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Literature summary extracted from

  • Hamilton, S.E.; Recny, M.; Hager, L.P.
    Identification of the high-affinity lipid binding site in Escherichia coli pyruvate oxidase (1986), Biochemistry, 25, 8179-8183.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.5.1 lauric acid activation by covalent attachment, binding site Lys544 Escherichia coli
1.2.5.1 Lipids enzyme is activated by lipids, high affinity binding site Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.5.1 expressed in Escherichia coli strain CG3 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.5.1 membrane peripheral membrane-associated enzyme Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.1 Mn2+ divalent metal ion required Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.5.1 60000
-
the lauric acid-labeled enzyme is not digested neither by trypsin nor alpha-chymotrypsin in the presence of 0.1% SDS. Effective digestion is achieved by thermolysin, to a 45000 and a 15000 Da fragment Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.1 Escherichia coli
-
-
-
1.2.5.1 Escherichia coli CG3
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.5.1 the enzyme is purified from an Escherichia coli strain CG3 harboring a plasmid carrying a plasmid th eoxidase gene Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.5.1 pyruvate + ferricyanide + H2O addition of 1% lauric acid Escherichia coli acetate + CO2 + ferrocyanide
-
?
1.2.5.1 pyruvate + ferricyanide + H2O addition of 1% lauric acid Escherichia coli CG3 acetate + CO2 + ferrocyanide
-
?

Synonyms

EC Number Synonyms Comment Organism
1.2.5.1 pyruvate oxidase
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.5.1 thiamine diphosphate required Escherichia coli