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Literature summary for 2.8.1.8 extracted from

  • Miller, J.R.; Busby, R.W.; Jordan, S.W.; Cheek, J.; Henshaw, T.F.; Ashley, G.W.; Broderick, J.B.; Cronan, J.E., Jr.; Marletta, M.A.
    Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein (2000), Biochemistry, 39, 15166-15178.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Iron iron-sulfur protein. Presence of [3Fe-4S] and/or [4Fe-4S]clusters in both monomeric and dimeric LipA Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43300
-
monomer, gel filtration Escherichia coli
84600
-
dimer, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and hexahistidine-tagged LipA Escherichia coli

Subunits

Subunits Comment Organism
More enzyme is isolated as a micture of 70% monomer and 30% dimer Escherichia coli