Literature summary for 3.1.3.11 extracted from

Balmer, Y.; Stritt-Etter, A.L.; Hirasawa, M.; Jacquot, J.P.; Keryer, E.; Knaff, D.B.; Schurmann, P.
Oxidation-reduction and activation properties of chloroplast fructose 1,6-bisphosphatase with mutated regulatory site (2001), Biochemistry, 40, 15444-15450.

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Activating Compound

Activating Compound	Comment	Organism	Structure
Thioredoxin f	activates wild-type enzyme and mutant C179S	Spinacia oleracea

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Spinacia oleracea

Protein Variants

Protein Variants	Comment	Organism
C155S	lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S	Spinacia oleracea
C174S	lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S	Spinacia oleracea
C179S	mutant significantly decreases the Mg2+ requirement of the oxidized enzyme, mutant is more easily activated by thioredoxin f in comparison to wild-type enzyme	Spinacia oleracea

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Spinacia oleracea	9507	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	the oxidized wild-type enzyme is active only at very high Mg2+ concentrations, the Mg2+ requirement of oxidized and reduced forms of wild-type and mutant enzymes is compared. The reduction of the regulatory disulfide has a positive allosteric effect on the binding of the catalytically essential Mg2+ in the active site.	Spinacia oleracea

Organism

Organism	UniProt	Comment	Textmining
Spinacia oleracea	-	-	-

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Release 2023.1 (January 2023)