Enzyme inhibitor

Angiotensin-Converting Enzyme Inhibitors (ACE Inhibitors) are a group of drugs that belong to the antihypertensive drug class. There are currently 10 ACE inhibitors that are available. ACE inhibitors can be taken either by themselves or can be combined with a calcium channel blocker or a thiazide diuretic to enhance the treatment This group of drugs is often used as a first line of treatment to treat both heart failure and hypertension. Some of these drugs include; benazepril (Lotensin), captopril

Acetylcholinesterase enzyme Inhibitors, preventing acetylcholine degredation through inhibition of Acetylcholinesterase enzyme. That would cause the accumulation of acetylcholine in synaptic cleft therefore prolong the neurotransmitter action. Acetylcholinesterase enzyme inhibitors action can be reversible and irreversible. The reversibility or irreversibility of the inhibitory action depends on the functional group available in the agent. Carbamates are derived from carbamic acid, the structure

Enzyme inhibitors are molecules that bind to enzymes to decrease their activity. Many drugs are enzyme inhibitors because by blocking the enzymes activity it can kill pathogens (shpanskaya and Melechko, 2008) Enzyme inhibitors assist in altering the catalytic action of an enzyme in order to slow down or stop catalysis (Worthington biochemical corporation, 2015). Inhabitation can either be reversible or irreversible. During irreversible inhabitation the inhibitor detaches slowly from its targeted

Introduction Enzymes are an important aspect of many physiological processes because they act as catalysts to speed up reaction rates. Some metabolic reactions have competitive and non-competitive inhibitors that can hinder reaction rates. Competitive inhibitors target the active site of an enzyme, resulting in an equal Vmax, but different Km. Noncompetitive inhibitors, on the other hand, bind to an allosteric site and change the shape of the active site, resulting in the same Km and a lower Vmax

Introduction to Urease Enzyme: Urease is an enzyme which catalyzes the hydrolysis of Urea into ammonia and carbamate; on later stage carbamate spontaneously yield carbonic acid and one more molecule of ammonia. Urease enzymes are included in super family of amidohydrolases and phosphotriestreases. It required binding of two nickel ions for its proper activity therefore known as Nickel dependent Metalloenzyme. (NH2)2CO +H2O → NH3 + NH2COOH NH2COOH +H2O → H2CO3 + NH3 Figure 1: Hydrolysis

Aconitase is one of the enzymes vital for the human. This enzyme is classified under the group of lyases. To be more specific, it functions as the hydro-lyases, breaking down the bond linking the carbon and oxygen through the dehydration. (NCBI, 1963) It also can perform the hydration under certain circumstances. Thus, aconitase is also known as citrate hydro-lyase and aconitate hydratase. (Kremer, 2013) The main metabolic pathway aconitase participates will be the aerobic respiration, especially

activity. Background: Malonate, also known as propanedioate, is a classic example of a competitive inhibitor. Malonate has a molecular structure that is similar to succinate, so it has the ability to bind to the active site of succinate dehydrogenase and inhibit enzyme activity. However, malonate is sufficiently different from succinate that it cannot be dehydrogenated. [1] Malonate working as an inhibitor to succinate oxidation is a popular occurrence. Succinate is oxidized to fumarate during the Kreb

Specific Aims We propose to modify the recently discovered natural product terpenoids to develop a selective iNOS inhibitor with improved in vivo properties. Specific Aim #1: To confirm and enhance bonding of terpenoids to iNOS. A SILAC experiment will allow the action of the small molecule on iNOS, eNOS, and nNOS to be confirmed. SAR studies will then be performed to enhance selectivity towards iNOS and improve pharmacological properties. Specific Aim #2: To study the effects of iNOS inhibition

competitively inhibit tyrosinase enzyme at binding site and DHICA (5,6-dihydroxyindole-2-caboxylic acid) and also inhibit melanosome maturation. (21, 24, 25) Arbutin can cause paradoxical hyperpigmentation if high concentration is used.(26, 27) Deoxyarbutin has shown a promising skin lightener.(25) Alpha-arbutin are widely use, 20-fold more potent and stronger inhibitory activity than arbutin.(21, 25) Aloesin Aloesin is a derivative of aloe vera plant.(21) Competitive inhibitor at binding site of tyrosinase

Abstract Glucosylceramide synthase (GCS) is an enzyme that catalyzes the first step in the biosynthesis of glucosylceramide (GlcCer)-related glycosphingolipids (GSLs). In the present report we have used atom-based 3D-QSAR method to analyze the structural aspect on a series of iminosugar derivatives as potent inhibitors of glycosylceramide synthase. In this approach the experimental dataset was divided into training and test sets and the model was chosen based on randomized trial distribution which