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Literature summary for 6.3.1.20 extracted from

  • Zhao, X.; Miller, J.R.; Jiang, Y.; Marletta, M.A.; Cronan, J.E.
    Assembly of the covalent linkage between lipoic acid and its cognate enzymes (2003), Chem. Biol., 10, 1293-1302.
    View publication on PubMed
Search for more literature for 6.3.1.20

Protein Variants

Protein Variants Comment Organism
additional information lipB mutant strain, grows well when supplemented with octanoate in place of lipoate Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli LplA potein attaches octanoate to the dehydrogenase and LipA protein then converts the octanoate to lipoate ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Escherichia coli
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 isoenzymes LipB, LplA
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + octanoate + pyruvate dehydrogenase subunit E2 lipoate-protein ligase attaches octanoate to the dehydrogenase subunit and sulfur insertion protein LipA, then converts octanoate to lipoate. LipA acts on both octanoate and octanoyl-proteins Escherichia coli diphosphate + AMP + octanoyl-pyruvate dehydrogenase subunit E2
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 ?
additional information LplA potein attaches octanoate to the dehydrogenase and LipA protein then converts the octanoate to lipoate Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
LPLA
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 Escherichia coli