Literature summary for 3.2.2.5 extracted from

Hsieh, C.; Huang, H.; Hsieh, S.; Zheng, P.; Lin, Y.; Chiang-Ni, C.; Tsai, P.; Wang, S.; Liu, C.; Wu, J.
NAD-glycohydrolase depletes intracellular NAD+ and inhibits acidification of autophagosomes to enhance multiplication of group A Streptococcus in endothelial cells (2018), Front. Microbiol., 9, 1733 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pyogenes serotype M1	Q7DAN2	-	-
Streptococcus pyogenes serotype M49	A0A0H3BX68	-	-
Streptococcus pyogenes serotype M49 NZ131	A0A0H3BX68	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

General Information

General Information	Comment	Organism
physiological function	strains MA49 and A20 have higher activities of NADase and intracellular multiplication than strain M1 in human endothelial cells. NADase activity is required for the intracellular growth of group A Streptococcus in endothelial cells. Intracellular levels of NAD+ and the NAD+/NADH ratio of MA49-infected HMEC-1 cells are both lower than in cells infected by the mutant lacking NADase activity. Only Nga mutant vacuoles are highly colocalized with acidified lysosomes. Intracellular multiplication of the Nga mutant is increased by bafilomycin A1 treatment	Streptococcus pyogenes serotype M49
physiological function	strains MA49 and A20 have higher activities of NADase and intracellular multiplication than strain M1 in human endothelial cells. NADase causes intracellular NAD+ imbalance and impairs acidification of autophagosomes to escape autophagocytic killing and enhance multiplication of group A Streptococci in endothelial cells	Streptococcus pyogenes serotype M1

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Release 2023.1 (January 2023)