Literature summary for 3.1.3.46 extracted from

Furumoto, T.; Teramoto, M.; Inada, N.; Ito, M.; Nishida, I.; Watanabe, A.
Phosphorylation of a bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase, is regulated physiologically and developmentally in rosette leaves of Arabidopsis thaliana (2001), Plant Cell Physiol., 42, 1044-1048.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
92000	-	x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE	Arabidopsis thaliana
96000	-	x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9MB58	bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	phosphorylatiopn of serine and threonine residues, phosphorylation status is regulated physiologically and developmentally	Arabidopsis thaliana

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	rosette leaf	Arabidopsis thaliana	-

Subunits

Subunits	Comment	Organism
?	x * 96000, phosphorylated form, x * 92000, unphosphorylated form, SDS-PAGE	Arabidopsis thaliana

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Release 2023.1 (January 2023)