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Literature summary for 2.7.1.40 extracted from

  • Pawluk, A.; Scopes, R.K.; Griffiths-Smith, K.
    Isolation and properties of the glycolytic enzymes from Zymomonas mobilis. The five enzymes from glyceraldehyde-3-phosphate dehydrogenase through to pyruvate kinase (1986), Biochem. J., 238, 275-281.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
D-fructose 1,6-diphosphate not Zymomonas mobilis
D-glucose 6-phosphate not Zymomonas mobilis
additional information no activation by 6-phosphogluconate Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.16 0.17 ADP pH 6.5, 25°C Zymomonas mobilis

Metals/Ions

Metals/Ions Comment Organism Structure
K+ not Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
2 * 57000, SDS-PAGE Zymomonas mobilis
115000
-
gel filtration Zymomonas mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
affinity chromatography Zymomonas mobilis

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Zymomonas mobilis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
280
-
-
Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate no allosteric activation Zymomonas mobilis ATP + pyruvate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 57000, SDS-PAGE Zymomonas mobilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Zymomonas mobilis