Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a potential target for antimalarial drug development and chemotherapy | Plasmodium falciparum |
Protein Variants | Comment | Organism |
---|---|---|
H219Q | site-directed mutagenesis, the mutation decreased the affinity toward the substrate 1-deoxy-D-xylulose 5-phosphate with an 8-fold increase in the Km compared to the wild-type enzyme | Plasmodium falciparum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
fosmidomycin | a natural antibiotic from Streptomyces lavendulae, a specific, mixed type inhibitor, the N-formyl-N-hydroxy amino headgroup of fosmidomycin coordinates Mg2+ ion forming an octahedral complex with active site residues Asp157, Glu159, and Glu241 and a critical binding site water molecule, residue His219 is essential for placing fosmidomycin in the active site for optimal catalysis, mechanism, overview, NADPH has a vital role in tight binding of the inhibitor within the enzyme active site | Plasmodium falciparum | |
FR900098 | - |
Plasmodium falciparum | |
additional information | design and development of inhibitors, structure and docking modeling, overview | Plasmodium falciparum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the enzyme requires divalent metal ions | Plasmodium falciparum | |
Mn2+ | the enzyme requires divalent metal ions | Plasmodium falciparum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-deoxy-D-xylulose 5-phosphate + NADPH + H+ | Plasmodium falciparum | second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate, overview | 2-C-methyl-D-erythritol 4-phosphate + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | O96693 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+ | highly conserved active site structure, active site residues Asp157, Glu159, and Glu241, residue His219 is essential for placing the substrate in the active site for optimal catalysis | Plasmodium falciparum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-deoxy-D-xylulose 5-phosphate + NADPH + H+ | - |
Plasmodium falciparum | 2-C-methyl-D-erythritol 4-phosphate + NADP+ | - |
? | |
1-deoxy-D-xylulose 5-phosphate + NADPH + H+ | second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate, overview | Plasmodium falciparum | 2-C-methyl-D-erythritol 4-phosphate + NADP+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | detailed three-dimensional modeling and analysis of structure-function relationship, comparative modeling through multiple alignment followed by intensive optimization, minimization, and validation, the three-dimensional structure shows monomeric subunit consisting of three domains: an N-terminal NADPH binding domain, a connective or linker domain, with most of the active site residues located in this domain, and a C-terminal domain | Plasmodium falciparum |
Synonyms | Comment | Organism |
---|---|---|
DXR | - |
Plasmodium falciparum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | NADPH has a vital role in tight binding of the inhibitor fosmidomycin within the enzyme active site | Plasmodium falciparum |