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Information on EC 2.3.1.181 - lipoyl(octanoyl) transferase and Organism(s) Bos taurus and UniProt Accession O46419

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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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Bos taurus
UNIPROT: O46419
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lipoyltransferase, lipt2, lipb octanoyltransferase, lipoyl(octanoyl) transferase 2, atlip2p2, lipoyl(octanoyl)transferase, lip2p2, lipoyl(octanoyl) transferase, octanoyltransferase lipm, lipoyl (octanoyl)-acyl carrier protein:protein transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoyl(octanoyl) transferase
-
lipoyltransferase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
show the reaction diagram
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
assay of lipoylation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay of lipoylation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIPT_BOVIN
373
0
42072
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of lipoyltransferase in complex with lipoyl-AMP is determined at a resolution of 2.1 A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hydroxylapatite and DEAE-Sepharose columns are used for the purification of the recombinant protein and for the purification of lipoyltransferase from bovine liver mitochondria
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for expression in Escherichia coli BL21DE3 pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujiwara, K.; Hosaka, H.; Matsuda, M.; Okamura-Ikeda, K.; Motokawa, Y.; Suzuki, M.; Nakagawa, A.; Taniguchi, H.
Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP
J. Mol. Biol.
371
222-234
2007
Bos taurus (O46419), Bos taurus
Manually annotated by BRENDA team