Literature summary for 1.18.1.2 extracted from

Thomsen-Ziegler, N.; Pandini, V.; Caprini, G.; aliverti, A.; Cramer, J.; Selzer, P.M.; Zanetti, G.; Seeber, F.
A single in vivo-selected point mutation in the active center of Toxoplasma gondii ferredoxin-NADP+ reductase leads to an inactive enzyme with greatly enhanced affinity for ferredoxin (2004), FEBS Lett., 576, 375-380.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
homology modeling of wild-type and mutant S267R in complex with ferredoxin. Mutant shows major sterical and electrostatical effects on the FAD function as well as on residues Y266, I268 and Y497 neighbouring the mutation	Toxoplasma gondii

Protein Variants

Protein Variants	Comment	Organism
Q242R	catalytic activity similar to wild-type. Protein moves faster than wild-type on SDS-PAGE	Toxoplasma gondii
Q242R/S267R	10fold increase in binding affinity for ferredoxin, 1-4% of wild-type activity.	Toxoplasma gondii
S267R	10fold increase in binding affinity for ferredoxin, 1-4% of wild-type activity	Toxoplasma gondii
S267V	no effect on binding of ferredoxin	Toxoplasma gondii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.035	-	NADPH	both wild-type and mutant Q242R	Toxoplasma gondii

Organism

Organism	UniProt	Comment	Textmining
Toxoplasma gondii	-	-	-

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
470	-	NADPH	wild-type	Toxoplasma gondii
625	-	NADPH	mutant Q242R	Toxoplasma gondii

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Release 2023.1 (January 2023)