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Literature summary 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

EC Number Inhibitors Comment Organism Structure
2.3.1.8 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
2.3.1.8 desulfo-CoA competitive inhibitor with respect to CoA, noncompetitive inhibitor with respect to acetyl phosphate Methanosarcina thermophila
2.3.1.8 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.8 0.065
-
CoA 25°C, pH 7.2 Methanosarcina thermophila
2.3.1.8 0.096
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila
2.3.1.8 0.186
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila
2.3.1.8 0.742
-
phosphate 25°C, pH 7.2 Methanosarcina thermophila

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.8 71000
-
dynamic light scattering Methanosarcina thermophila

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.8 Methanosarcina thermophila
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.8 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.8 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

EC Number Subunits Comment Organism
2.3.1.8 dimer dynamic light scattering Methanosarcina thermophila

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.8 1500
-
phosphate 25°C, pH 7.2 Methanosarcina thermophila
2.3.1.8 1500
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila
2.3.1.8 5190
-
CoA 25°C, pH 7.2 Methanosarcina thermophila
2.3.1.8 5190
-
acetyl phosphate 25°C, pH 7.2 Methanosarcina thermophila

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.8 0.0013
-
desulfo-CoA 25°C, pH 7.2, with respect to CoA Methanosarcina thermophila
2.3.1.8 0.0028
-
desulfo-CoA 25°C, pH 7.2, with respect to acetyl phosphate Methanosarcina thermophila