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Literature summary for 1.2.1.13 extracted from

  • Mekhalfi, M.; Puppo, C.; Avilan, L.; Lebrun, R.; Mansuelle, P.; Maberly, S.C.; Gontero, B.
    Glyceraldehyde-3-phosphate dehydrogenase is regulated by ferredoxin-NADP reductase in the diatom Asterionella formosa (2014), New Phytol., 203, 414-423 .
    View publication on PubMed
Search for more literature for 1.2.1.13

Activating Compound

Activating Compound Comment Organism Structure
DTT activates Asterionella formosa
NADP+ activates Asterionella formosa

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis Asterionella formosa

Inhibitors

Inhibitors Comment Organism Structure
additional information the activity of the GAPDH-CP12 complex is not affected by addition of bovine serum albumin, Rubisco, EC 4.1.1.39, or phosphoribulokinase, PRK EC 2.7.1.19. Incubation of GAPDH alone with NADPH, DTT or NADP has no effect on its activity Asterionella formosa
NADPH NADPH can inhibit GAPDH in complex with chloroplast protein CP12 in the presence of NADP+ reductase ferredoxin-NADP+ reductase, FNR, EC 1.18.1.1, because FNR is inhibited by NADPH. NADPH can also directly inhibit GAPDH. In crude extracts, glyceraldehyde-3-phosphate dehydrogenase can be inhibited by NADPH under oxidizing conditions. DTT reactivates the enzyme. The addition of commercial FNR from Spinacia oleracea inhibits GAPDH activity by 40% under oxidizing conditions when NADPH is present, and the effect is abolished by the addition of DTT Asterionella formosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
 GAPDH, gel filtration Asterionella formosa
299000
-
 GAPDH–CP12–FNR complex, gel filtration Asterionella formosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NADP+ Asterionella formosa
-
 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 ?
additional information Asterionella formosa the enzyme interacts with small chloroplast protein CP12, and a strong interaction between GAPDH-CP12 and ferredoxin-NADP+ reductase, FNR EC 1.18.1.1, with a very low dissociation constant is observed, protein complex interaction kinetics, overview. The GAPDH-CP12-FNR complex is disrupted with NADP+ ?
-
 ?

Organism

Organism UniProt Comment Textmining
Asterionella formosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
the GAPDH–CP12–FNR complex is purified using ion exchange chromatography and gel filtration, followed by complex dissociation with 20 mM DTT for 20 min at 30°C, and gel filtration to about 86% purity, all steps in presence of NADPH Asterionella formosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 Asterionella formosa 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 ?
additional information the enzyme interacts with small chloroplast protein CP12, and a strong interaction between GAPDH-CP12 and ferredoxin-NADP+ reductase, FNR EC 1.18.1.1, with a very low dissociation constant is observed, protein complex interaction kinetics, overview. The GAPDH-CP12-FNR complex is disrupted with NADP+ Asterionella formosa ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 36700, about, mass spectrometry, 4 * 47000, SDS-PAGE Asterionella formosa

Synonyms

Synonyms Comment Organism
GAPDH
-
 Asterionella formosa

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Asterionella formosa

Expression

Organism Comment Expression
Asterionella formosa downregulation of GAPDH in the dark down

General Information

General Information Comment Organism
metabolism Diatom plastids lack of the oxidative pentose phosphate pathway, and so cannot produce NADPH in the dark. The observed downregulation of GAPDH in the dark may allow NADPH to be rerouted towards other reductive processes contributing to their ecological success Asterionella formosa
physiological function GAPDH has a strategic position within cell metabolism because GAP is an intermediate in many metabolic pathways, and therefore GAPDH needs to be highly regulated. In cyanobacteria, green and red algae and higher plants, GAPDH and phosphoribulokinase (PRK, EC 2.7.1.19) are downregulated by forming a ternary complex with CP12. Regulation of the key Calvin cycle enzymes of diatom algae differs from that of the Plantae. Enzyme GAPDH interacts with ferredoxin-nicotinamide adenine dinucleotide phosphate (NADP) reductase (FNR) from the primary phase of photosynthesis, and the small chloroplast protein, CP12 Asterionella formosa