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Literature summary for 2.7.7.85 extracted from

  • Witte, G.; Hartung, S.; Buettner, K.; Hopfner, K.P.
    Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates (2008), Mol. Cell, 30, 167-178.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis
expression in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallisation of apoenzyme, apoenzyme + ATPgammaS, apoenzyme + cordycepin-triphosphate, determination of the crystal structure at 2.1 A Thermotoga maritima

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Thermotoga maritima

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42700
-
2 * 42700 Thermotoga maritima
42900
-
8 * 42900 Bacillus subtilis
300000
-
gel filtration Bacillus subtilis
353500
-
analytical ultracentrifugation Thermotoga maritima
370000
-
gel filtration Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ATP Thermotoga maritima specific recognition of adenine in the active site pocked. The enzyme signals DNA structures that interfere with chromosome segregation cyclic di-3',5'-adenylate. The enzyme activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions 2 diphosphate + cyclic di-3',5'-adenylate
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P37573
-
-
Thermotoga maritima Q9WY43
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis
-
Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP specific recognition of adenine in the active site pocked. The enzyme signals DNA structures that interfere with chromosome segregation cyclic di-3',5'-adenylate. The enzyme activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions Thermotoga maritima 2 diphosphate + cyclic di-3',5'-adenylate
-
?
2 ATP specific recognition of adenine in the active site pocked. The enzyme does not convert GTP to cyclic di-3',5'-guanylate Thermotoga maritima 2 diphosphate + cyclic di-3',5'-adenylate
-
?

Subunits

Subunits Comment Organism
octamer 2 * 42700 Thermotoga maritima
octamer 8 * 42900 Bacillus subtilis

Synonyms

Synonyms Comment Organism
BsuDisA
-
Bacillus subtilis
TmaDisA
-
Thermotoga maritima

General Information

General Information Comment Organism
physiological function the enzyme signals DNA structures that interfere with chromosome segregation cyclic di-3',5'-adenylate. The enzyme activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions Thermotoga maritima