Inhibitors | Comment | Organism | Structure |
---|---|---|---|
epigallocatechin gallate | - |
Toxoplasma gondii | |
additional information | no inhibition by curcumin | Toxoplasma gondii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0091 | - |
NADP+ | pH 8.8, temperature not specified in the publication | Toxoplasma gondii | |
0.0527 | - |
shikimate | pH 8.8, temperature not specified in the publication | Toxoplasma gondii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
shikimate + NADP+ | Toxoplasma gondii | - |
3-dehydroshikimate + NADPH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Toxoplasma gondii | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
shikimate + NADP+ | - |
Toxoplasma gondii | 3-dehydroshikimate + NADPH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 50000-60000, recombinant enzyme, SDS-PAGE | Toxoplasma gondii |
More | structural modeling of TgSDH suggests that the protein's three large amino acid insertions form surface-exposed loops with alpha-helical character, structure modelling and structure comparisons, overview | Toxoplasma gondii |
Synonyms | Comment | Organism |
---|---|---|
TgSDH | - |
Toxoplasma gondii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.78 | - |
shikimate | pH 8.8, temperature not specified in the publication | Toxoplasma gondii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.8 | - |
assay at | Toxoplasma gondii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | specificity of TgSDH for NADP+ is consistent with the presence of the NRTXXR motif identified in the primary sequence of the protein | Toxoplasma gondii |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0098 | - |
pH 8.8, temperature not specified in the publication | Toxoplasma gondii | epigallocatechin gallate |
General Information | Comment | Organism |
---|---|---|
evolution | a three-dimensional structural model of TgSDH predicts a high level of conservation in the core structure of the enzyme | Toxoplasma gondii |
metabolism | the enzyme is part of the AROM complex, a large pentafunctional polypeptide, which catalyzes steps two through six of the shikimate pathway in fungi. This complex has the following functional domains (from N- to C-terminus): dehydroquinate synthase, 5-enolypyruvylshikimate-3-phosphate synthase, shikimate kinase, dehydroquinate dehydratase, and SDH. These domains catalyze steps 2, 6, 5, 3, and 4 of the pathway, respectively. The first and last enzymes of the fungal shikimate pathway,3-deoxy-D-arabinoheptulosonate 7-phosphate synthase and chorismate synthase, are discrete enzymes | Toxoplasma gondii |
physiological function | Toxoplasma gondii encodes a large pentafunctional polypeptide known as the AROM complex which catalyzes five reactions in the shikimate pathway, a metabolic pathway required for the biosynthesis of the aromatic amino acids and a promising target for anti-parasitic agents. The shikimate dehydrogenase domain (TgSDH) from the Toxoplasma gondii AROM complex catalyzes the NADP+-dependent oxidation of shikimate in the absence of the remaining AROM domains | Toxoplasma gondii |