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

BRENDA support

Literature summary for 1.2.5.1 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

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

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain CG3 Escherichia coli

Localization

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

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli CG3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

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

Synonyms

Synonyms Comment Organism
pyruvate oxidase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate required Escherichia coli