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Literature summary extracted from

  • Pelroy, R.A.; Whiteley, H.R.
    Kinetic properties of phosphotransacetylase from Veillonella alcalescens (1972), J. Bacteriol., 111, 47-55.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.8 acetyl-CoA competitive Veillonella parvula
2.3.1.8 ADP 50% inhibition at 6 mM, MgCl2 reverses inhibition Veillonella parvula
2.3.1.8 ATP 50% inhibition at 1.5 mM, MgCl2 reverses inhibition Veillonella parvula
2.3.1.8 coenzyme A competitive Veillonella parvula

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.8 0.0086
-
acetyl-CoA
-
Veillonella parvula
2.3.1.8 0.33
-
CoA
-
Veillonella parvula
2.3.1.8 0.59
-
acetyl phosphate
-
Veillonella parvula
2.3.1.8 9.3
-
phosphate
-
Veillonella parvula

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.8 acetyl-CoA + phosphate Veillonella parvula
-
CoA + acetyl phosphate
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.8 Veillonella parvula
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.8 partial Veillonella parvula

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.8 acetyl-CoA + phosphate = CoA + acetyl phosphate rapid equilibrium random bi-bi reaction mechanism Veillonella parvula

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.8 additional information
-
-
Veillonella parvula

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.8 acetyl-CoA + phosphate
-
Veillonella parvula CoA + acetyl phosphate
-
r
2.3.1.8 acetyl-CoA + phosphate rate of acetyl-CoA synthesis is 6.5times greater than rate of acetyl phosphate synthesis Veillonella parvula CoA + acetyl phosphate
-
r