Literature summary extracted from
Mutschler, H.; Reinstein, J.; Meinhart, A.
Assembly dynamics and stability of the pneumococcal epsilon zeta antitoxin toxin (PezAT) system from Streptococcus pneumoniae (2010), J. Biol. Chem., 285, 21797-21806.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.7.1.176 |
additional information |
PezAT activation of toxin by antitoxin displacement |
Streptococcus pneumoniae |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.1.176 |
expression of His-tagged wild-type and mutant enzymes with or without PezA in Escherichia coli strain BL21(DE3) |
Streptococcus pneumoniae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.1.176 |
D66T |
site-directed mutagenesis, a nontoxicPezT variant |
Streptococcus pneumoniae |
2.7.1.176 |
D66T/W232Y |
site-directed mutagenesis, a mutated tryptophan-free PezT variant |
Streptococcus pneumoniae |
General Stability
EC Number |
General Stability |
Organism |
---|
2.7.1.176 |
overall stability of the chromosomally encoded PezAT TA system, overview. High affinity of PezAT and the resulting stabilization of PezA upon complex formation with PezT seem to impair toxin release by simple dissociation |
Streptococcus pneumoniae |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.1.176 |
additional information |
neutralization of the bacteriotoxic protein PezT is carried out by complex formation with its cognate antitoxin PezA, proteolytic resistance of PezA once bound to PezT |
Streptococcus pneumoniae |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
2.7.1.176 |
additional information |
- |
additional information |
association and dissociation kinetics of the PezAT complex, with wild-type and mutant D66T PezT, stopped-flow measurements, femtomolar affinity of PezA and PezT, detailed kinetic analysis of the PezAT interaction determined using rapid mixing methods and time-resolved size exclusion chromatography, overview |
Streptococcus pneumoniae |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.1.176 |
additional information |
Streptococcus pneumoniae |
neutralization of the bacteriotoxic protein PezT is carried out by complex formation with its cognate antitoxin PezA, proteolytic resistance of PezA once bound to PezT |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.1.176 |
Streptococcus pneumoniae |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.1.176 |
recombinant His-tagged wild-type and mutant enzymes with or without PezA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography |
Streptococcus pneumoniae |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.1.176 |
additional information |
neutralization of the bacteriotoxic protein PezT is carried out by complex formation with its cognate antitoxin PezA, proteolytic resistance of PezA once bound to PezT |
Streptococcus pneumoniae |
? |
- |
? |
|
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.7.1.176 |
25 |
- |
assay at |
Streptococcus pneumoniae |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.1.176 |
malfunction |
PezT inhibition renders the host-cell capable to actively control toxin release |
Streptococcus pneumoniae |
2.7.1.176 |
additional information |
the pneumococcal chromosomally encoded, class II epsilon zeta antitoxin toxin, PezAT, system is a chromosomally encoded, class II toxin antitoxin system from the human pathogen, assembly and dynamics of the epsilon zeta antitoxin toxin, PezAT association is electrostatically enhanced, overview. Proteolytic removal of the transcriptional repressor domain of PezA, because the C-terminal domains binds to PezT with comparable affinity as full-length protein |
Streptococcus pneumoniae |