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Literature summary for 2.7.2.3 extracted from

  • Reddy, G.K.; Wendisch, V.F.
    Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production (2014), BMC Microbiol., 14, 54.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.2.3

Activating Compound

Activating Compound Comment Organism Structure
additional information no effects by glycerol-2-phosphate, glycerol-3-phosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1, 6-bisphosphate, phosphoenolpyruvate, pyruvate, acetate, L-lysine, L-alanine, L-glutamate, GTP, and AMP on the enzyme activity Corynebacterium glutamicum

Cloned(Commentary)

Cloned (Comment) Organism
gene pgk, phylogenetic analysis, recombinant expression as soluble N-terminally His-tagged enzyme in Escherichia coli. Gene pgk is overexpressed in L-arginine and L-ornithine production strains and the production increases by 8% and by 17.5%, respectively Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
additional information construction of an enzyme knockout pgkDELTA mutant Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
ADP competitive inhibition, 50% inhibition at 0.1 mM Corynebacterium glutamicum
Ca2+
-
 Corynebacterium glutamicum
Cd2+
-
 Corynebacterium glutamicum
Co2+
-
 Corynebacterium glutamicum
Mn2+
-
 Corynebacterium glutamicum
additional information no effects by glycerol-2-phosphate, glycerol-3-phosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1, 6-bisphosphate, phosphoenolpyruvate, pyruvate, acetate, L-lysine, L-alanine, L-glutamate, GTP, and AMP on the enzyme activity Corynebacterium glutamicum
Ni2+
-
 Corynebacterium glutamicum
Zn2+
-
 Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.11
-
 ATP pH 7.4, 30°C, recombinant enzyme Corynebacterium glutamicum
0.26
-
 3-phospho-D-glycerate pH 7.4, 30°C, recombinant enzyme Corynebacterium glutamicum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, most effective divalent metal ion Corynebacterium glutamicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
 2 * 47000, SDS-PAGE Corynebacterium glutamicum
104000
-
 recombinant His-tagged enzyme, gel filtration Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 3-phospho-D-glycerate Corynebacterium glutamicum
-
 ADP + 3-phospho-D-glyceroyl phosphate
-
 ?
ATP + 3-phospho-D-glycerate Corynebacterium glutamicum ATCC 13032
-
 ADP + 3-phospho-D-glyceroyl phosphate
-
 ?
additional information Corynebacterium glutamicum 3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation ?
-
 ?
additional information Corynebacterium glutamicum ATCC 13032 3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q01655 gene cg1790 or pgk
-
Corynebacterium glutamicum ATCC 13032 Q01655 gene cg1790 or pgk
-

Purification (Commentary)

Purification (Comment) Organism
recombinant soluble His-tagged enzyme from Escherichia coli Corynebacterium glutamicum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
150 220 pH 7.4, 30°C, recombinant His-tagged enzyme Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-phospho-D-glycerate
-
 Corynebacterium glutamicum ADP + 3-phospho-D-glyceroyl phosphate
-
 ?
ATP + 3-phospho-D-glycerate
-
 Corynebacterium glutamicum ATCC 13032 ADP + 3-phospho-D-glyceroyl phosphate
-
 ?
additional information 3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation Corynebacterium glutamicum ?
-
 ?
additional information 3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation Corynebacterium glutamicum ATCC 13032 ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 47000, SDS-PAGE Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
3-phosphoglycerate kinase
-
 Corynebacterium glutamicum
PGK
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50 65 recombinant His-tagged enzyme Corynebacterium glutamicum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 65 enzyme protein precipitation was observed above 65°C Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.4 recombinant His-tagged enzyme Corynebacterium glutamicum

pH Range

pH Minimum pH Maximum Comment Organism
4.5 9.8 10% of PGK activity remaining at pH 4.5 and 33% at pH 8.9, maximal activity at pH 7.0-7.4 Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Corynebacterium glutamicum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.45
-
 Zn2+ pH 7.4, 30°C, recombinant His-tagged enzyme Corynebacterium glutamicum

General Information

General Information Comment Organism
physiological function 3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation. The enzyme is essential for growth of the organism with carbon sources requiring glycolysis and gluconeogenesis, critical role of PGK in Corynebacterium glutamicum