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Literature summary for 2.3.1.8 extracted from

  • Brinsmade, S.R.; Escalante-Semerena, J.C.
    In vivo and in vitro analyses of single-amino acid variants of the Salmonella enterica phosphotransacetylase enzyme provide insights into the function of its N-terminal domain (2007), J. Biol. Chem., 282, 12629-12640.
    View publication on PubMed
Search for more literature for 2.3.1.8

Activating Compound

Activating Compound Comment Organism Structure
NH4Cl maximal stimulation at 40 mM, 3fold Salmonella enterica
NH4Cl 3fold stimulation at 40 mM. No significant increase in activity above 40 mM Salmonella enterica
pyruvate stimulates activity of wild-type enzyme 0.2fold over control, and the activity of the mutant enzyme R252H 3fold over control Salmonella enterica
pyruvate stimulates wild-type activity, its effect is potentiated in the variants, being most pronounced on R252H Salmonella enterica

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Salmonella enterica

Protein Variants

Protein Variants Comment Organism
G273D kcat for reaction with acetyl-CoA and phosphate is 3fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.3fold higher than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme Salmonella enterica
G273D kcat/Km for CoA is 2.2fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 3.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme Salmonella enterica
M294I kcat for reaction with acetyl-CoA and phosphate is 143fold lower than wild-type value, kcat for reaction with CoA and acetyl phosphate is 1.4fold lower than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme Salmonella enterica
M294I kcat/Km for CoA is 1.7fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.2lower higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme Salmonella enterica
R252H kcat for reaction with acetyl-CoA and phosphate is 2.5fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.5fold higher than wild-type value. No inhibition by NADH. Mutant enzyme shows less aggregation than wild type enzyme Salmonella enterica
R252H kcat/Km for CoA is 2.6fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme Salmonella enterica

Inhibitors

Inhibitors Comment Organism Structure
NADH inhibits by changing enzyme conformation, pyruvate counteracts the inhibitory effect of NADH; inhibits by changing the conformation of the enzyme Salmonella enterica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1621
-
 CoA wild-type enzyme Salmonella enterica
0.1621
-
 CoA 37°C, pH 7.5, wild-type enzyme Salmonella enterica
0.163
-
 CoA 37°C, pH 7.5, mutant enzyme R252H Salmonella enterica
0.163
-
 CoA mutant enzyme R252H Salmonella enterica
0.168
-
 CoA 37°C, pH 7.5, mutant enzyme G273D Salmonella enterica
0.1683
-
 CoA mutant enzyme G273D Salmonella enterica
0.192
-
 CoA 37°C, pH 7.5, mutant enzyme M294I Salmonella enterica
0.192
-
 CoA mutant enzyme M294I Salmonella enterica
0.2812
-
 acetyl-CoA 37°C, pH 7.5, mutant enzyme G273D Salmonella enterica
0.2812
-
 acetyl-CoA mutant enzyme G273D Salmonella enterica
0.2814
-
 acetyl-CoA 37°C, pH 7.5, mutant enzyme M294I Salmonella enterica
0.2814
-
 acetyl-CoA mutant enzyme M294I Salmonella enterica
0.3293
-
 acetyl-CoA wild-type enzyme Salmonella enterica
0.3293
-
 acetyl-CoA 37°C, pH 7.5, wild-type enzyme Salmonella enterica
0.5297
-
 acetyl-CoA 37°C, pH 7.5, mutant enzyme R252H Salmonella enterica
0.5297
-
 acetyl-CoA mutant enzyme R252H Salmonella enterica
1.1
-
 phosphate 37°C, pH 7.5, mutant enzyme G273D Salmonella enterica
1.1
-
 phosphate mutant enzyme G273D Salmonella enterica
1.3
-
 phosphate 37°C, pH 7.5, mutant enzyme M294I Salmonella enterica
1.3
-
 phosphate mutant enzyme M294I Salmonella enterica
1.5
-
 phosphate wild-type enzyme Salmonella enterica
1.5
-
 phosphate 37°C, pH 7.5, wild-type enzyme Salmonella enterica
2.8
-
 phosphate 37°C, pH 7.5, mutant enzyme R252H Salmonella enterica
2.8
-
 phosphate mutant enzyme R252H Salmonella enterica

Metals/Ions

Metals/Ions Comment Organism Structure
KCl stimulates Salmonella enterica
KCl stimulates enzyme activity 2.5-fold Salmonella enterica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
490000
-
 gel filtration Salmonella enterica

Organism

Organism UniProt Comment Textmining
Salmonella enterica
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + phosphate
-
 Salmonella enterica CoA + acetyl phosphate
-
 ?
CoA + acetyl phosphate
-
 Salmonella enterica acetyl-CoA + phosphate
-
 r

Subunits

Subunits Comment Organism
hexamer it is possible that native Pta is a dimer of trimers Salmonella enterica
trimer wild-type enzyme is a trimer. Pta variants formmore hexamer than the wild-typ protein Salmonella enterica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.73
-
 acetyl-CoA 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme Salmonella enterica
25
-
 acetyl-CoA 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme Salmonella enterica
57.9
-
 acetyl-CoA 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme Salmonella enterica
57.9
-
 acetyl-CoA mutant enzyme M294I Salmonella enterica
83.1
-
 acetyl-CoA wild-type enzyme Salmonella enterica
208.9
-
 acetyl-CoA mutant enzyme R252H Salmonella enterica
252.5
-
 acetyl-CoA 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme Salmonella enterica
252.5
-
 acetyl-CoA mutant enzyme G273D Salmonella enterica
403
-
 CoA 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme Salmonella enterica
403.5
-
 acetyl phosphate mutant enzyme M294I Salmonella enterica
574.5
-
 acetyl phosphate wild-type enzyme Salmonella enterica
574.5
-
 CoA 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme Salmonella enterica
1301
-
 CoA 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme Salmonella enterica
1301
-
 acetyl phosphate mutant enzyme G273D Salmonella enterica
1480
-
 CoA 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme Salmonella enterica
1480
-
 acetyl phosphate mutant enzyme R252H Salmonella enterica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Salmonella enterica

pH Range

pH Minimum pH Maximum Comment Organism
7 8.5 pH 7.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity Salmonella enterica

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1
-
 NADH wild type enzyme Salmonella enterica
1.1
-
 NADH 37°C, pH 7.5, wild-type enzyme Salmonella enterica