Related Experiment Video
Updated: Sep 11, 2026

Using Fluorescent Proteins to Monitor Glycosome Dynamics in the African Trypanosome
Published on: August 19, 2014
Purification and properties of glucose-6-phosphate dehydrogenase from Leishmania tropical promastigotes
Abstract:
Glucose-6-phosphate dehydrogenase specific for NADP (EC 1.1.1.49) was purified to homogeneity from Leishmania tropica promastigotes. The enzyme was found to exist as dimer. The molecular weight of the native enzyme was determined to be 110 000, that of the subunit to be 55 000. The occurence of isoenzymes was demonstrated by isoelectrofocusing. Isoelectric points of glucose-6-phosphate dehydrogenase activity were found at pH 5.5 and pH 6.8. The isoenzymes do not differ with respect to Michaelis constants. The Km-values for NADP and glucose-6-phosphate were determined to be 0.012 mM and 0.15 mM respectively. Glucose-6-phosphate dehydrogenase activity was found to be regulated by product inhibition. The inhibition constant for NADPH was calculated to be 0.05 mM.
Related Concept Videos
What is Glycolysis?
Cells make energy by breaking down macromolecules. Cellular respiration is the biochemical process that converts "food energy" (from the chemical bonds of macromolecules) into chemical energy in the form of adenosine triphosphate (ATP). The first step of this tightly regulated and intricate process is glycolysis. The word glycolysis originates from the Latin glyco (sugar) and lysis (breakdown). Glycolysis serves two main intracellular functions: generating ATP and generating...
Energy-requiring Steps of Glycolysis
Glycolysis: Preparatory Phase
Biosynthesis of Polysaccharides
Leishmaniasis
Antiprotozoal Agents

