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Literature summary extracted from

  • Morisse, S.; Michelet, L.; Bedhomme, M.; Marchand, C.H.; Calvaresi, M.; Trost, P.; Fermani, S.; Zaffagnini, M.; Lemaire, S.D.
    Thioredoxin-dependent redox regulation of chloroplastic phosphoglycerate kinase from Chlamydomonas reinhardtii (2014), J. Biol. Chem., 289, 30012-30024.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.2.3 additional information the oxidized CrPGK1 retains 25% of its maximal activity and is fully activated by reducing treatments, leading to a 4fold activation Chlamydomonas reinhardtii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.3 gene PGK1, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3) Chlamydomonas reinhardtii

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.3 C108S site-directed mutagenesis, the mutant enzyme is almost completely inactive under oxidizing conditions (DTTox), but is strongly reactivated in the presence of DTTred, suggesting that the absence of Cys108 does not alter the sensitivity of the protein to the redox environment Chlamydomonas reinhardtii
2.7.2.3 C227S site-directed mutagenesis, the mutant is contitutively active and is totally insensitive to oxidizing treatments, and no variation of protein activity is observed after incubation with DTTred. Absence of Cys227 allows the mutant proteins to maintain a fully active conformation comparable with the reduced wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 C361S site-directed mutagenesis, the mutant is contitutively active and is totally insensitive to oxidizing treatments, and no variation of protein activity is observed after incubation with DTTred. Absence of Cys361 allows the mutant proteins to maintain a fully active conformation comparable with the reduced wild-type enzyme Chlamydomonas reinhardtii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.3 additional information PGK1 activity is inhibited by the formation of a single regulatory disulfide bond Cys227-Cys361 with a low midpoint redox potential Chlamydomonas reinhardtii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.3 additional information
-
 additional information Michaelis-Menten kinetics, kinetic analysis or CrPGK1, overview Chlamydomonas reinhardtii
2.7.2.3 0.31
-
 ATP pH 7.9, 25°C, recombinant oxidized wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 0.35
-
 3-phospho-D-glycerate pH 7.9, 25°C, recombinant oxidized wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 0.37
-
 3-phospho-D-glycerate pH 7.9, 25°C, recombinant reduced wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 0.4
-
 ATP pH 7.9, 25°C, recombinant reduced wild-type enzyme Chlamydomonas reinhardtii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.2.3 chloroplast
-
 Chlamydomonas reinhardtii 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.3 Mg2+ essentially required Chlamydomonas reinhardtii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.3 45000
-
-
 Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.2.3 ATP + 3-phospho-D-glycerate Chlamydomonas reinhardtii
-
 ADP + 3-phospho-D-glyceroyl phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.3 Chlamydomonas reinhardtii A8JC04
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
2.7.2.3 the oxidized CrPGK1 retains 25% of its maximal activity and is fully activated by reducing treatments, leading to a 4fold activation Chlamydomonas reinhardtii

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.3 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Chlamydomonas reinhardtii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.3 ATP + 3-phospho-D-glycerate
-
 Chlamydomonas reinhardtii ADP + 3-phospho-D-glyceroyl phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.2.3 monomer 1 * 45000, oxidized enzyme form, SDS-PAGE Chlamydomonas reinhardtii
2.7.2.3 More CrPGK1 is a monomeric enzyme with two distinct domains, wild-type and mutant enzyme structures by dynamic light scattering. Peptide mass fingerprinting of CrPGK1-WT and CrPGK1-C227Smutant after trypsin digestion, overview Chlamydomonas reinhardtii

Synonyms

EC Number Synonyms Comment Organism
2.7.2.3 PGK1
-
 Chlamydomonas reinhardtii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.3 25
-
 assay at Chlamydomonas reinhardtii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.2.3 28.5
-
 ATP pH 7.9, 25°C, recombinant oxidized wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 28.5
-
 3-phospho-D-glycerate pH 7.9, 25°C, recombinant oxidized wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 83.4
-
 ATP pH 7.9, 25°C, recombinant reduced wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 84.7
-
 3-phospho-D-glycerate pH 7.9, 25°C, recombinant reduced wild-type enzyme Chlamydomonas reinhardtii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.3 7.9
-
 assay at Chlamydomonas reinhardtii

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.2.3 ATP
-
 Chlamydomonas reinhardtii

General Information

EC Number General Information Comment Organism
2.7.2.3 metabolism PGK1 is a potentially light-modulated Calvin-Benson cycle enzyme Chlamydomonas reinhardtii
2.7.2.3 additional information three-dimensional enzyme structure modeling and molecular dynamics, overview Chlamydomonas reinhardtii
2.7.2.3 physiological function thioredoxin-dependent redox regulation of chloroplastic phosphoglycerate kinase via oxidoreduction of the Cys227-Cys361 disulfide bond. Based on molecular mechanics calculation, the formation of the disulfide is proposed to impose structural constraints in the C-terminal domain of the enzyme that may lower its catalytic efficiency Chlamydomonas reinhardtii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.2.3 81.4
-
 3-phospho-D-glycerate pH 7.9, 25°C, recombinant oxidized wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 91.9
-
 ATP pH 7.9, 25°C, recombinant oxidized wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 208.5
-
 ATP pH 7.9, 25°C, recombinant reduced wild-type enzyme Chlamydomonas reinhardtii
2.7.2.3 229
-
 3-phospho-D-glycerate pH 7.9, 25°C, recombinant reduced wild-type enzyme Chlamydomonas reinhardtii