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Literature summary for 3.6.1.9 extracted from

  • Jaemsen, J.; Baykov, A.A.; Lahti, R.
    Fast kinetics of nucleotide binding to Clostridium perfringens family II pyrophosphatase containing CBS and DRTGG domains (2012), Biochemistry (Moscow), 77, 165-170.
    View publication on PubMed
Search for more literature for 3.6.1.9

Activating Compound

Activating Compound Comment Organism Structure
ATP
-
 Clostridium perfringens
diadenosine polyphosphate APnA with n over 2, no effect by AP4 and AP2A Clostridium perfringens
P1,P3-bis(5'-adenosyl) triphosphate
-
 Clostridium perfringens
P1,P4-bis(5'-adenosyl) tetraphosphate
-
 Clostridium perfringens
P1,P6-bis(5'-adenosyl) hexaphosphate
-
 Clostridium perfringens

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Clostridium perfringens
AMP
-
 Clostridium perfringens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information fast kinetics of nucleotide binding, overview Clostridium perfringens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates only slightly Clostridium perfringens
Co2+ required Clostridium perfringens
Mg2+ required, best cation Clostridium perfringens
additional information effects of different divalent metal ion combinations on the enzyme activity, overview. Mn2+ is not effective in enzyme activation, and diminishes activation by Mg2+ Clostridium perfringens

Organism

Organism UniProt Comment Textmining
Clostridium perfringens
-
-
-

Synonyms

Synonyms Comment Organism
CBS-PPase
-
 Clostridium perfringens
CBS-pyrophosphatase
-
 Clostridium perfringens
family II pyrophosphatase
-
 Clostridium perfringens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Clostridium perfringens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Clostridium perfringens

General Information

General Information Comment Organism
evolution the family II PPase has acquired a pair of nucleotide-binding cystathionine beta-synthase, CBS, domains during evolution, thus endowing the protein with the capacity to be allosterically regulated by adenine nucleotides. Additionally it contains a DRTGG domain between the two CBS domains in the regulatory part, which affords greater flexibility to the regulatory part, allowing it to more rapidly undergo conformational changes in response to binding Clostridium perfringens