Nicotinamide Adenine DinucleotidPhosphate
Nicotinamide adenine dinucleotide phosphate is a coenzyme form of vitamin niacin. The enzyme also known as NADP is needed for many biochemical reactions to take place. Protein catalysts including trypsin and lysozyme catalyze different reactions by themselves. However, many other catalysts require metal ions as well as ribonucleic acid to carry out a reaction.
Niacin is a component of nicotinamide adenine dinucleotide phosphate and NAD. These enzymes are very crucial in catabolism, and in the production of energy as well as biosynthesis of sugars and fats.
Nicotinamide adenine dinucleotide phosphate is therefore very important and plays a crucial role in ensuring that biochemical reactions take place. Redox reactions for instance cannot take place without NADP. This is a reaction in which oxidoreductase enzymes transfer hydrogen.
Redox reaction is catalyzed by nicotinamide adenine dinucleotide phosphate or the oxidoreducrase enzyme. During the process, two electrons and two hydrogens are removed from an ethanol molecule. A hydrogen atom and two electrons will then be transferred to generate an active NADP+.
Enzymes that require NADP to carry out different reactions
- Alcohol dehydrogenase requires NADP to metabolize alcohol
- Glyceraldehyde phosphate dehydrogenase needs NADP to catalyze an important step in glycolysis
- Lactate dehydrogenase also requires NADP to catalyze reactions in liver and muscle cells
- Pyruvate dehydrogenase needs NADP to catalyze any reaction connecting to glycolysis to the Krebs cycle
- a-keto-glutatarate dehydrogenase, malate dehydrogenase and isocitrate dehydrogenase also require NADP to catalyze oxidative phosphorylation reactions
- Hydroxyl-acyl-sCoA dehydrogenase needs NADP to catalyze oxidative phosphorylation reactions
- Glucose 6-phosphate dehydrogenase is also needed to catalyze reactions in pentose phosphate pathway, in the Calvin cycle and in fatty acid synthesis.
Additionally, biosynthetic and energy producing functions of Glucose 6-phosphate dehydrogenase also come in handy. The enzyme act as an electron acceptor in oxidoreductase catalyzed reactions. It acts as an electron donor to ensure successful reactions in different cycles and metabolic processes.
Glucose 6-phosphate dehydrogenase can also act as a side enzyme in different reactions. This depends on the side of NAD molecule that the enzyme acts on. For instance alcohol dehydrogenase catalyzes an alcoholic reaction. NADP therefore acts as a side enzyme by ensuring sufficient transfer of hydrogen from ethanol and to the position that is required to produce quality alcohol.
Similarly, nicotinamide group can be used with dehydrogenase enzyme unexpectedly to complete a catalytic reaction. It is also important to note that NADP has a very distinctive signal in ultra-violet spectroscopy. The enzyme is used by scientists to monitor a wide range of enzyme catalyzed reactions.
Who established Glucose 6-phosphate dehydrogenase?
Glucose 6-phosphate dehydrogenase is an enzyme that has been proven to be very important in a wide range of metabolic reactions. This is an enzyme that was first established by Hans von Euler. He was the first to realize the structure of the enzyme. In 1929, Hans shared a Nobel Prize with Arthur Harden in medicine and in physiology for the discovery of the enzyme as well as NAD.
Later on, Euler proved that NAD contains two phosphate groups including one adenine, one nicotinamide unit and ribose sugar. These are important compounds that offer a positive charge on the enzyme and nitrogen atoms in different reactions.
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