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Information on EC 2.3.1.181 - lipoyl(octanoyl) transferase
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2.3.1.181 lipoyl(octanoyl) transferaseIUBMB 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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Word Map
- 2.3.1.181
-
lipoylation
-
lipoic
-
octanoylated
- lipoyl-amp
- 2-oxoacid
- h-protein
-
lipoate-dependent
-
lipoate-protein
- acidosis
-
octanoic
-
2-ketoacid
- 2-oxoadipate
-
epsilon-amino
- fe-s
-
alpha-keto
-
swinging
-
fujiwara
-
nonketotic
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
lipoyltransferase, lipt2, lipb octanoyltransferase, lipoyl(octanoyl) transferase 2, atlip2p2, lipoyl(octanoyl) transferase, octanoyltransferase lipm, lipoyl (octanoyl)-acyl carrier protein:protein transferase, octanoyl (lipoyl) n-octanoyl (lipoyl) transferase, lipoyl(octanoyl)transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
At1g47578
At4G31050
AtLIP2p2
LIP2
LIP2P1
Lip2p2
LipB
lipoyltransferase
LIPT2
plastidial octanoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
octanoyl-[acyl-carrier protein] + protein = protein 6-N-(octanoyl)lysine + acyl carrier protein
octanoyl-[acyl-carrier protein] + protein = protein 6-N-(octanoyl)lysine + acyl carrier protein
-
-
-
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octanoyl-[acyl-carrier protein] + protein = protein 6-N-(octanoyl)lysine + acyl carrier protein
enzyme functions as a cysteine/lysine dyad acyltransferase, where K142 and C176 are acid/base catalysts. Reaction proceeds via an internal thioester intermediate
octanoyl-[acyl-carrier protein] + protein = protein 6-N-(octanoyl)lysine + acyl carrier protein
enzyme functions as a cysteine/lysine dyad acyltransferase, where K142 and C176 are acid/base catalysts. Reaction proceeds via an internal thioester intermediate
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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).
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CAS REGISTRY NUMBER
COMMENTARY
392687-64-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
an octanoyl-[acyl-carrier protein] + GCSH protein
GCSH protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
-
-
?
an octanoyl-[acyl-carrier protein] + glycine cleavage system protein
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
-
-
-
-
?
lipoyl-[acyl-carrier protein] + apo-pyruvate dehydrogenase protein
?
-
-
-
-
?
octanoyl-CoA + [glycine cleavage system 3]-L-lysine
[glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA
-
-
-
-
?
octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine
[oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA
-
-
-
-
?
octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine
[pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA
-
-
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
octanoyl-[acyl-carrier protein] + alpha-ketoglutarate dehydrogenase apo-E2 domain
alpha-ketoglutarate dehydrogenase E2-domain N6-(octanoyl)lysine + acyl-carrier protein
octanoyl-[acyl-carrier protein] + apo-E2 domain
apo E2-domain protein N6-(octanoyl)lysine + acyl-carrier protein
-
reaction proceeds through an acyl-enzyme intermediate
-
-
?
octanoyl-[acyl-carrier protein] + apo-H protein
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
-
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
-
-
?
octanoyl-[acyl-carrier protein] + apo-H protein
apo-H protein N6-(octanoyl)lysine + acyl-carrier protein
-
apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
-
-
?
octanoyl-[acyl-carrier protein] + apo-pyruvate dehydrogenase protein
apo-pyruvate dehydrogenase protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
-
?
octanoyl-[acyl-carrier protein] + glycine dehydrogenase H-protein
glycine dehydrogenase H-protein N6-(octanoyl)lysine + acyl-carrier protein
-
glycine dehydrogenase H-protein can be octanoylated both by Lip2 or by lipoate-protein ligase LPLA, EC 2.7.7.63
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
-
-
-
?
octanoyl-[acyl-carrier protein] + pyruvate dehydrogenase apo-E2 domain
pyruvate dehydrogenase apo E2-domain N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
?
octanoyl-[acyl-carrier protein] + [glycine cleavage system 3]-L-lysine
[glycine cleavage system 3]-N6-octanoyl-L-lysine + acyl-carrier protein
-
-
in vitro reaction
-
?
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
-
-
-
?
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
LipM specifically modifies the glycine cleavage system protein, GcvH
-
-
?
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
acyl-enzyme intermediate mechanism
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
-
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
the transfer of the octanoyl group from octanoyl-ACP to Bacillus subtilis GcvH occurs in a LipM-dependent manner. The LipM reaction proceeds through a thioester-linked acyl enzyme intermediate. The LipM active site nucleophile is identified as C150
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. LipB accumulates an octanoyl-enzyme intermediate with no sign of a lipoyl-enzyme intermediate
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. The binding sites for LipB reside both in the lipoyl domain and catalytic core sequences
-
-
?
octanoyl-[acyl-carrier protein] + alpha-ketoglutarate dehydrogenase apo-E2 domain
alpha-ketoglutarate dehydrogenase E2-domain N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
?
octanoyl-[acyl-carrier protein] + alpha-ketoglutarate dehydrogenase apo-E2 domain
alpha-ketoglutarate dehydrogenase E2-domain N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) and of the 2-oxoglutarate dehydrogenase complex
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of glycine cleavage system (H protein)
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)
-
-
?
additional information
?
-
pyruvate dehydrogenase E2 domain is exclusively octanoylated by lipoate-protein ligase LPLA, EC 2.7.7.63
-
-
?
additional information
?
-
-
Lip3 is unable to modify either lipoyl domains or glycine cleavage system 3 when provided with free octanoate, ATP and MgCl2
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
an octanoyl-[acyl-carrier protein] + glycine cleavage system protein
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
-
-
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
octanoyl-[acyl-carrier protein] + apo-H protein
APO H-protein N6-(octanoyl)lysine + acyl-carrier protein
-
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
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
-
-
-
?
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
-
-
-
?
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
LipM specifically modifies the glycine cleavage system protein, GcvH
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
-
-
-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. LipB accumulates an octanoyl-enzyme intermediate with no sign of a lipoyl-enzyme intermediate
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) and of the 2-oxoglutarate dehydrogenase complex
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
-
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of glycine cleavage system (H protein)
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)
-
-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
-
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
LipL
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis, Lactic
Lipoyltransferase 1 Gene Defect Resulting in Fatal Lactic Acidosis in Two Siblings.
Brain Diseases
Biallelic Mutations in LIPT2 Cause a Mitochondrial Lipoylation Defect Associated with Severe Neonatal Encephalopathy.
Leigh Disease
Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.
Mitochondrial Diseases
Progress in the Enzymology of the Mitochondrial Diseases of Lipoic Acid Requiring Enzymes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 65% of maximal activity, pH 9.0: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis
Uniprot
brenda
enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis
Uniprot
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
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
malfunction
biallelic mutations in LIPT2 cause a mitochondrial lipoylation defect associated with severe neonatal encephalopathy
malfunction
first 31 amino acids of the N-terminus of LIPT2 represent a mitochondrial targeting sequence and inhibition of the transit of LIPT2 to the mitochondrion results in apoptotic cell death associated with activation of the apoptotic volume decrease current in normotonic conditions, as well as over-activation of the swelling-activated chloride current, mitochondrial membrane potential collapse, caspase-3 cleavage and nuclear DNA fragmentation
malfunction
lack of the AtLIP2p2 isoform results in decrease in palmitic acid, 16:0, and polyunsaturated fatty acids at the expenses of oleate and significant increases of the seed oil content
malfunction
the silencing of Lip2p1 results in a significant decrease in 16:0 and 18:3 fatty acids accompanied by an increase in 18:1 and 18:2 content
malfunction
-
lack of the AtLIP2p2 isoform results in decrease in palmitic acid, 16:0, and polyunsaturated fatty acids at the expenses of oleate and significant increases of the seed oil content
-
malfunction
-
the silencing of Lip2p1 results in a significant decrease in 16:0 and 18:3 fatty acids accompanied by an increase in 18:1 and 18:2 content
-
metabolism
-
The apicoplast-specific LipB is dispensable for parasite growth due to functional redundancy of the parasites lipoic acid/octanoic acid ligases/transferases.
metabolism
-
The LipB octanoyltransferase catalyzes the first step of lipoic acid synthesis in Escherichia coli, transfer of the octanoyl moiety from octanoyl-acyl carrier protein to the lipoyl domains of the E2 subunits of the 2-oxoacid dehydrogenases of aerobic metabolism.
metabolism
the enzyme is involved in the biosynthesis of lipoyl cofactor
metabolism
the enzyme is involved in the biosynthesis of the lipoyl cofactor
metabolism
the enzyme is involved in the post-translational modification of key energy metabolism enzymes in humans
metabolism
-
the enzyme is involved in the biosynthesis of the lipoyl cofactor
-
metabolism
-
the enzyme is involved in the biosynthesis of lipoyl cofactor
-
physiological function
-
LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes
physiological function
-
LipM is required for modification of lipoyl domains by the biosynthetic pathway, it is responsible for octanoyl transfer in vivo requirement for LipL. But LipM is only required for the endogenous lipoylation pathway, whereas LipL also plays a role in lipoic acid scavenging
physiological function
-
LipM specifically modifies the glycine cleavage system protein, GcvH. GcvH is required in Bacillus subtilis lipoic acid biosynthesis, overview. LipM is an octanoyltransferase required for lipoic acid synthesis, and LipL 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-glycine cleavage system protein to the E2 subunit of pyruvate dehydrogenase
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
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
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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C150A
-
loss of the overall catalytic activity and an inability to form the acyl-enzyme intermediate
C150S
-
loss of the overall catalytic activity and an inability to form the acyl-enzyme intermediate
C169A
-
mutant enzyme retains trace activity, mutant enzyme forms an octanoyl-LpiB species that is not catalytically competent
C169S
additional information
C169S
-
mutant enzyme has no activity, mutant enzyme forms an octanoyl-LpiB species that is not catalytically competent
C169S
-
the hydrolyzed C169S mutant protein shows higher methyl octanoate levels than those of the wild type protein preparations
additional information
-
construction of strain NM57 in which lipM is replaced with a kanamycin-resistance determinant. Gene lipM is placed under control of a xylose-inducible promoter PxylA is introduced into the DELTAlipM strain NM57 giving the lipM amyE::PxylA-lipM strain NM08. LipM can be functionally replaced by expression of Escherichia coli lipB, expression of Escherichia coli lipB allows growth of Bacillus subtilis DELTAlipL or DELATlipM strains in the absence of supplements. In contrast, growth of an Escherichia coli DELTAlipB strain can be complemented with lipM, but not lipL
additional information
-
Escherichia coli wild type strain and several spontaneous LipB knockout strains are used
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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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine