Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Zhou, X.; Kay, S.; Toney, M.D.
    Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ions (1998), Biochemistry, 37, 5761-5769.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.64 expression in Escherichia coli Burkholderia cepacia

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.64 1-aminocyclopropane 1-carboxylate
-
Burkholderia cepacia
4.1.1.64 Li+
-
Burkholderia cepacia
4.1.1.64 Na+
-
Burkholderia cepacia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.64 1.12
-
2-aminoisobutanoate enzyme with Na+ in the metal binding site Burkholderia cepacia
4.1.1.64 2
-
2-aminoisobutanoate enzyme with K+ in the metal binding site Burkholderia cepacia
4.1.1.64 8.7
-
2-aminoisobutanoate enzyme with Na+ in the metal binding site Burkholderia cepacia

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.64 K+ activates Burkholderia cepacia
4.1.1.64 K+ the K+-activated enzyme in solution exists in two conformations differing in catalytic competence Burkholderia cepacia
4.1.1.64 additional information hysteretic enzyme whose conformational distribution is controlled by the identity of the alkali metal ion bound near the active site Burkholderia cepacia
4.1.1.64 Rb+ activates Burkholderia cepacia

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.64 2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine cooperativity does not play a role in catalysis or regulation Burkholderia cepacia

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.64 1.29
-
2-aminoisobutanoate enzyme with Na+ in the metal binding site Burkholderia cepacia
4.1.1.64 4.47
-
2-aminoisobutanoate enzyme with Rb+ in the metal binding site Burkholderia cepacia
4.1.1.64 13.1
-
2-aminoisobutanoate enzyme with K+ in the metal binding site Burkholderia cepacia

Cofactor

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