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Literature summary extracted from

  • Tittmann, K.; Golbik, R.; Ghisla, S.; Hubner, G.
    Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum (2000), Biochemistry, 39, 10747-10754.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.3.3 pyruvate + phosphate + O2 + H2O Lactiplantibacillus plantarum specifically favors phosphorylysis rather than hydrolysis, decarboxylation step not rate-limiting acetyl phosphate + CO2 + H2O2
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.3 Lactiplantibacillus plantarum
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.3.3 pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O artificial electron acceptor 2,6-dichlorophenolindophenol reacts with the carbanion of the enzyme-bound intermediate hydroxyethyl-thiamine diphosphate Lactiplantibacillus plantarum acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
-
 ?
1.2.3.3 pyruvate + phosphate + O2 reduction of enzyme by its substrate, pyruvate, in the absence of oxygen Lactiplantibacillus plantarum acetyl phosphate + CO2 + H2O2
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 ir
1.2.3.3 pyruvate + phosphate + O2 + H2O specifically favors phosphorylysis rather than hydrolysis, decarboxylation step not rate-limiting Lactiplantibacillus plantarum acetyl phosphate + CO2 + H2O2
-
 ir

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.3.3 16
-
 pyruvate electron acceptor: O2 Lactiplantibacillus plantarum
1.2.3.3 26
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 pyruvate electron acceptor: 2,6-dichlorophenolindophenol Lactiplantibacillus plantarum

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.3.3 FAD reduction of FAD via a two-step single-electron transfer Lactiplantibacillus plantarum
1.2.3.3 thiamine diphosphate
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 Lactiplantibacillus plantarum