BRENDA - Enzyme Database

Divalent metal activation of beta-methylaspartase. The importance of ionic radius

Bright, H.J.; Biochemistry 6, 1191-1203 (1967)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.1.2
Ca2+
competitive inhibition of Mg2+ activation of the enzyme
Clostridium tetanomorphum
4.3.1.2
Cu2+
-
Clostridium tetanomorphum
4.3.1.2
Sr2+
competitive inhibition of Mg2+ activation of the enzyme
Clostridium tetanomorphum
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.3.1.2
Cd2+
activates
Clostridium tetanomorphum
4.3.1.2
Co2+
activates
Clostridium tetanomorphum
4.3.1.2
Fe2+
activates
Clostridium tetanomorphum
4.3.1.2
K+
-
Clostridium tetanomorphum
4.3.1.2
Mg2+
activates
Clostridium tetanomorphum
4.3.1.2
Mn2+
activates
Clostridium tetanomorphum
4.3.1.2
additional information
ionic radius plays an important part in determing the catalytic efficiency of divalent metal activators
Clostridium tetanomorphum
4.3.1.2
Ni2+
activates
Clostridium tetanomorphum
4.3.1.2
Zn2+
activates
Clostridium tetanomorphum
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.1.2
L-threo-3-methylaspartate
Clostridium tetanomorphum
-
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.1.2
Clostridium tetanomorphum
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
4.3.1.2
L-threo-3-methylaspartate = mesaconate + NH3
mechanism
Clostridium tetanomorphum
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.1.2
L-threo-3-methylaspartate
r
6050
Clostridium tetanomorphum
mesaconate + NH3
-
6050
Clostridium tetanomorphum
-
4.3.1.2
L-threo-3-methylaspartate
-
6050
Clostridium tetanomorphum
?
-
-
-
-
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.1.2
Ca2+
competitive inhibition of Mg2+ activation of the enzyme
Clostridium tetanomorphum
4.3.1.2
Cu2+
-
Clostridium tetanomorphum
4.3.1.2
Sr2+
competitive inhibition of Mg2+ activation of the enzyme
Clostridium tetanomorphum
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.3.1.2
Cd2+
activates
Clostridium tetanomorphum
4.3.1.2
Co2+
activates
Clostridium tetanomorphum
4.3.1.2
Fe2+
activates
Clostridium tetanomorphum
4.3.1.2
K+
-
Clostridium tetanomorphum
4.3.1.2
Mg2+
activates
Clostridium tetanomorphum
4.3.1.2
Mn2+
activates
Clostridium tetanomorphum
4.3.1.2
additional information
ionic radius plays an important part in determing the catalytic efficiency of divalent metal activators
Clostridium tetanomorphum
4.3.1.2
Ni2+
activates
Clostridium tetanomorphum
4.3.1.2
Zn2+
activates
Clostridium tetanomorphum
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.1.2
L-threo-3-methylaspartate
Clostridium tetanomorphum
-
?
-
-
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.1.2
L-threo-3-methylaspartate
r
6050
Clostridium tetanomorphum
mesaconate + NH3
-
6050
Clostridium tetanomorphum
-
4.3.1.2
L-threo-3-methylaspartate
-
6050
Clostridium tetanomorphum
?
-
-
-
-