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Literature summary extracted from

  • Liu, W.; Toney, M.D.
    Kinetic and thermodynamic analysis of the interaction of cations with dialkylglycine decarboxylase (2004), Biochemistry, 43, 4998-5010.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.64 2
-
 2-aminoisobutanoate activated by K+ Burkholderia cepacia
4.1.1.64 2.2
-
 2-aminoisobutanoate activated by Rb+ Burkholderia cepacia
4.1.1.64 4.4
-
 2-aminoisobutanoate activated by NH4+ Burkholderia cepacia
4.1.1.64 5.8
-
 2-aminoisobutanoate activated by Mg2+ Burkholderia cepacia
4.1.1.64 6.6
-
 2-aminoisobutanoate activated by Tl+ Burkholderia cepacia
4.1.1.64 7.3
-
 2-aminoisobutanoate activated by Cs+ Burkholderia cepacia
4.1.1.64 11
-
 2-aminoisobutanoate activated by Li+ Burkholderia cepacia
4.1.1.64 13
-
 2-aminoisobutanoate activated by Na+ Burkholderia cepacia
4.1.1.64 18
-
 2-aminoisobutanoate activated by Ca2+ Burkholderia cepacia
4.1.1.64 66
-
 2-aminoisobutanoate activated by Ba2+ Burkholderia cepacia

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.64 Ba2+ gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate Burkholderia cepacia
4.1.1.64 Ca2+ gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius Burkholderia cepacia
4.1.1.64 Cs+ activates to a lesser extent than K+ Burkholderia cepacia
4.1.1.64 K+ activity is dependent on cations. K+ is the monovalent cation with the optimal size for catalytic activity, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate Burkholderia cepacia
4.1.1.64 Li+ activates to a lesser extent than K+ Burkholderia cepacia
4.1.1.64 Mg2+ gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius Burkholderia cepacia
4.1.1.64 Na+ activates to a lesser extent than K+, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate Burkholderia cepacia
4.1.1.64 NH4+ activates to a lesser extent than K+ Burkholderia cepacia
4.1.1.64 Rb+ activates to a lesser extent than K+ Burkholderia cepacia
4.1.1.64 Tl+ activates to a lesser extent than K+ Burkholderia cepacia

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.64 Burkholderia cepacia
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.64 2-Aminoisobutanoate + pyruvate
-
 Burkholderia cepacia L-Ala + acetone + CO2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.64 0.05
-
 2-aminoisobutanoate activated by Ca2+ Burkholderia cepacia
4.1.1.64 0.076
-
 2-aminoisobutanoate activated by Mg2+ Burkholderia cepacia
4.1.1.64 0.86
-
 2-aminoisobutanoate activated by Li+ Burkholderia cepacia
4.1.1.64 1.4
-
 2-aminoisobutanoate activated by Ba2+ Burkholderia cepacia
4.1.1.64 1.83
-
 2-aminoisobutanoate activated by Na+ Burkholderia cepacia
4.1.1.64 3.8
-
 2-aminoisobutanoate activated by Cs+ Burkholderia cepacia
4.1.1.64 4.9
-
 2-aminoisobutanoate activated by NH4+ Burkholderia cepacia
4.1.1.64 5.22
-
 2-aminoisobutanoate activated by Tl+ Burkholderia cepacia
4.1.1.64 7.4
-
 2-aminoisobutanoate activated by Rb+ Burkholderia cepacia
4.1.1.64 10.4
-
 2-aminoisobutanoate activated by K+ Burkholderia cepacia

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.64 pyridoxal 5'-phosphate dependent on Burkholderia cepacia