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

BRENDA support

Literature summary for 1.2.3.3 extracted from

  • Wille, G.; Ritter, M.; Weiss, M.S.; Koenig, S.; Maentele, W.; Huebner, G.
    The role of Val-265 for flavin adenine dinucleotide (FAD) binding in pyruvate oxidase: FTIR, kinetic, and crystallographic studies on the enzyme variant V265A (2005), Biochemistry, 44, 5086-5094.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Lactiplantibacillus plantarum

Crystallization (Commentary)

Crystallization (Comment) Organism
V265A mutant Lactiplantibacillus plantarum

Protein Variants

Protein Variants Comment Organism
V265A similar catalytic properties compared to the wild-type protein, but decreased affinity for FAD Lactiplantibacillus plantarum

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum P37063
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Lactiplantibacillus plantarum

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Lactiplantibacillus plantarum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + phosphate + O2 + H2O
-
Lactiplantibacillus plantarum acetyl phosphate + CO2 + H2O2
-
?

Synonyms

Synonyms Comment Organism
POX
-
Lactiplantibacillus plantarum
pyruvate oxidase
-
Lactiplantibacillus plantarum

Cofactor

Cofactor Comment Organism Structure
FAD bound to V265 Lactiplantibacillus plantarum
thiamine diphosphate
-
Lactiplantibacillus plantarum