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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.
    View publication on PubMedView publication on EuropePMC

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