Phosphorylation

Phosphorylation is the formation of a high-energy bond between a phosphate group and a target molecule in the presence of an enzyme. In a cellular environment, it is estimated that 1/10th to half of the total proteins are phosphorylated to perform a specific function in the cell. The concept of protein phosphorylation was first introduced by Edmond Fischer and Edwin Krebs in the year 1955, where they elucidated the necessity of ATP and a kinase (Known then as “converting enzyme”). Interestingly,

Molecular Biology Final Exam TITLE Mechanistic Analysis of Biguanide-Induced Inhibition of Oxidative Phosphorylation ABSTRACT Biguanide compounds are used clinically to treat a variety of conditions ranging from diabetes to malaria. Despite showing efficacy the underlying mechanisms of how these compounds work is still debated. It has be previously shown biguanides inhibit oxidative phosphorylation, specifically through inhibiting complexes in the electron transport chain. In the current study we

Introduction The Na-K-Cl cotransporter is a group of ubiquitous membrane transport proteins. This secretory cotransporter maintains electroneutrality by transporting ions with the stoichiometry of 1Na+: 1K+: 2Cl-. Two different gene isoforms of the Na-K-Cl cotransporter have been found. Both varieties of the symporter act to regulate and maintain cell volume and intracellular Cl- concentrations. However, the two different isoforms of NKCC vary structurally as although NKCC2 is around 60% homologous

Both substrate-level phosphorylation and chemiosmotic phosphorylation are mechanism that is utilize by the cell to add a phosphate group onto the substrate ADP to form ATP. In substrate-level phosphorylation, the phosphate is transfer from a phosphorylated compound to ADP forming ATP with the help of an enzyme. The source of energy that drive substrate-level phosphorylation come from energy released from the hydrolysis of the phosphorylated compound or also known as the phosphate transfer potential

NetPhos 2.0 analysis projected 9/11/11 serine, 2/3/2 threonine and 5/7/7 tyrosine phosphorylation sites for GS01/GS02/GS03 proteins respectively. The homology modelling of the enzyme shows 12 identical subunits, arranged in two layers of 6. The secondary structure of GS consisted of 7 alpha helix and 15 beta strands. The binding residues,

Introduction Bacteria are prone to various stressors so they need to sense and respond to these fluctuating conditions in order to survive. Two-component plays an important role in the bacterial kingdom to sense and adapt themselves to these varieties of stressors, for example oxidative stress, protein misfolding, nutrient starvation and many more. It is first described by Ninfa and Magasanik (1986) in the study of nitrogen starvation in Escherichia coli. Two-component system consists of a sensor

complex with others such as c-fos and is an important substrate of JNK phosphorylation playing a role in regulation of gene expression relating to a number of cytokines (Gius et al, 1999; Johnson and Lapadat, 2002; Weston and Davis, 2007). The c-Jun can arrange into homodimers with itself but only occurs when c-fos is not present and it can also arrange into a heterodimer with c-fos (Halazonetis et al, 1988). Phosphorylation by JNK on c-Jun occurs at the N-terminal in the activation domain at serine

produces less reactive oxygen species (ROS), and it generates ATP more rapidly than oxidative phosphorylation, all of which are considered to facilitate rapid growth and survival (1). Besides inducing apoptosis and controlling the cell cycle, p53 has been demonstrated to be a central component and key regulator of the metabolic stress machinery. The metabolic balance between glycolysis and oxidative phosphorylation is heavily coordinated by p53 activity, which is activated by

waste products. Glycolysis, Oxidation of Pyruvate, Citric Acid Cycle, and Oxidative Phosphorylation are the steps that help cells function properly. Glycolysis is the first step that takes place inside of the cytoplasm. The first half of glycolysis uses two ATP molecules in the phosphorylation of glucose, which is then split into two three-carbon molecules. The second half of glycolysis involves phosphorylation without ATP investment and produces two NADH and four ATP molecules per glucose. Pyruvate

monoacylglycerol, a chain of fatty acids, peptides and amino acids, respectively. There are two ways that ATP is synthesized: 1. Oxidative Phosphorylation, the main method for energy production and the second is substrate level phosphorylation which is the transfer of a phosphoryl group and this method can happen both in the cytoplasma and mitochondria. In oxidative phosphorylation, electrons from the fuel molecules are removed by coenzymes, such as nicotinamide adenine and flavin adenine through protein complexes