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Literature summary for 3.1.4.59 extracted from

  • Gundlach, J.; Mehne, F.M.; Herzberg, C.; Kampf, J.; Valerius, O.; Kaever, V.; Stuelke, J.
    An essential poison: synthesis and degradation of cyclic di-AMP in Bacillus subtilis (2015), J. Bacteriol., 197, 3265-3274.
    View publication on PubMed
Search for more literature for 3.1.4.59

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P37484
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Bacillus subtilis P46344
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Bacillus subtilis 168 P37484
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Bacillus subtilis 168 P46344
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-

Synonyms

Synonyms Comment Organism
gdpP
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 Bacillus subtilis
PgpH
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 Bacillus subtilis

General Information

General Information Comment Organism
physiological function both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to this accumulation by inactivation of the diadenylate cyclase CdaA Bacillus subtilis
physiological function both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to accumulation by inactivation of the diadenylate cyclase CdaA Bacillus subtilis