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Literature summary for 2.3.1.8 extracted from

  • Lawrence, S.H.; Ferry, J.G.
    Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila (2006), J. Bacteriol., 188, 1155-1158.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
acetyl-CoA competitive inhibitor versus CoA when acetyl phosphate is at subsaturating levels but it does not inhibit versus CoA when acetyl phosphate is at saturating levels. Acetyl-CoA is a competitive inhibitor versus acetyl phosphate when CoA is at subsaturating levels but it does not inhibit versus acetyl phosphate when CoA is at saturating levels Methanosarcina thermophila
desulfo-CoA competitive inhibitor with respect to CoA, noncompetitive inhibitor with respect to acetyl phosphate Methanosarcina thermophila
phosphate competitive inhibitor versus acetyl phosphate when CoA is at saturating or subsaturating levels. Phosphate is a noncompetitive inhibitor versus CoA when acetyl phosphate is at a subsaturating level (0.15 mM), but it does not inhibit versus CoA when acetyl phosphate is at a saturating level (4 mM) Methanosarcina thermophila

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.065
-
CoA 25°C, pH 7.2 Methanosarcina thermophila
0.096
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila
0.186
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila
0.742
-
phosphate 25°C, pH 7.2 Methanosarcina thermophila

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
71000
-
dynamic light scattering Methanosarcina thermophila

Organism

Organism UniProt Comment Textmining
Methanosarcina thermophila
-
-
-

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + phosphate = CoA + acetyl phosphate ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order Methanosarcina thermophila

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-phosphate + CoA ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order Methanosarcina thermophila acetyl-CoA + phosphate
-
r

Subunits

Subunits Comment Organism
dimer dynamic light scattering Methanosarcina thermophila

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1500
-
phosphate 25°C, pH 7.2 Methanosarcina thermophila
1500
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila
5190
-
CoA 25°C, pH 7.2 Methanosarcina thermophila
5190
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0013
-
desulfo-CoA 25°C, pH 7.2, with respect to CoA Methanosarcina thermophila
0.0028
-
desulfo-CoA 25°C, pH 7.2, with respect to acetyl phosphate Methanosarcina thermophila