General Information about Urease
Urease is an enzyme found abundantly within organisms such as plants, fungi, bacteria, invertebrates, and is also present within the soil. Its function is to convert the organic compound urea into ammonia and carbon dioxide. Within animals, urea is excreted as a waste compound through the metabolism of nitrogen-containing substances; urease is therefore not required within animals. For organisms such as plants, fungi, bacteria etc., urea serves as a source of nitrogen, which is essential for normal growth. Urease is abundantly present within these organisms to assist in this conversion.
Structure, Function, and Applications of Urease in various fields
Structure: Urease is a trimer consisting of 3 subunits, α, β, and γ. Each of these units (αβγ) is further composed of four structural domains, two for the α subunit and one each of the β and γ subunits; each unit is arranged in a T-shape and has dimensions of 75 x 80 x 80 Å. These subunits are further arranged in a triangle consisting of three of these αβγ-trimers denoted as αβγ, α’β’γ’, and α”β”γ”, and this final molecule has the dimensions of 120 Å. These subunits form substantial hydrogen bonds and hydrophobic interactions between them that stabilize the molecule. Each portion of the triangular molecule is composed of specific components of the trimer; the sides consist of α, α’, and α” subunits containing 570 residues of each, the vertices are composed of the β, β’, and β” subunits containing 121 residues of each. The γ, γ’, and γ” are smaller residues and are tightly packed on one side of the triangle, containing 100 residues each.
The active site of the enzyme is present in the α, α’, and α” subunits contained within the αβ-barrels, which ...
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...nium given off by processes other than the activity of urease.
Discussion: This particular enzyme assay in question employs the optimal techniques/materials in order to achieve the highest amount of precision in the assay process. As urease is a soil enzyme and is actively involved in the breakdown of urea the release of its products, ammonia and carbon dioxide, are direct indicators of its concentration and activity within the soil. In this experiment, the liberation of ammonia is being employed as an indicator. Other components being utilized play a vital role in controlling the conditions of the experiment, as the THAM buffer, and the limitation of microbial activity, through toluene. The control experiment is crucial as it eliminates the addition of ammonia content being released by other sources within the soil into the final reading, providing accurate data.
The isolate possesses some enzymes required for hydrolytic reactions. Hydrolytic enzymes found to be secreted from the bacterium, are -amylase, casein, and PYRase. In the starch hydrolysis and casein tests, there was a zone of clearing around the bacterium, which was indicative of the secreted enzymes necessary to break down starch and casein. In the PYR test, the presence of PYRase was detected by a color change to red on the PYR disc after the addition of the PYR reagent (p-dimethylaminocinnamaldehyde). Hydrolytic enzymes for which the EI tested negative were urease, gelatinase, and DNAse. In the Urea Hydrolysis test, it was observed that the urea broth did not have a color change, indicating that there was no urease secreted to break down urea in the broth. Similarly, there was no gelatinase present to break down gelatin in the Gelatin Hydrolysis test, so the nutrient gelatin remained solid. It was concluded that the EI does not possess DNase because there was no clearing zone around the bacteria, indicating that DNA had not been
The control for both curves was the beaker with 0% concentration of substrate, which produced no enzyme activity, as there were no substrate molecules for...
When this substrate fits into the active site, it forms an enzyme-substrate complex. This means that an enzyme is specific. The bonds that hold enzymes together are quite weak and so are easily broken by conditions that are very different when compared with their optimum conditions. When these bonds are broken the enzyme, along with the active site, is deformed, thus deactivating the enzyme. This is known as a denatured enzyme.
The setting in both Lord of the Flies and I Only Came to Use the Phone contributes to the dehumanization of the characters in each of the readings. The settings are both isolated, which is the cause of all the chaos that takes place because when you take a human being out of the comfort of society, they go back to their natural animalistic tendencies in order to survive. Survival of the fittest is present in these quotes. Also, the island archetype plays a huge role in both of the stories.
Finally, the last part of the experiment examined the enzyme activity at different pH levels. Four sets of 11 tubes were set up in this part. The procedure for this part is the same as before, but 4 other buffers were substituted for the standard pH 7.3 phosphate buffer. Set A used the 5.5 pH buffer while set B used the 6.5 pH buffer. The buffer of pH 8.5 was used for set B and for set D the pH was 9. The absorbance readings for 4 sets were taken and recorded in table 13. Using the linear equation that the best-fit line gave for each set, the Km and the Vmax of each set were determined. Then, table 15 was made by dividing the Vmax by the Km. of the four pHs. The Vmax and Km of the control set were also used to make
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
The enzymes have active sites on their surfaces to allow the binding of a substrate through the help of coenzymes to form enzyme-substrate complex. The chemical reaction thus converts the substrate to a new product then released and the catalytic cycle proceeds.
An enzyme is a catalysis and catalysis s substance that increases the rate of a chemical reaction without itself going through a permanent chemical change. In this lab we will discover exactly how the substrate connects with the active site. The main substance we use throughout this lab is peroxidase a eukaryotic organelle from plant tissues. Once there is a color change we test that using a spectrophotometer. Introduction
Meningitis, it’s an infection in the cerebral spinal fluid and inflammation of the meninges; the three outer layers of the brain. To be more specific, those three layers are called the Dura mater, Arachnoid mater, and the Pia mater. There are three main types of meningitis that will be discussed throughout this paper; viral, bacterial, and fungal. Each form is very similar but they all vary in terms of causative organisms, treatment and severity. Although meningitis is not very common, it can become very severe and always needs to be treated immediately.
Cystitis is the medical term for inflammation of the urinary bladder. Most of the time, the inflammation is caused by a bacterial infection, and it’s called a urinary tract infection. A bladder infection can be painful and annoying, and it can become a serious health problem if the infection spreads to your kidney.
The UBE3A gene is responsible for the synthesis of the enzyme ubiquitin protein ligase. Ubiquitins are enzymes, which act as markers for proteins that need to be degraded. These enzymes attach a small protein called ubiquitin to ...
As a biochemist, I am interested in how the cell works in highly regulated manner. Ubiquitination, the degradation mechanism, has been a fascinating field for many researchers. From this enzyme project, ubiquitination pathway was introduced in step by step. Also, the mechanistic details of RNF4 E3 Ligase were investigated with various experimental data.
Urinary Tract Infection, also known as UTI, occurs in two common locations, the bladder and kidneys. The kidneys are important organs that aid in filtering out waste products from blood and maintaining water distribution throughout the body. The waste products are filtered out via bladder, which is the reason of the bladder being the second site for the infection. A normal human being has two kidneys, one on left and right side, a bean shaped organ, and is located at the back of the abdomen. “Each kidney is about 11.5 cm long, 5-7.5 cm broad, 5 cm thick, and weight about 150 grams” (HealthInfoNet, Paragraph 2). Furthermore, a bacterium named Escherichia coli lives in both the kidneys and the GI tract. E. coli is part of the human body and produces
Enzymes are biological catalysts, usually made of proteins that speed up chemical reactions in biological systems. They are biodegradable and not consumed within the reaction. They usually catalyze the hydrolysis of specific bonds.Enzymes are categorized by which type of reaction they catalyze and the substance the act on to their active site (substrate). The suffix “ase” is connected to the substrate to signal the enzyme acting on it. For example,