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Literature summary for 2.3.1.8 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
Search for more literature for 2.3.1.8

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Veillonella parvula
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Veillonella parvula

Reaction

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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