Serine Protease Lab Report

4) Dehydration reaction between α and β carbons catalyzed by β-hydroxyacyl ACP dehydratase. 5) Reduction of trans-double bond by enoyl-ACP reductase utilizing NADPH as coenzyme. 6) Repetition of the above mentioned steps until palmitoyl-ACP is produced, the final product. This palmitoyl-ACP is then cleaved to palmitate and ACP by palmitoylthioesterase enzyme Regulation Of fatty acid

As one would expect this enzyme is allosterically regulated. This enzyme is allosterically activated by N-acetyl glutamate. N-acetylglutamate is a precursor for ornithine biosynthesis and is an essential activator for the urea cycle. N-acetyl glutamate also serves to coordinate related pathways. The carbamoyl phosphate formed by this reaction enters into the urea cycle as a substrate for ornithine transcarbamoylase which catalyzes the following

coli reacts with the CoA affinity. The synthesis of succinyl CoA is thought to occur at an active binding site in the case of E. coli. If ATP binds at the second active site, there is formation and release of the Succinyl CoA at the initial site. Binding of ATP at the second site causes the site to undergo phosphorylation. ATP, magnesium ions, the enzyme, and phosphate incubated in the presence of hydroxylamine trapping succinyl CoA and pyruvate kinase-lactate dehydrogenase ADP.

It involves initial activation of the carboxylic acid moiety with ATP, generating an acyl adenylate and pyrophosphate. Bound acyl adenylate reacts with coenzyme A (CoASH) to yield a high energy xenobiotic-CoA thioester intermediate that will link the activated acyl group to the amino group of the acceptor amino acid with regeneration of CoASH.101 Glutathione conjugation involves conjugation of the tripeptide glutathione with a xenobiotic that is enzymatically catalyzed by glutathione transferases. The detoxification pathway of xenobiotics via glutathione is discussed in

Alkaline phosphatases (ALP), members of the phosphomonoesterase family, hydrolyze the oxygen-phosphorus bond of organophosphates using metal ions to release an inorganic phosphate under alkaline conditions.1,2 These enzymes are dimeric metalloenzymes containing two Zn2+, one Mg2+, and a serine residue in the active site of each monomeric subunit, in both prokaryotes and higher eukaryotes.2,3 Studies have shown that the three divalent cations are essential for enzymatic activity to catalyze the formation of an alcohol and an inorganic phosphate (Figure 1). In E. coli, the zinc ions are positioned to activate the serine and water for nucleophilic attack and ultimate cleavage of the bond, in addition to holding the phosphate moiety of the substrate. The magnesium ion has been suggested to stabilize the transferred phosphoryl group by a water molecule, using a separate mechanism by which the zinc ions function.3 Although ALPs are found widely in nature and function similarly on the biochemical level, there are locational

The α-ketoglutarate then enters the tricarboxylic acid (TCA) cycle where it is reduced, then co-enzymes (NADH and FADH2) are produced. The co-enzymes are used in the electron transport chain by the mitochondria to synthesize ATP (Blachier,

One monosaccharide will lose an H atom from carbon atom number 1 and the other will lose an OH group from carbon number 4. This is what is known as the C1-4 bond or a glyosidic bond. When the bond is formed, because one bond loses a H atom and the other a OH atom a loss of water will take place which is known as a condensation reaction. The opposite of this formation is when 2 monosaccharides become a disaccharide. This requires a water molecule (H) and sugar molecule (OH) to be injected back into the formation and this reaction is called a hydrolysis

Therefore, water and ethylene terephthalate are formed. 2. Mechanism between dimethyl terephthalic and ethylene glycol In this reaction, heat use as catalyst. Figure 10: Mechanism between dimethyl terephthalate and ethylene glycol As we known heat is involved in this reaction. Figure 10 shows the reaction between dimethyl terephthalate and ethylene glycol.

Davidek and Davidek (1995) stated that biogenic amines are normally formed in food as a consequence of the metabolic process during storage, spoilage or ripening. After degradation of proteins either by autolysis or by bacterial proteolysis, free amino acids are formed which act as precursors of biogenic amine with the aid of decarboxylase enzymes. Straub et al. (1995) mentioned that the biogenic amines in foods are mainly formed by amino acid decarboxylation of bacteria. During a fermentation process the protein breakdown products, peptides

This enzyme catalyzes the decomposition of hydrogen peroxide (substrate) into water and oxygen when it is not denatured. The enzyme substrate complex is when the enzyme and substrate bonded together on the active site splits and splits the hydrogen peroxide into oxygen and water. Lastly, the induce fit hypothesis is stating how the exposure of an enzyme to a substrate causes the active site of an enzyme to change until a substrate can completely bind to

As this electron shift occurred, the alcohol attacked the carbocation that lost its double bond. The acid catalyst then deprotonates the alcohol so it could retain its neutral charge and then the acid protonates the other hydroxide group, to produce H2O which separates from the main compound to stabilize its own charge and then carbocation rearrangement occurs to form a pi bond.

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 the production of hydrogen sulfide from cysteine and fermentation of glucose and lactose. Last test, inoculation of litmus milk is used to determine the fermentation of lactose, casein, lactalbumin, and

Dibasic phosphate and ammonia are considered renal buffers. Once buffered, the hydrogen is secreted and buffered within the lumen by phosphate and ammonia. As stated above in the carbonic acid-bicarbonate, the bicarbonate is then reabsorbed. This results in new bicarbonate within the plasma. This attributes to the

Enzymes are made of amino acids, it 's made of anywhere from a hundred to a million amino acids, each they are bonded to other chemical bonds. The enzymeʼs have an active site that allows only certain substances to bind, they do this by having an enzyme and substrate that fit together perfectly. If the enzyme shape is changed then the binding