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Literature summary extracted from

  • Ye, M.; Zhang, J.J.; Fang, X.; Lawlis, G.B.; Troxell, B.; Zhou, Y.; Gomelsky, M.; Lou, Y.; Yang, X.F.
    DhhP, a cyclic di-AMP phosphodiesterase of Borrelia burgdorferi, is essential for cell growth and virulence (2014), Infect. Immun., 82, 1840-1849 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.59 Ca2+
-
 Borreliella burgdorferi
3.1.4.59 Zn2+
-
 Borreliella burgdorferi

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.59 Mg2+ may substitute for Mn2+ Borreliella burgdorferi
3.1.4.59 Mn2+ maximum activity is observed with Mn2+ as a cofactor Borreliella burgdorferi

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.59 Borreliella burgdorferi O51564
-
-
3.1.4.59 Borreliella burgdorferi DSM 4680 O51564
-
-
3.1.4.60 Borreliella burgdorferi O51564 enzyme is a DHH-DHHA1 domain protein
-
3.1.4.60 Borreliella burgdorferi DSM 4680 O51564 enzyme is a DHH-DHHA1 domain protein
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.59 cyclic di-3',5'-adenylate + H2O
-
 Borreliella burgdorferi 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
 ?
3.1.4.59 cyclic di-3',5'-adenylate + H2O
-
 Borreliella burgdorferi DSM 4680 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.59 additional information PdeA is a DHH-DHHA1 domain protein Borreliella burgdorferi
3.1.4.60 additional information PdeA is a DHH-DHHA1 domain protein Borreliella burgdorferi

Synonyms

EC Number Synonyms Comment Organism
3.1.4.59 BB0619
-
 Borreliella burgdorferi
3.1.4.59 Dhhp
-
 Borreliella burgdorferi
3.1.4.60 BB0619
-
 Borreliella burgdorferi
3.1.4.60 Dhhp
-
 Borreliella burgdorferi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.59 8.5
-
-
 Borreliella burgdorferi

General Information

EC Number General Information Comment Organism
3.1.4.59 physiological function DhhP is essential for Borrelia burgdorferi growth both in vitro and in the mammalian host. The conditional DhhP mutant has a dramatic increase in intracellular c-di-AMP level in comparison to the isogenic wild-type strain. Elevated cellular c-di-AMP in Borrelia burgdorferi does not result in an increased resistance to beta-lactamase antibiotics. The DhhP mutant is defective in induction of the sigmaS factor, RpoS, and the RpoS-dependent outer membrane virulence factor OspC Borreliella burgdorferi
3.1.4.60 physiological function DhhP is essential for Borrelia burgdorferi growth both in vitro and in the mammalian host. The conditional DhhP mutant has a dramatic increase in intracellular c-di-AMP level in comparison to the isogenic wild-type strain. Elevated cellular c-di-AMP in Borrelia burgdorferi does not result in an increased resistance to beta-lactamase antibiotics. The DhhP mutant is defective in induction of the sigmaS factor, RpoS, and the RpoS-dependent outer membrane virulence factor OspC Borreliella burgdorferi