Literature summary for 1.1.1.25 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.

Search for more literature for 1.1.1.25

Inhibitors

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

KM Value [mM]

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/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Toxoplasma gondii	-	-	-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms	Comment	Organism
TgSDH	-	Toxoplasma gondii

Turnover Number [1/s]

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

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

Cofactor

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

General Information

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

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Release 2023.1 (January 2023)