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Literature summary for 1.2.3.3 extracted from

  • Tittmann, K.; Wille, G.; Golbik, R.; Weidner, A.; Ghisla, S.; Huebner, G.
    Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum. Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FA (2005), Biochemistry, 44, 13291-13303.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Lactiplantibacillus plantarum

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum
-
-
-

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
-
Lactiplantibacillus plantarum acetyl phosphate + CO2 + H2O2
-
r
pyruvate + phosphate + O2 + H2O
-
Lactiplantibacillus plantarum acetyl phosphate + CO2 + H2O2
-
?

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.32
-
pyruvate in phosphate-free medium Lactiplantibacillus plantarum
35
-
pyruvate in phosphate buffer Lactiplantibacillus plantarum

Cofactor

Cofactor Comment Organism Structure
FAD
-
Lactiplantibacillus plantarum
thiamine diphosphate
-
Lactiplantibacillus plantarum