Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Activating Compound

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.8 expression in Escherichia coli Salmonella enterica

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.8 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
2.3.1.8 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
2.3.1.8 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
2.3.1.8 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
2.3.1.8 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
2.3.1.8 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

EC Number Inhibitors Comment Organism Structure
2.3.1.8 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.8 0.1621
-
CoA wild-type enzyme Salmonella enterica
2.3.1.8 0.1621
-
CoA 37°C, pH 7.5, wild-type enzyme Salmonella enterica
2.3.1.8 0.163
-
CoA 37°C, pH 7.5, mutant enzyme R252H Salmonella enterica
2.3.1.8 0.163
-
CoA mutant enzyme R252H Salmonella enterica
2.3.1.8 0.168
-
CoA 37°C, pH 7.5, mutant enzyme G273D Salmonella enterica
2.3.1.8 0.1683
-
CoA mutant enzyme G273D Salmonella enterica
2.3.1.8 0.192
-
CoA 37°C, pH 7.5, mutant enzyme M294I Salmonella enterica
2.3.1.8 0.192
-
CoA mutant enzyme M294I Salmonella enterica
2.3.1.8 0.2812
-
acetyl-CoA 37°C, pH 7.5, mutant enzyme G273D Salmonella enterica
2.3.1.8 0.2812
-
acetyl-CoA mutant enzyme G273D Salmonella enterica
2.3.1.8 0.2814
-
acetyl-CoA 37°C, pH 7.5, mutant enzyme M294I Salmonella enterica
2.3.1.8 0.2814
-
acetyl-CoA mutant enzyme M294I Salmonella enterica
2.3.1.8 0.3293
-
acetyl-CoA wild-type enzyme Salmonella enterica
2.3.1.8 0.3293
-
acetyl-CoA 37°C, pH 7.5, wild-type enzyme Salmonella enterica
2.3.1.8 0.5297
-
acetyl-CoA 37°C, pH 7.5, mutant enzyme R252H Salmonella enterica
2.3.1.8 0.5297
-
acetyl-CoA mutant enzyme R252H Salmonella enterica
2.3.1.8 1.1
-
phosphate 37°C, pH 7.5, mutant enzyme G273D Salmonella enterica
2.3.1.8 1.1
-
phosphate mutant enzyme G273D Salmonella enterica
2.3.1.8 1.3
-
phosphate 37°C, pH 7.5, mutant enzyme M294I Salmonella enterica
2.3.1.8 1.3
-
phosphate mutant enzyme M294I Salmonella enterica
2.3.1.8 1.5
-
phosphate wild-type enzyme Salmonella enterica
2.3.1.8 1.5
-
phosphate 37°C, pH 7.5, wild-type enzyme Salmonella enterica
2.3.1.8 2.8
-
phosphate 37°C, pH 7.5, mutant enzyme R252H Salmonella enterica
2.3.1.8 2.8
-
phosphate mutant enzyme R252H Salmonella enterica

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.8 490000
-
gel filtration Salmonella enterica

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.8 Salmonella enterica
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.8 1.73
-
acetyl-CoA 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 25
-
acetyl-CoA 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 57.9
-
acetyl-CoA 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 57.9
-
acetyl-CoA mutant enzyme M294I Salmonella enterica
2.3.1.8 83.1
-
acetyl-CoA wild-type enzyme Salmonella enterica
2.3.1.8 208.9
-
acetyl-CoA mutant enzyme R252H Salmonella enterica
2.3.1.8 252.5
-
acetyl-CoA 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 252.5
-
acetyl-CoA mutant enzyme G273D Salmonella enterica
2.3.1.8 403
-
CoA 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 403.5
-
acetyl phosphate mutant enzyme M294I Salmonella enterica
2.3.1.8 574.5
-
acetyl phosphate wild-type enzyme Salmonella enterica
2.3.1.8 574.5
-
CoA 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 1301
-
CoA 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 1301
-
acetyl phosphate mutant enzyme G273D Salmonella enterica
2.3.1.8 1480
-
CoA 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme Salmonella enterica
2.3.1.8 1480
-
acetyl phosphate mutant enzyme R252H Salmonella enterica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.8 7.5
-
-
Salmonella enterica

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.1.8 7 8.5 pH 7.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity Salmonella enterica

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.8 1.1
-
NADH wild type enzyme Salmonella enterica
2.3.1.8 1.1
-
NADH 37°C, pH 7.5, wild-type enzyme Salmonella enterica