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Literature summary extracted from

  • Serrato, A.J.; Romero-Puertas, M.C.; Lazaro-Payo, A.; Sahrawy, M.
    Regulation by S-nitrosylation of the Calvin-Benson cycle fructose-1,6-bisphosphatase in Pisum sativum (2018), Redox Biol., 14, 409-416 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.11 Thioredoxin f the enzyme is redox activated by thioredoxin f through the reduction of a disulphide bridge involving Cys153 and Cys173 Pisum sativum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.11 gene FBP Pisum sativum

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.11 C153S site-directed mutagenesis Pisum sativum
3.1.3.11 C173S/C178S site-directed mutagenesis Pisum sativum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.11 additional information cFBP1 is quite sensitive to higher oxidant concentrations Pisum sativum
3.1.3.11 S-nitrosoglutathione GSNO, the chloroplast FBPase isoform cFBP1 is efficiently S-nitrosylated in vitro. GSNO inhibits the FBPase activity in the mutant C173S/C178S but not in mutant C153S. 0.02 mM GSNO produces a 75% activity inhibition in the mutant C173S/C178S, compared with the nontreated protein, S-nitrosylation of FBPase mutants in the Cys of the redox regulatory domain Pisum sativum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.11
-
 D-fructose 1,6-bisphosphate pH 8.0, 26-27°C, recombinant nontreated mutant C173S/C178S Pisum sativum
3.1.3.11 0.3
-
 D-fructose 1,6-bisphosphate pH 8.0, 26-27°C, recombinant S-nitrosoglutathione-treated mutant C173S/C178S Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.11 chloroplast
-
 Pisum sativum 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.11 Mg2+ required for catalysis Pisum sativum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.11 D-fructose 1,6-bisphosphate + H2O Pisum sativum
-
 D-fructose 6-phosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Pisum sativum P46275
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
3.1.3.11 cFBP1 is quite sensitive to higher oxidant concentrations. Almost complete oxidation 2 h after S-nitrosoglutathione, GSNO, incubation. GSNO incubation leads to the formation of the regulatory disulphide Cys153-Cys173. H2O2 and oxidized glutathione do not lead to enzyme oxidation Pisum sativum

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.11 additional information the Pisum sativum cFBP1 isozyme from chloroplasts can be efficiently S-nitrosylated by S-nitrosoglutathione (GSNO) and S-nitroso-N-acetyl-D,L-penicillamine, triggering the formation of the regulatory disulfide. Cys153 S-nitrosylation induces FBPase oxidation in a GSNO concentration manner Pisum sativum
3.1.3.11 nitrosylation the enzyme (cFBP1) can be efficiently S-nitrosylated by S-nitrosoglutathione and S-nitroso-N-acetyl-D,L-penicillamine, triggering the formation of the regulatory disulphide. S-nitrosylation only occurs during the light period Pisum sativum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.11
-
 Pisum sativum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.11 leaf
-
 Pisum sativum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.11 D-fructose 1,6-bisphosphate + H2O
-
 Pisum sativum D-fructose 6-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.11 homotetramer
-
 Pisum sativum

Synonyms

EC Number Synonyms Comment Organism
3.1.3.11 cFBP1
-
 Pisum sativum
3.1.3.11 cFBP1 Calvin-Benson cycle fructose-1,6-bisphosphatase isoform Pisum sativum
3.1.3.11 Fbp
-
 Pisum sativum
3.1.3.11 FBPase
-
 Pisum sativum
3.1.3.11 fructose-1,6-bisphosphatase
-
 Pisum sativum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.11 26 27 assay at, room temperature Pisum sativum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.11 8
-
 assay at Pisum sativum

General Information

EC Number General Information Comment Organism
3.1.3.11 evolution FBPases are homotetrameric enzymes with three different isoforms present in plants, two in chloroplasts (cFBP1 and cFBP2) and one in the cytosol (cyFBP). Only cFBP1 needs to be redox activated in order to be fully active, whilst cFBP2 is not redox regulated and, despite its activity, resists higher oxidant concentrations than cFBP1 Pisum sativum
3.1.3.11 metabolism fructose-1,6-bisphosphatase (FBPase) is the key enzyme in the Calvin-Benson cycle (CBC). The enzyme is involved in redox regulation in chloroplasts, model of the redox regulation, overview Pisum sativum
3.1.3.11 metabolism the enzyme belongs to the Calvin-Benson cycle Pisum sativum
3.1.3.11 additional information redox pattern displayed by cFBP1, overview Pisum sativum
3.1.3.11 physiological function the Calvin-Benson cycle (CBC) fructose-1,6-bisphosphatase (FBPase) isoform is well known to be redox activated by thioredoxin f through the reduction of a disulfide bridge involving Cys153 and Cys173. cFBP1 needs to be redox activated in order to be fully active Pisum sativum