Literature summary for 3.2.2.5 extracted from

Velarde, J.; O'Seaghdha, M.; Baddal, B.; Bastiat-Sempe, B.; Wessels, M.
Binding of NAD+-glycohydrolase to streptolysin O stabilizes both toxins and promotes virulence of group A Streptococcus (2017), mBio, 8, e01382 .

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Organism

Organism	UniProt	Comment	Textmining
Streptococcus pyogenes serotype M1	Q7DAN2	-	-

General Information

General Information	Comment	Organism
physiological function	expression of NADase, either enzymatically active or inactive, augments streptolysin SLO-mediated toxicity for keratinocytes. In culture supernatants, SLO and NADase are mutually interdependent for protein stability. Presence of SLO protects NADase from proteolytic cleavage of its translocation domain. The two proteins interact in solution with 1:1 stoichiometry and both the translocation domain and catalytic domain of NADase are required for maximal binding between the two toxins	Streptococcus pyogenes serotype M1

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Release 2023.1 (January 2023)