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Literature summary for 6.3.1.20 extracted from

  • Brookfield, D.E.; Green, J.; Ali, S.T.; Machado, R.S.; Guest, J.R.
    Evidence for two protein-lipoylation activities in Escherichia coli (1991), FEBS Lett., 295, 13-16.
    View publication on PubMed
Search for more literature for 6.3.1.20

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ may substitute for Mg2+, LPL-B Escherichia coli
Co2+ may substitute for Mg2+, both LPL-A and LPL-B Escherichia coli
Cu2+ may substitute for Mg2+, LPL-A Escherichia coli
Fe2+ may substitute for Mg2+, LPL-B Escherichia coli
Fe3+ may substitute for Mg2+, LPL-B Escherichia coli
Mg2+ required, both LPL-A and LPL-B Escherichia coli
Mn2+ may substitute for Mg2+, both LPL-A and LPL-B Escherichia coli
Ni2+ may substitute for Mg2+, both LPL-A and LPL-B Escherichia coli
Zn2+ may substitute for Mg2+, both LPL-A and LPL-B Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
 x * 47000, SDS-PAGE, both LPL-A and LPL-B Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 isoenzymes LPL-A and LPL-B
-

Purification (Commentary)

Purification (Comment) Organism
both LPL-A and LPL-B, partial Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + DL-lipoic acid + protein
-
 Escherichia coli diphosphate + AMP + DL-lipoyl-protein
-
 ?
DL-lipoyladenylate + protein
-
 Escherichia coli adenylate + DL-lipoyl-protein
-
 ?
octanoyl adenylate + protein
-
 Escherichia coli adenylate + octanoyl-protein
-
 ?

Subunits

Subunits Comment Organism
? x * 47000, SDS-PAGE, both LPL-A and LPL-B Escherichia coli