acids in various types of

The first task that I had to do upon receiving my unknown was making two subcultures of it. The “stock” culture would serve as my emergency backup in case my bug got contaminated, while the “working” culture was the one I would utilize to perform the biochemical tests. The next thing I did after this was the gram stain. The purpose of this was to find my bug’s gram designation and morphology so that I would be working in the right direction. My bug retained the safranin stain which meant it was gram

Why using natural pet safe ant killer can be advantageous? Description: to get rid of the pesky ants you can use both chemical ant killers and natural pet safe ant killer products. But the advantages that you can get from using the latter one cannot be gained from the former one. Whenever you think about getting rid of the ants from your home two things may come in your mind. There are mainly two ways by which you can tackle the problem effectively if the first one is using the chemicals then the