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Literature summary for 3.1.3.11 extracted from

  • Rodriguez-Suarez, R.J.; Mora-Garcia, S.; Wolosiuk, R.A.
    Characterization of cysteine residues involved in the reductive activation and the structural stability of rapeseed (Brassica napus) chloroplast fructose-1,6-bisphosphatase (1997), Biochem. Biophys. Res. Commun., 232, 388-393.
    View publication on PubMed
Search for more literature for 3.1.3.11

Cloned(Commentary)

Cloned (Comment) Organism
-
 Brassica napus

Protein Variants

Protein Variants Comment Organism
C157S slightly more active than wild type enzyme Brassica napus
C157S/C174S activity remains unchanged Brassica napus
C174S mildly less active than wild type enzyme Brassica napus
C174S/C179S slightly more active than wild type enzyme Brassica napus
C174S/C307S activity remains unchanged Brassica napus
C179S slightly more active than wild type enzyme Brassica napus
C307S activity remains unchanged Brassica napus
C53S mildly less active than wild type enzyme Brassica napus
C53S/C174S mildly less active than wild type enzyme Brassica napus
C96S slightly more active than wild type enzyme Brassica napus

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ wild type and mutant enzyme Brassica napus

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast light enhances the activity of chloroplast enzyme via a cascade of thiol/disulfide exchanges Brassica napus 9507
-
cytoplasm
-
 Brassica napus 5737
-

Organism

Organism UniProt Comment Textmining
Brassica napus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-diphosphate + H2O
-
 Brassica napus D-fructose 6-phosphate + phosphate
-
 ?