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Literature summary for 2.7.2.3 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
Search for more literature for 2.7.2.3

Inhibitors

Inhibitors Comment Organism Structure
SO42-
-
 Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1
-
 ATP pH 6.5, 25°C Zymomonas mobilis
1.5
-
 3-phospho-D-glycerate pH 6.5, 25°C Zymomonas mobilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ true substrate is the magnesium complexes of ATP Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
 gel filtration Zymomonas mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Zymomonas mobilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
800
-
 purified enzyme Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-phospho-D-glycerate
-
 Zymomonas mobilis ADP + 1,3-diphosphoglycerate
-
 r

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
ADP
-
 Zymomonas mobilis
ATP true substrate is the magnesium complexes of ATP Zymomonas mobilis
ATP required as phosphate donor Zymomonas mobilis