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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
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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
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malfunction
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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
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metabolism
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The apicoplast-specific LipB is dispensable for parasite growth due to functional redundancy of the parasites lipoic acid/octanoic acid ligases/transferases.
metabolism
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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
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the enzyme is involved in the biosynthesis of the lipoyl cofactor
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metabolism
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the enzyme is involved in the biosynthesis of lipoyl cofactor
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physiological function
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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
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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
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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
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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