Literature summary for 2.7.7.85 extracted from

Zhu, Y.; Pham, T.H.; Nhiep, T.H.; Vu, N.M.; Marcellin, E.; Chakrabortti, A.; Wang, Y.; Waanders, J.; Lo, R.; Huston, W.M.; Bansal, N.; Nielsen, L.K.; Liang, Z.X.; Turner, M.S.
Cyclic-di-AMP synthesis by the diadenylate cyclase CdaA is modulated by the peptidoglycan biosynthesis enzyme GlmM in Lactococcus lactis (2016), Mol. Microbiol., 99, 1015-1027.

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Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis	-	-	-

Synonyms

Synonyms	Comment	Organism
CdaA	-	Lactococcus lactis

General Information

General Information	Comment	Organism
physiological function	the mutation I154F in phosphoglucosamine mutase gene GlmM results in a lowering of the cyclic di-AMP level and a reduction in the key peptidoglycan precursor UDP-N-acetylglucosamine. Cyclic di-AMP synthesis by CdaA is inhibited by GlmM mutant I154F more than GlmM and GlmM mutant I154F binds more strongly to CdaA than GlmM. Mutations in the cdaA restore osmoresistance in phosphodiesterase gdpP-defective mutants	Lactococcus lactis

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Release 2023.1 (January 2023)