BRENDA - Enzyme Database

Fast kinetics of nucleotide binding to Clostridium perfringens family II pyrophosphatase containing CBS and DRTGG domains

Jaemsen, J.; Baykov, A.A.; Lahti, R.; Biochemistry (Moscow) 77, 165-170 (2012)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
3.6.1.9
ATP
-
Clostridium perfringens
3.6.1.9
diadenosine polyphosphate
APnA with n over 2, no effect by AP4 and AP2A
Clostridium perfringens
3.6.1.9
P1,P3-bis(5'-adenosyl) triphosphate
-
Clostridium perfringens
3.6.1.9
P1,P4-bis(5'-adenosyl) tetraphosphate
-
Clostridium perfringens
3.6.1.9
P1,P6-bis(5'-adenosyl) hexaphosphate
-
Clostridium perfringens
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.6.1.9
ADP
-
Clostridium perfringens
3.6.1.9
AMP
-
Clostridium perfringens
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.6.1.9
additional information
-
additional information
fast kinetics of nucleotide binding, overview
Clostridium perfringens
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.6.1.9
Ca2+
activates only slightly
Clostridium perfringens
3.6.1.9
Co2+
required
Clostridium perfringens
3.6.1.9
Mg2+
required, best cation
Clostridium perfringens
3.6.1.9
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.6.1.9
Clostridium perfringens
-
-
-
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.6.1.9
25
-
assay at
Clostridium perfringens
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.6.1.9
7.2
-
assay at
Clostridium perfringens
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
3.6.1.9
ATP
-
Clostridium perfringens
3.6.1.9
diadenosine polyphosphate
APnA with n over 2, no effect by AP4 and AP2A
Clostridium perfringens
3.6.1.9
P1,P3-bis(5'-adenosyl) triphosphate
-
Clostridium perfringens
3.6.1.9
P1,P4-bis(5'-adenosyl) tetraphosphate
-
Clostridium perfringens
3.6.1.9
P1,P6-bis(5'-adenosyl) hexaphosphate
-
Clostridium perfringens
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.6.1.9
ADP
-
Clostridium perfringens
3.6.1.9
AMP
-
Clostridium perfringens
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.6.1.9
additional information
-
additional information
fast kinetics of nucleotide binding, overview
Clostridium perfringens
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.6.1.9
Ca2+
activates only slightly
Clostridium perfringens
3.6.1.9
Co2+
required
Clostridium perfringens
3.6.1.9
Mg2+
required, best cation
Clostridium perfringens
3.6.1.9
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
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.6.1.9
25
-
assay at
Clostridium perfringens
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.6.1.9
7.2
-
assay at
Clostridium perfringens
General Information
EC Number
General Information
Commentary
Organism
3.6.1.9
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
General Information (protein specific)
EC Number
General Information
Commentary
Organism
3.6.1.9
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