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Literature summary for 1.8.3.1 extracted from

  • Brokx, S.J.; Rothery, R.A.; Zhang, G.; Ng, D.P.; Weiner, J.H.
    Characterization of an Escherichia coli sulfite oxidase homologue reveals the role of a conserved active site cysteine in assembly and function (2005), Biochemistry, 44, 10339-10348.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C102S different location compared to the wild type enzyme Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane wild type enzyme Escherichia coli
-
-
periplasm mutant enzyme C102S Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information The optimal substrate or precise physiological role for YedYZ in Escherichia coli and its well-conserved orthologs in other bacteria remains unknown. Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
sulfite oxidase homologue
-
Escherichia coli
YedY soluble periplasmic catalytic subunit of the oxidoreductase containing a molybdo-molybdopterin form of the molybdenum cofactor Escherichia coli
YedYZ soluble catalytic subunit with a twin arginine leader sequence for export to the periplasm by the Tat translocation system Escherichia coli