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Information on EC 2.3.1.181 - lipoyl(octanoyl) transferase and Organism(s) Mus musculus and UniProt Accession Q9D009

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IUBMB Comments
This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate . The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).
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Mus musculus
UNIPROT: Q9D009
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lipoyltransferase, lipt2, lipb octanoyltransferase, lipoyl(octanoyl) transferase 2, atlip2p2, octanoyl (lipoyl) n-octanoyl (lipoyl) transferase, lipoyl(octanoyl)transferase, lip2p2, lipoyl(octanoyl) transferase, octanoyltransferase lipm, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
octanoyl-[acyl-carrier protein]:protein N-octanoyltransferase
This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate [4] although octanoyl-ACP is likely to be the true substrate [6]. The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).
CAS REGISTRY NUMBER
COMMENTARY hide
392687-64-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
an octanoyl-[acyl-carrier protein] + GCSH protein
GCSH protein N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme initiates lipoyl group assembly
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIPT2_MOUSE
231
0
24955
Swiss-Prot
Mitochondrion (Reliability: 5)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli DH5alpha cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cao, X.; Zhu, L.; Song, X.; Hu, Z.; Cronan, J.
Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes
Proc. Natl. Acad. Sci. USA
115
E7063-E7072
2018
Mus musculus (Q9D009)
Manually annotated by BRENDA team