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Literature summary extracted from

  • Peek, J.; Castiglione, G.; Shi, T.; Christendat, D.
    Isolation and molecular characterization of the shikimate dehydrogenase domain from the Toxoplasma gondii AROM complex (2014), Mol. Biochem. Parasitol., 194, 16-19.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.25 epigallocatechin gallate
-
 Toxoplasma gondii
1.1.1.25 additional information no inhibition by curcumin Toxoplasma gondii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.25 0.0091
-
 NADP+ pH 8.8, temperature not specified in the publication Toxoplasma gondii
1.1.1.25 0.0527
-
 shikimate pH 8.8, temperature not specified in the publication Toxoplasma gondii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.25 shikimate + NADP+ Toxoplasma gondii
-
 3-dehydroshikimate + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.25 Toxoplasma gondii
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.25 shikimate + NADP+
-
 Toxoplasma gondii 3-dehydroshikimate + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.25 ? x * 50000-60000, recombinant enzyme, SDS-PAGE Toxoplasma gondii
1.1.1.25 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

EC Number Synonyms Comment Organism
1.1.1.25 TgSDH
-
 Toxoplasma gondii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.25 2.78
-
 shikimate pH 8.8, temperature not specified in the publication Toxoplasma gondii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.25 8.8
-
 assay at Toxoplasma gondii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.25 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

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.1.1.25 0.0098
-
 pH 8.8, temperature not specified in the publication Toxoplasma gondii epigallocatechin gallate

General Information

EC Number General Information Comment Organism
1.1.1.25 evolution a three-dimensional structural model of TgSDH predicts a high level of conservation in the core structure of the enzyme Toxoplasma gondii
1.1.1.25 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
1.1.1.25 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