Therefore pyruvate must be oxidised to yield Acetyl-CoA and CO2 which is carried out by pyruvate dehydrogenase (PHD). This is a complex structure that consist of a cluster of enzymes found in the mitochondria of eukaryotic cells. This reaction is called the oxidative decarboxylation. It is an irreversible oxidative process. Here the carboxyl group is removed from the pyruvate as a molecule of C02 and the remaining two carbons are used to become the acetyl group in the Acetyl-CoA.
Oxidoreductase catalyses an oxidation- reduction reaction as implied by its name. This reaction involves oxidation which is the loss of electrons and reduction which is the gain of electrons, both of which occur simultaneously and depend upon each other. An example of an Oxidoreductase enzyme is Lactate Dehydrogenase. The class Transferase catalyses reactions which transfer functional groups such as amino groups, phosphate groups or others. An example of the Transferase class of enzyme is Alanine Deaminase.
The three things that can cause the enzyme to denature is a large change in pH level, High Temperature, and substrate concentration. According to our knowledge, we know that a large change in pH will cause instability in the protein structure thus resulting in denaturation of the enzyme. From the data, we can see that pH 3 (total:6.3) and 10 (total:6.2) were the slowest because pH 3 is probably the highest acid and pH 10 is the highest base. The highest acid or base pH represents a large change which would cause the enzyme to denature. The fastest pH was 6 (total:34.5), and it seems that there wasn’t a large change which resulted in a stable structure.
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
Globin- It is a protein surrounding & protecting the heme molecule. Heme synthesis: Heme synthesis is carried out in mitochondria & cytosol of the cell involving cascade of steps :- 1) The first step occurs in mitochondria, where condensation of succinyl-CoA & glycine is carried out by enzyme ALA-synthase resulting in product formation i.e. 5-aminolevulinic acid. 2) 5-aminolevulinic acid is transported to the cytosol for formation of porphobilinogen molecule. 3) After formation
Porphyrin can also be found in cytochromes, haemoglobin, and the oxygen storage myoglobin. Chlorophyll a, the most common form of chlorophyll, is contained within all photosynthetic organisms which absorbs light from violet-blue and orange-red wavelengths making them green.
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
INTRODUCTION: Arginase is an enzyme- enzymes are biological catalyst which drives a reaction at the speed of life. Arginase is a hydrolase, hydrolases catalyze hydrolysis reactions, this is determined via the E.C number (Nelson and Cox 2008). Arginase has the EC number is 22.214.171.124 (Schomburg 2015). The enzyme ‘commission number’ is the arithmetical classification that is used for enzymes which indicates the chemical reaction they catalyze. EC 3 are hydrolases, which forms two products from the substrate via hydrolysis.
Temperatures that are too high denature the enzyme and halt the enzyme’s activity (2). Catalase denatures starts to denature at fifty five degrees Celsius (2). Reactions in the human body produce hydrogen peroxide as a product (1). Since hydrogen peroxide is poisonous to the human body, catalase catalyzes hydrogen peroxide into water and oxygen (2 H2O2 → 2 H2O + O2) (1). According to the collision theory, a reaction can only occur if particles collide with sufficient energy to overcome the activation energy and with correct geometrical orientation (3).
On the other hand chlorine when reacts with any substance it adds chlorine molecule or substitutes chlorine atom from substance. Chlorine dioxide responds specifically with amino acids and the RNA in the cell. It is not clear whether chlorine dioxide attacks the cell structure or the acids inside the cell. The generation of proteins is avoided. Chlorine dioxide influences the cell layer by changing film proteins and fats and by anticipation of
Polarity shared electrons get pull away difference in electrical charge at one end as opposed to the other end 2.3 The Ionic Bond 1. Ionic bonding when the electronegativity differences between 2 atoms were so extreme that the electrons were pulled off 1 atom only to latch on to the atom that was attracting them A: What is an Ion? 1. Ion is a changed atom or an atom with the number of electrons different from it number of protons 2. Ionic bonding is the chemical bonding in which 2 or more ions are linked by virtue of its opposite charge 3.
In aerobic respiration the “CO2 produced during cellular respiration can combine with water to produce carbonic acid.” While CO2 is produced, the amount of CO2 produced is different depending on the organisms, in this case crayfish. To test the changes in pH, NaOH is used to neutralize the carbonic acid produced by the crayfish, by which the