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Literature summary for 2.3.1.181 extracted from

  • Ewald, R.; Hoffmann, C.; Neuhaus, E.; Bauwe, H.
    Two redundant octanoyltransferases and one obligatory lipoyl synthase provide protein-lipoylation autonomy to plastids of Arabidopsis (2014), Plant Biol., 16, 35-42.
    View publication on PubMed
Search for more literature for 2.3.1.181

Localization

Localization Comment Organism GeneOntology No. Textmining
plastid
-
 Arabidopsis thaliana 9536
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P0C7R2 isoform Li2p2
-
Arabidopsis thaliana Q9SXP7 isoform Li2p
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-
root
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
octanoyl-[acyl-carrier protein] + alpha-ketoglutarate dehydrogenase apo-E2 domain
-
 Arabidopsis thaliana alpha-ketoglutarate dehydrogenase E2-domain N6-(octanoyl)lysine + acyl-carrier protein
-
 ?
octanoyl-[acyl-carrier protein] + pyruvate dehydrogenase apo-E2 domain
-
 Arabidopsis thaliana pyruvate dehydrogenase apo E2-domain N6-(octanoyl)lysine + acyl-carrier protein
-
 ?

Synonyms

Synonyms Comment Organism
At1g47578
-
 Arabidopsis thaliana
Lip2p2
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function two redundant LIP2 isoforms, LIP2p and LIP2p2, operate in plastids of Arabidopsis. The combined deletion of the two isoenzymes is embryolethal. Disruption of the LIP2p gene in the T-DNA insertion line SALK_031372 does not result in any visible phenotypic alterations relative to the wild type Arabidopsis thaliana
physiological function two redundant LIP2 isoforms, LIP2p and LIP2p2, operate in plastids of Arabidopsis. The combined deletion of the two isoenzymes is embryolethal. LIP2p2 complements a lipoylation-deficient Escherichia coli mutant Arabidopsis thaliana