Abstract
Cryptosporidium parvum is one of several Cryptosporidium spp. that cause the parasitic infection cryptosporidiosis. Cryptosporidiosis is a diarrheal infection that is spread via the fecal-oral route and is commonly caused by contaminated drinking water. Triosephosphate isomerase is an enzyme that is ubiquitous to all organisms that perform glycolysis. Triosephosphate isomerase catalyzes the formation of glyceraldehyde 3-phosphate from dihydroxyacetone phosphate, which is a critical step to ensure the maximum ATP production per glucose molecule. In this paper, the 1.55 Å resolution crystal structure of the open-loop form of triosephosphate isomerase from C. parvum Iowa II is presented. An unidentified electron density was found in the active site.
Highlights
Triosephosphate isomerase (TIM) is an enzyme that is only active in its dimeric form and that has been found in almost all organisms that participate in glycolysis
The aldolase step of glycolysis ends with two products: dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP)
During the fifth glycolysis step, TIM catalyzes the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde 3-phosphate (GAP)
Summary
Triosephosphate isomerase (TIM) is an enzyme that is only active in its dimeric form and that has been found in almost all organisms that participate in glycolysis. The aldolase (fourth) step of glycolysis ends with two products: dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (GAP). GAP is able to proceed to the phase of glycolysis. During the fifth glycolysis step, TIM catalyzes the reversible isomerization of dihydroxyacetone phosphate (DHAP) to d-glyceraldehyde 3-phosphate (GAP) (see Fig. 1). TIM is essential for maximum energy production. Because of its important role in glycolysis, triosephosphate isomerase has been described as an ‘an attractive target for drug design against parasites’ (Mande et al, 1994)
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