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Literature summary for 2.3.1.181 extracted from

  • Hermes, F.A.; Cronan, J.E.
    The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis (2013), Yeast, 30, 415-427.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.181

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Lip3 is unable to modify either lipoyl domains or glycine cleavage system 3 when provided with free octanoate, ATP and MgCl2 Saccharomyces cerevisiae ?
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 ?
octanoyl-CoA + [glycine cleavage system 3]-L-lysine
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 Saccharomyces cerevisiae [glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA
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 ?
octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine
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 Saccharomyces cerevisiae [oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA
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 ?
octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine
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 Saccharomyces cerevisiae [pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA
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 ?
octanoyl-[acyl-carrier protein] + [glycine cleavage system 3]-L-lysine
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 Saccharomyces cerevisiae [glycine cleavage system 3]-N6-octanoyl-L-lysine + acyl-carrier protein in vitro reaction ?

Synonyms

Synonyms Comment Organism
LIP3
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function octanoyltransferase Lip2 specifically modifies glycine cleavage system 3 using octanoyl-ACP from mitochondrial FA biosynthesis. When all glycine cleavage system 3 is octanoylated, octanoyl-ACP accumulates. An octanoyl-ACP: CoA transferase transfers the octanoyl moiety to CoA, providing substrate for octanoyltransferase Lip3 to modify pyruvate dehydrogenase and oxoglutarate dehydrogenase. Complementation of the Escherichia coli DELTAlipB DELTAlplA strain by expression of Lip3 requires a host-encoded acyl-CoA synthase Saccharomyces cerevisiae