Information on EC 2.3.1.181 - lipoyl(octanoyl) transferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.1.181
-
RECOMMENDED NAME
GeneOntology No.
lipoyl(octanoyl) transferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an octanoyl-[acyl-carrier protein] + a protein = a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lipoate biosynthesis
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lipoate biosynthesis and incorporation (yeast)
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lipoate biosynthesis and incorporation I
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lipoate biosynthesis and incorporation III (Bacillus)
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Lipoic acid metabolism
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Metabolic 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 2.7.7.63, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).
CAS REGISTRY NUMBER
COMMENTARY hide
392687-64-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Columbia ecotype
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis
Uniprot
Manually annotated by BRENDA team
enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis
Uniprot
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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LipM and LipL phylogenetic tree analysis, overview
malfunction
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DELTAlipL strains are unable to synthesize lipoic acid despite the presence of LipM and the sulfur insertion enzyme, LipA, which should suffice for lipoic acid biosynthesis. Strain NM57 DELTAlipM is auxotrophic for lipoic acid when grown in minimal medium but grew as well as the wild type strain JH642 in the presence of lipoic acid
metabolism
physiological function
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] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
an octanoyl-[acyl-carrier protein] + glycine cleavage system protein
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
lipoyl-[acyl-carrier protein] + apo-pyruvate dehydrogenase protein
?
show the reaction diagram
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-
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
octanoyl-[acyl-carrier protein] + apo-E2 domain
apo E2-domain protein N6-(octanoyl)lysine + acyl-carrier protein
show the reaction diagram
-
reaction proceeds through an acyl-enzyme intermediate
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-
?
octanoyl-[acyl-carrier protein] + apo-H protein
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
show the reaction diagram
-
LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
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-
?
octanoyl-[acyl-carrier protein] + apo-H protein
apo-H protein N6-(octanoyl)lysine + acyl-carrier protein
show the reaction diagram
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apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
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-
?
octanoyl-[acyl-carrier protein] + apo-pyruvate dehydogenase protein
apo-pyruvate dehydrogenase protein N6-(octanoyl)lysine + acyl-carrier protein
show the reaction diagram
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-
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
show the reaction diagram
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
show the reaction diagram
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-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
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] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
an octanoyl-[acyl-carrier protein] + glycine cleavage system protein
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
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-
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
show the reaction diagram
octanoyl-[acyl-carrier protein] + apo-H protein
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
show the reaction diagram
-
LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
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-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
show the reaction diagram
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
show the reaction diagram
O46419
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-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Octanoyl-CoA
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0.5 mM, 67% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KHCO3
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100 mM, slight activation
LipL
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is essential for lipoic acid synthesis, but has no detectable octanoyltransferase or ligase activity either in vitro or in vivo. It catalyses the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the E2 subunit of pyruvate dehydrogenase
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NaOAc
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100 mM, slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0132
apo-H protein
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pH 7.2, 37°C
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0.001
lipoyl-[acyl-carrier protein]
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0.0102
octanoyl-[acyl-carrier protein]
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pH 7.2, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
apo-H protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
7.8
assay of lipoylation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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pH 6.0: about 65% of maximal activity, pH 9.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
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monomer, gel filtration
14000
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gel filtration
26220
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MALDI mass spectrometry
29000
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trimer, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 14000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structure of lipoyltransferase in complex with lipoyl-AMP is determined at a resolution of 2.1 A
enzyme shows thioether-linked active site complex with decanoic acid. Structural comparison with lipoate protein ligase 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
isolation and properties of a very stable complex between LipB and acyl cyrrier protein
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N-terminal hexahistidine-tagged apo-H protein
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wild-type and mutant His-tagged LipB proteins
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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for expression in Escherichia coli BL21DE3 pLysS cells
gene lipM, complements a lipB-defective Escherichia coli mutant strain
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His-tagged LipB
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N-terminal hexahistidine-tagged apo-H protein
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wild-type and mutant His-tagged LipB proteins
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C150A
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loss of the overall catalytic activity and an inability to form the acyl-enzyme intermediate
C150S
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loss of the overall catalytic activity and an inability to form the acyl-enzyme intermediate
K165A
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mutant has weakened catalytic ability
K165R
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mutant remains active
C137A/C169A
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mutant protein retains trace activity
C169A
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mutant enzyme retains trace activity, mutant enzyme forms an octanoyl-LpiB species that is not catalytically competent
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis
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