Tropb Enzyme Lab Report

Following the known procedures [72]–[75] which start from the Diels-Alder reaction of naphthoquinone and β-myrcene, compound 4a (Figure 3.18) was obtained in a one pot synthesis. This anthraquinone was used as the precursor for the following steps and also as the reference compound in the NMR-experiment. For the next step a classical method for the reduction of

The purpose of this experiment was to perform a nucleophilic substitution reaction to construct a biologically active compound from two simple parts and then to recrystallize the product collected, which is a purification technique that purifies solids based on differences in solubility. In order to accomplish this, other techniques such as heating at reflux, and suction filtration were used. Heating at reflux is a technique used in lab that allows a solution to be heated for a certain amount of time once it begins boiling. Suction filtration is a separation technique that is combined with a water aspirator and was used to collect the product from this experiment, which was 2-methylphenooxyacetic acid.

William Fung TA: Gayani Batugedara Bio 1LA, Monday 4-7pm Lab 5 Introduction: Enzymes Question #1: How does the concentration of substrate affect the reaction rate? 1. If the amount of concentration of substrate is increased, the reaction rate will be also be increased.

1 was reacted in a prepared solution of potassium tert-butoxide and methyltriphenylphosphonium bromide for 18 hours. Reactions were performed in dried diethyl ether in an atmosphere of nitrogen at room temperature. Reaction products were isolated by column chromatography. The yield of 4 was determined by initially by weight, followed by purity determinations from the 1H NMR spectrum analysis, and found to be 20%. Results of six published articles for the synthesis of 4 with these reagents show varying yields from 36 (Radomkit et al., 2011) to 89% (Ventura & Taylor, 2014) under differing experimental

THE EFFECT OF TEMPERATURE ON THE RATE OF ENZYME ACTIVITY DB-16-0081 Co-partner: TIMORE NURDINOV Introduction The aim from this experiment is to observe the effect of factors such as pH, temperature and inhibitor on enzyme activity and how it works.

Introduction: Enzymes are specifically folded proteins which catalyse biological reactions in living organisms, they consist of an active site in which specific substrates can enter and a reaction takes place. As the enzyme does not permanently change structure, meaning the active site stays the same it allows multiple substrates to complete the reaction through single enzymes. The substrates are complementary to the active site of the enzyme and can be synthesised or degraded in order to create new products useful to the organism. Enzymes enable the substrates to be orientated in a way that allows for the reaction to take place more readily without relying on the chance of accurately positioned collisions of particles with sufficient energy.

Starting from Naphthalene, the following synthetic strategy, Figure-5, was created using techniques discovered by the national chemical laboratory. Step one is the addition of an alcohol group to Naphthalene using Toluene and 4-monooxygenase (Copley, S. D). Once 1-naphthanol is the starting material used by the nation chemical laboratory to synthesis propranolol. The following synthetic strategy is used to create propranolol from 1-naphthol: “(a) 3-bromopropanol, 10% aq NaOH, reflux, 6 h, 67%; (b) IBX, DMSO, rt, 2 h, 89%; (c) PhNO, L-proline, CH3CN, 20 °C, 24 h then NaBH4, MeOH, 20 °C, 0.5 h; (d) 10% Pd/C, MeOH, H2, rt, 6 h, for two steps 79%; (e) PPh3, DIAD, reflux, 6 h, 67%; (f) isopropylamine, CH2Cl2, rt, 12 h, 83%; (g) Et2O, HCl gas, 1 h, 86%” (Panchgalle, S. P.). Some of the important steps in this synthetic strategy is using 1-naphthol because it is a cheap and readily available starting material. Also this procedure produces high yields and is not harmful to the environment (Panchgalle, S. P.). Figure-6 and 7 are mechanisms for the conversion of naphthalene to 1-naphthol by toluene 4-monooxygenase, and the reaction labeled “a” in

The enzyme lab was used to determine the different factors that could affect the productivity of an enzyme. In the lab, the reaction between the hydrogen peroxide and the liver was an exothermic reaction because the temperature of the test tube rose when the hydrogen peroxide was placed into the liver. Heat is a form of energy and the temperature rose as the reaction progressed. In the test tube B, the temperature rose from room temperature to around r30ºC showing that it was an exothermic reaction. I think that the heat from the reactions of the enzymes inside my body keep my body warm and prevent the environment of these enzymes from becoming too cold and the basic functions of the body could not be carried out.

To a suspension of an a-N Boc protected 2,4-diaminobutanoic acid (1.0mmol, 1.0eq.) in MeOH (5mL), Ethyl 2 – azido – 2,2 – difluoroacetate (1.5mmol, 1.5eq.) and TEA (2.0mmol, 2.0eq.) were added. The reaction mixture was stirred for 3 hours at rt. After evaporation the mixture was dissolved in ethylacetate (10mL) and washed with 0.1M NaHSO4 aqueous solution, water, and brine, dried over anhydrous Na2SO4, filtered, and evaporated to dryness to give essentially pure (S)-2-amino-Boc-4-(2-azido-2,2-difluoroacetamido)butanoic acid. To this solution of acylated α–N–Boc protected diaminoacid in dry DCM (3mL) 4M HCl in dioxane solution (1.25mL, 5.0mmol, 5.0eq.) was added dropwise at 00C. The reaction mixture was stirred for 3 hours at rt. The precipitate

Using various alcohols, the substitution reactions (Sn2 and Sn) were utilized by helping with which functional groups reacted, in which way. Developing a mechanism for the alcohols are discussed.

Bis(2-chloroethy1)aminophosphoric dichloride (73.5g, 28.4mmol) is dissolved in THF (150mL).6 A solution of 3-aminopropanol (21.3g, 28.4mmol) is dissolved in a separate bath of THF (150mL), and triethylamine (79.0mL) is added.6 These two solutions are simultaneously added dropwise into stirred dry THF (300mL) over 3 h.6 Once both of the solutions have been added, the reaction is left overnight at room temperature, with continuous stirring.6 The resulting solution is then vacuum filtered as to remove the Triethylammonium hydrochloride, and the filtrate will evaporate under vacuum.6 The remaining residue is then subject the silica gel chromatography (100g), with chloroform-methanol.6 This should result in a colourless oil, which is dried under vacuum over P401o. The dried substance is then recyrstallised from dry ether at -78oC.6 This chemical synthesisV was reported by Verkade in 1978. Verkade and his research team reported a yield of

The rate at which O2 is produced at normal body temperature with a plus or minus temperature. Introduction The scientific report is on the testing the effect of temperature with enzymes. Enzymes are proteins that act as a catalyst which speeds up the rate of reaction of the substance. These reaction rate are chemical reaction pushed or forced by environment factors like temperature, time, concentration, other enzymes which may block the reaction or even pH. Basically, enzymes are proteins that speed up chemical reactions.

Enzymes are considered catalysts that speed up chemical reactions without being used in the process. Enzymes react with substrates to form a temporary intermediary complex from which the new product gets released. The enzyme that is unchanged and released at the end of the reaction will be able to again combine with more substrate until all of the substrate is utilized. The enzymes in living cells immensely accelerate chemical reactions and by governing relative reaction rates, regulate the directions of metabolic change. Enzymes are greatly affected by changes in pH because they are proteins.

NADH regeneration technologies have made numerous advances in recent decades(2). The most adopted technology by industry is for this purpose is the enzymatic regeneration of NADH. However, current enzymatic methods are technically difficult to execute and are not applicable to all biosynthetic transformations. These methods require a suitable enzyme to couple to the co-substrate, engineering an efficient separation strategy plus ultimately designing a rational reaction route(2-5). Moreover, these methods require excess amounts of sacrificial electron donors (e.g. 1,4-butanediol, ethanol, isopropanol) and the corresponding products are discarded as waste also, many result in the production CO2.

It is made up of extraordinary form, with two ring fused jointly through one of their sides. The two rings are ureido and thiophene moieties. Biotin is heterocyclic, S-comprising monocarboxylic acid. It is formed from two precursors, alanine and pimeloyl-CoA around three enzymes. 8-Amino-7-oxopelargonic acid synthase is a pyrodixal 5ᶦ-phosphate enzyme. The pimeloyl-CoA, be able to developed by a qualified fatty acid pathway comprising a malonyl as the starter. 7 and 8 Diaminopelargonic acid or DAPA aminotransferase is unique in using S-adenosyl methionine or SAM as the NH₂ donor. Dethiobiotin synthethase catalyzes the establishment of the ureido ring through a DAPA carbamate started with ATP. Biotin synthase reductively devides SAM into a deoxyadenosyl radical‒a primary radical created on dethiobiotin is trapped by the sulfur donor, which was form to be the iron-sulfur (Fe-S) center contained in