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Literature summary for 3.1.4.59 extracted from

  • Manikandan, K.; Sabareesh, V.; Singh, N.; Saigal, K.; Mechold, U.; Sinha, K.
    Two-step synthesis and hydrolysis of cyclic di-AMP in Mycobacterium tuberculosis (2014), PLoS ONE, 9, e86096.
    View publication on PubMed
Search for more literature for 3.1.4.59

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
D130A/H131A mutant fails to hydrolyze c-di-AMP Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Mycobacterium tuberculosis
-
-

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P71615 bifunctional oligoribonuclease and PAP phosphatase, cf. EC 3.1.3.7. Enzyme has a DHH/DHHA1 domain
-
Mycobacterium tuberculosis H37Rv P71615 bifunctional oligoribonuclease and PAP phosphatase, cf. EC 3.1.3.7. Enzyme has a DHH/DHHA1 domain
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclic di-3',5'-adenylate + H2O
-
 Mycobacterium tuberculosis 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
 ?
cyclic di-3',5'-adenylate + H2O
-
 Mycobacterium tuberculosis H37Rv 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
 ?
additional information enzyme has c-di-AMP specific phosphodiesterase activity. It hydrolyzes c-di-AMP to 5'-AMP in two steps. First, it linearizes c-di-AMP into pApA , reaction of EC 3.1.4.59, which is further hydrolyzed to 5'-AMP, reaction of EC 3.1.4.60 Mycobacterium tuberculosis ?
-
 ?
additional information enzyme has c-di-AMP specific phosphodiesterase activity. It hydrolyzes c-di-AMP to 5'-AMP in two steps. First, it linearizes c-di-AMP into pApA , reaction of EC 3.1.4.59, which is further hydrolyzed to 5'-AMP, reaction of EC 3.1.4.60 Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

Synonyms Comment Organism
NrnA
-
 Mycobacterium tuberculosis
Rv2837c
-
 Mycobacterium tuberculosis