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Literature summary extracted from

  • Hohenester, E.; Keller, J.W.; Jansonius, J.N.
    An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase (1994), Biochemistry, 33, 13561-13570.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.64 crystal structure at 2.8 A resolution of tzhe enzyme with Li+ or Rb+ bound Burkholderia cepacia
4.1.1.64 crystal structures at 2.8 A resolution with Li+ and Rb+ bound at the binding site for alkali metal ions which is close to the active site, i.e. site 1 Burkholderia cepacia

Inhibitors

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.64 K+ activates Burkholderia cepacia
4.1.1.64 additional information a binding site for alkali metal ions is close to the active site. Exchange of K+ for Na+ at this site is shown to affect the conformation of two active site residues Burkholderia cepacia
4.1.1.64 Rb+ activates Burkholderia cepacia

Organism

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

Cofactor

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