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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]
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-
?
an octanoyl-[acyl-carrier protein] + glycine cleavage system protein
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
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-
?
lipoyl-[acyl-carrier protein] + apo-pyruvate dehydrogenase protein
?
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-
?
octanoyl-CoA + [glycine cleavage system 3]-L-lysine
[glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA
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?
octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine
[oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA
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?
octanoyl-CoA + [pyruvate dehydrogenase]-L-lysine
[pyruvate dehydrogenase]-N6-octanoyl-L-lysine + CoA
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-
?
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
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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
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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
-
apo-H protein is the lipoyl bearing subunit of the glycine cleavage system
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-
?
octanoyl-[acyl-carrier protein] + apo-pyruvate dehydrogenase protein
apo-pyruvate dehydrogenase protein N6-(octanoyl)lysine + acyl-carrier protein
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-
-
-
?
octanoyl-[acyl-carrier protein] + glycine dehydrogenase H-protein
glycine dehydrogenase H-protein N6-(octanoyl)lysine + acyl-carrier protein
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glycine dehydrogenase H-protein can be octanoylated both by Lip2 or by lipoate-protein ligase LPLA, EC 2.7.7.63
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?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
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-
-
?
octanoyl-[acyl-carrier protein] + pyruvate dehydrogenase apo-E2 domain
pyruvate dehydrogenase apo E2-domain N6-(octanoyl)lysine + acyl-carrier protein
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-
-
?
octanoyl-[acyl-carrier protein] + [glycine cleavage system 3]-L-lysine
[glycine cleavage system 3]-N6-octanoyl-L-lysine + acyl-carrier protein
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-
in vitro reaction
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?
additional information
?
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an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
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-
-
-
?
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
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-
?
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
acyl-enzyme intermediate mechanism
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-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
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-
-
-
?
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
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-
?
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
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-
?
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
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-
?
octanoyl-[acyl-carrier protein] + alpha-ketoglutarate dehydrogenase apo-E2 domain
alpha-ketoglutarate dehydrogenase E2-domain N6-(octanoyl)lysine + acyl-carrier protein
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-
-
?
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
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-
-
-
?
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)
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-
?
additional information
?
-
pyruvate dehydrogenase E2 domain is exclusively octanoylated by lipoate-protein ligase LPLA, EC 2.7.7.63
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?
additional information
?
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-
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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?
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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]
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-
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-
?
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
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-
?
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + acyl-carrier protein
octanoyl-[acyl-carrier protein] + protein
protein N6-(octanoyl)lysine + [acyl-carrier protein]
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-
-
?
an octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
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-
-
-
?
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
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-
?
octanoyl-[acyl-carrier protein] + a protein
a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
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-
-
-
?
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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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
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
LIPT2 is required in intramitochondrial lipoate synthesis
metabolism
the enzyme initiates lipoyl group assembly
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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Zhao, X.; Miller, J.R.; Cronan, J.E.
The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate
Biochemistry
44
16737-16746
2005
Escherichia coli
brenda
vanden Boom, T.J.; Reed, K.E.; Cronan, J.E.
Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system
J. Bacteriol.
173
6411-6420
1991
Escherichia coli
brenda
Jordan, S.W.; Cronan, J.E., Jr.
The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase
J. Bacteriol.
185
1582-1589
2003
Escherichia coli
brenda
Jordan, S.W.; Cronan, J.E.
A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli
J. Biol. Chem.
272
17903-17906
1997
Escherichia coli, Neurospora crassa, Pisum sativum
brenda
Wada, M.; Yasuno, R.; Jordan, S.W.; Cronan, J.E., Jr.; Wada, H.
Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase
Plant Cell Physiol.
42
650-656
2001
Arabidopsis thaliana
brenda
Nesbitt, N.M.; Baleanu-Gogonea, C.; Cicchillo, R.M.; Goodson, K.; Iwig, D.F.; Broadwater, J.A.; Haas, J.A.; Fox, B.G.; Booker, S.J.
Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase
Protein Expr. Purif.
39
269-282
2005
Escherichia coli
brenda
Ma, Q.; Zhao, X.; Nasser Eddine, A.; Geerlof, A.; Li, X.; Cronan, J.E.; Kaufmann, S.H.; Wilmanns, M.
The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase
Proc. Natl. Acad. Sci. USA
103
8662-8667
2006
Mycobacterium tuberculosis (P9WK83), Mycobacterium tuberculosis H37Rv (P9WK83)
brenda
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
brenda
Hermes, F.A.; Cronan, J.E.
Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis
J. Bacteriol.
191
6796-6803
2009
Escherichia coli
brenda
Guenther, S.; Matuschewski, K.; Mueller, S.
Knockout studies reveal an important role of Plasmodium lipoic acid protein ligase A1 for asexual blood stage parasite survival
PLoS ONE
4
e5510
2009
Plasmodium falciparum
brenda
Christensen, Q.H.; Cronan, J.E.
Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases
Biochemistry
49
10024-10036
2010
Bacillus subtilis
brenda
Hassan, B.H.; Cronan, J.E.
Protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism
J. Biol. Chem.
286
8263-8276
2011
Escherichia coli
brenda
Martin, N.; Christensen, Q.H.; Mansilla, M.C.; Cronan, J.E.; de Mendoza, D.
A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
Mol. Microbiol.
80
335-349
2011
Bacillus subtilis
brenda
Christensen, Q.H.; Martin, N.; Mansilla, M.C.; de Mendoza, D.; Cronan, J.E.
A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
Mol. Microbiol.
80
350-363
2011
Bacillus subtilis
brenda
Ewald, R.; Hoffmann, C.; Neuhaus, E.; Bauwe, H.
Two redundant octanoyltransferases and one obligatory lipoyl synthase provide protein-lipoylation autonomy to plastids of Arabidopsis
Plant Biol.
16
35-42
2014
Arabidopsis thaliana (P0C7R2), Arabidopsis thaliana (Q9SXP7)
brenda
Ewald, R.; Hoffmann, C.; Florian, A.; Neuhaus, E.; Fernie, A.R.; Bauwe, H.
Lipoate-protein ligase and octanoyltransferase are essential for protein lipoylation in mitochondria of Arabidopsis
Plant Physiol.
165
978-990
2014
Arabidopsis thaliana (Q9SXP7)
brenda
Hermes, F.A.; Cronan, J.E.
The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis
Yeast
30
415-427
2013
Saccharomyces cerevisiae
brenda
Habarou, F.; Hamel, Y.; Haack, T.; Feichtinger, R.; Lebigot, E.; Marquardt, I.; Busiah, K.; Laroche, C.; Madrange, M.; Grisel, C.; Pontoizeau, C.; Eisermann, M.; Boutron, A.; Chrtien, D.; Chadefaux-Vekemans, B.; Barouki, R.; Bole-Feysot, C.; Nitschke, P
Biallelic mutations in LIPT2 cause a mitochondrial lipoylation defect associated with severe neonatal encephalopathy
Am. J. Hum. Genet.
101
283-290
2017
Homo sapiens (A6NK58)
brenda
Martins-Noguerol, R.; Moreno-Perez, A.J.; Acket, S.; Makni, S.; Garces, R.; Troncoso-Ponce, A.; Salas, J.J.; Thomasset, B.; Martinez-Force, E.
Lipidomic analysis of plastidial octanoyltransferase mutants of Arabidopsis thaliana
Metabolites
9
209
2019
Arabidopsis thaliana (P0C7R2), Arabidopsis thaliana (Q948J9), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (P0C7R2), Arabidopsis thaliana Col-0 (Q948J9)
brenda
Bernardinelli, E.; Costa, R.; Scantamburlo, G.; To, J.; Morabito, R.; Nofziger, C.; Doerrier, C.; Krumschnabel, G.; Paulmichl, M.; Dossena, S.
Mis-targeting of the mitochondrial protein LIPT2 leads to apoptotic cell death
PLoS ONE
12
e0179591
2017
Homo sapiens (A6NK58), Homo sapiens
brenda
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)
brenda