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Literature summary for 2.7.1.176 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
Search for more literature for 2.7.1.176

Activating Compound

Activating Compound Comment Organism Structure
additional information PezAT activation of toxin by antitoxin displacement Streptococcus pneumoniae

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes with or without PezA in Escherichia coli strain BL21(DE3) Streptococcus pneumoniae

Protein Variants

Protein Variants Comment Organism
D66T site-directed mutagenesis, a nontoxicPezT variant Streptococcus pneumoniae
D66T/W232Y site-directed mutagenesis, a mutated tryptophan-free PezT variant Streptococcus pneumoniae

General Stability

General Stability Organism
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

Inhibitors Comment Organism Structure
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Streptococcus pneumoniae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Streptococcus pneumoniae

General Information

General Information Comment Organism
malfunction PezT inhibition renders the host-cell capable to actively control toxin release Streptococcus pneumoniae
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