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ATP + (R)-lipoate
lipoyl-AMP + diphosphate
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
ATP + (R)-lipoic acid + Escherichia coli apoH-protein
diphosphate + AMP + Escherichia coli (R)-lipoyl-apoH-protein
-
-
-
-
?
ATP + 5-[[(1R,2R,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]pentanoic acid + a [lipoyl-carrier protein]-L-lysine
?
-
-
-
-
?
ATP + 5-[[(1R,2S,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]pentanoic acid + a [lipoyl-carrier protein]-L-lysine
?
-
-
-
-
?
ATP + 6-([[(1R,4R)-bicyclo[2.2.1]hept-5-en-2-yl]methyl]amino)hexanoic acid + a [lipoyl-carrier protein]-L-lysine
?
-
-
-
-
?
ATP + 6-thio-octanoic acid
diphosphate + 6-thio-octanoyl-AMP
-
at 326% of the rate with DL-lipoic acid
-
-
?
ATP + 6-[[(1R,2R,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid + a [lipoyl-carrier protein]-L-lysine
?
-
-
-
-
?
ATP + 6-[[(1S,2R,4S)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid + a [lipoyl-carrier protein]-L-lysine
?
ATP + 8-methyl-lipoic acid
diphosphate + 8-methyl-lipoyl-AMP
-
at 73% of the rate with DL-lipoic acid
-
-
?
ATP + 8-[[(1R,2S,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]octanoic acid + a [lipoyl-carrier protein]-L-lysine
?
-
-
-
-
?
ATP + D-lipoic acid
diphosphate + D-lipoyl-AMP
ATP + dihydro-DL-lipoic acid
diphosphate + dihydro-DL-lipoyl-AMP
-
at 80% of the rate with DL-lipoic acid
-
-
?
ATP + DL-lipoic acid
diphosphate + DL-lipoyl-AMP
-
-
-
-
?
ATP + DL-lipoic acid + protein
AMP + diphosphate + DL-lipoyl-protein
-
-
-
?
ATP + DL-lipoic acid + protein
diphosphate + AMP + DL-lipoyl-protein
-
-
-
-
?
ATP + L-lipoic acid
diphosphate + L-lipoyl-AMP
-
at 36% of the rate with DL-lipoic acid
-
-
?
ATP + lipoate + apoH-protein
?
-
-
-
-
?
ATP + lipoate + apoprotein
AMP + diphosphate + protein N6-(lipoyl)lysine
ATP + lipoate + biotin
AMP + diphosphate + ?
-
-
-
-
?
ATP + lipoate + H-protein
AMP + diphosphate + ?
-
-
-
-
?
ATP + lipoate + LplA acceptor peptide 1
?
-
-
-
-
?
ATP + lipoate + LplA acceptor peptide 2
?
-
-
-
-
?
ATP + octanoate + pyruvate dehydrogenase subunit E2
diphosphate + AMP + octanoyl-pyruvate dehydrogenase subunit E2
-
lipoate-protein ligase attaches octanoate to the dehydrogenase subunit and sulfur insertion protein LipA, then converts octanoate to lipoate. LipA acts on both octanoate and octanoyl-proteins
-
-
?
ATP + octanoic acid
diphosphate + octanoyl-AMP
ATP + selenolipoic acid
diphosphate + selenolipoyl-AMP
-
at 12% of the rate with DL-lipoic acid
-
-
?
DL-lipoyladenylate + protein
adenylate + DL-lipoyl-protein
-
-
-
-
?
lipoic acid + ATP + apoprotein
diphosphate + AMP + N6-(lipoyl)-lysine
lipoyl-AMP + [GLDH1 protein]-L-lysine
[GLDH1 protein]-N6-(lipoyl)lysine + AMP
-
-
-
-
?
lipoyl-AMP + [glycine cleavage H protein]-L-lysine
[glycine cleavage H protein]-N6-(lipoyl)lysine + AMP
-
-
-
-
ir
lipoyl-AMP + [lE2p subunit of the pyruvate dehydrogenase complex]-L-lysine
[E2p subunit of the pyruvate dehydrogenase complex]-N6-(lipoyl)lysine + AMP
-
-
-
-
ir
lipoyl-AMP + [pyruvate dehydrogenase-E2]-L-lysine
[pyruvate dehydrogenase-E2]-N6-(lipoyl)lysine + AMP
-
-
-
-
?
lipoyl-AMP + [TM137 soluble protein]-L-lysine
[TM137 soluble protein]-N6-(lipoyl)lysine + AMP
-
-
-
-
?
octanoic acid + ATP
diphosphate + octanoyl-AMP
-
-
-
-
?
octanoyl adenylate + protein
adenylate + octanoyl-protein
-
-
-
-
?
octanoyl-ACP + lipoyl protein
octanoylated lipoyl protein + ACP
additional information
?
-
ATP + (R)-lipoate
lipoyl-AMP + diphosphate
-
-
-
-
?
ATP + (R)-lipoate
lipoyl-AMP + diphosphate
-
-
-
-
r
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
-
?
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
?
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
?
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
?
ATP + 6-[[(1S,2R,4S)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid + a [lipoyl-carrier protein]-L-lysine
?
-
-
-
-
?
ATP + 6-[[(1S,2R,4S)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid + a [lipoyl-carrier protein]-L-lysine
?
-
6-[[(1S,2R,4S)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid-LAP-eDHFR labeled with tetrazine-fluorescein
-
-
?
ATP + D-lipoic acid
diphosphate + D-lipoyl-AMP
-
-
-
?
ATP + D-lipoic acid
diphosphate + D-lipoyl-AMP
-
at 83% of the rate with DL-lipoic acid
-
-
?
ATP + D-lipoic acid
diphosphate + D-lipoyl-AMP
-
-
-
-
?
ATP + D-lipoic acid
diphosphate + D-lipoyl-AMP
-
-
-
-
?
ATP + D-lipoic acid
diphosphate + D-lipoyl-AMP
-
-
-
?
ATP + lipoate + apoprotein
AMP + diphosphate + protein N6-(lipoyl)lysine
-
protein lipoylation, salvage pathway
-
-
?
ATP + lipoate + apoprotein
AMP + diphosphate + protein N6-(lipoyl)lysine
-
protein lipoylation, salvage pathway
-
-
?
ATP + octanoic acid
diphosphate + octanoyl-AMP
-
-
-
-
?
ATP + octanoic acid
diphosphate + octanoyl-AMP
-
at 13% of the rate with DL-lipoic acid
-
-
?
lipoic acid + ATP + apoprotein
diphosphate + AMP + N6-(lipoyl)-lysine
-
lipoic acid is (R)-5-(1,2-dithiolan-3-yl)pentanoic acid, also called 6,8-dithiooctanoic acid or thioctic acid
-
-
?
lipoic acid + ATP + apoprotein
diphosphate + AMP + N6-(lipoyl)-lysine
-
two-step reaction of protein lipoylation at lysine residues with lipoyl-AMP intermediate
-
-
?
lipoic acid + ATP + apoprotein
diphosphate + AMP + N6-(lipoyl)-lysine
-
complementation assay in LplA-deficient Escherichia coli strain TM137 (2 days, 37°C) using exogenous lipoate
detection of lipoylated proteins in Western blot
-
?
octanoyl-ACP + lipoyl protein
octanoylated lipoyl protein + ACP
-
-
-
-
?
octanoyl-ACP + lipoyl protein
octanoylated lipoyl protein + ACP
-
-
-
-
?
additional information
?
-
-
the enzyme uses octanoyl-nucleoside monophosphate and possibly other donor substrates for the octanoylation of mitochondrial pyruvate dehydrogenase-E2 (essentially) and glycine decarboxylase H-protein, and shows no reactivity with bacterial and possibly plant alpha- ketoglutarate dehydrogenase-E2
-
-
?
additional information
?
-
-
recombinant LplA1Ct is able to lipoylate apo-PDH and 2-OGDH-E2 subunits purified from Escherichia coli ATM967 as detected by Western blotting with anti-lipoic acid antibody. LplA1Ct is also able to lipoylate the recombinant chlamydial BCKDH-E2 subunit
-
-
?
additional information
?
-
-
LipB protein utilizes lipoyl groups generated via endogenous, LipA mediated biosynthesis and causes the accumulation of aberrantly modified octanoyl-proteins in lipoate-deficient cells
-
-
?
additional information
?
-
-
LplA potein attaches octanoate to the dehydrogenase and LipA protein then converts the octanoate to lipoate
-
-
?
additional information
?
-
-
LplA's natural protein substrates have a conserved beta-hairpin structure
-
-
?
additional information
?
-
enzyme LplA is able to ligate with high specificity an alkyl azide to a target protein previously fused with a 13 aa recognition sequence for LplA, ligase-acceptor peptide (LAP)
-
-
?
additional information
?
-
-
two-step protein labeling by using lipoic acid ligase with norbornene substrates and subsequent inverse-electron demand Diels-Alder reaction, identification of a potential candidate for use as a norbornene-bearing substrate for LplAW37V-mediated peptide labeling. The norbornene moiety is highly stable in the presence of nucleophiles, and can be efficiently coupled to the 13-aa LAP-tag and further modified with tetrazine fluorophore conjugates in inverse-electron-demand Diels-Alder cycloaddition. The rigid compounds 4-[(3aS,4R,7S,7aS)-1,3-dioxo-1,3,3a,4,7,7a-hexahydro-2H-4,7-methanoisoindol-2-yl]butanoic acid, 5-[(3aS,4R,7S,7aS)-1,3-dioxo-1,3,3a,4,7,7a-hexahydro-2H-4,7-methanoisoindol-2-yl]pentanoic acid, and 6-[(3aS,4R,7S,7aS)-1,3-dioxo-1,3,3a,4,7,7a-hexahydro-2H-4,7-methanoisoindol-2-yl]hexanoic acid are not accepted as substrates at all, likely due to less flexibility and steric hindrance. Derivatives with shorter (4-[[(1R,2S,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]butanoic acid, 5-[[(1R,2S,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]pentanoic acid, and 4-[[(1R,2S,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]butanoic acid) and longer (9-[[(1R,2S,4R)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]nonanoic acid) aliphatic chains are not accepted by LplAW37V, thus indicating the necessity of a particular chain length to fit the dimensions of the active site of LplAW37V
-
-
?
additional information
?
-
-
the enzyme lipoic acid ligase (LplA) is used to conjugate [18F]-fluorooctanoic acid to an antibody fragment bearing the peptide substrate of LplA, termed LAP, method development, assay optimization and evaluation, overview. Enzyme LplA recognizes the unnatural substrate [18F]-fluorooctanoic acid and conjugates it site-specifically to its peptide substrate LAP
-
-
?
additional information
?
-
-
utilization of host-derived lipoyl peptides which is prerequisite for bacterial fitness and intracellular proliferation
-
-
?
additional information
?
-
-
LplA1, lipoamide as lipoate source does not dictate LplA1-supported bacterial growth
-
-
?
additional information
?
-
-
LplA1, lipoate ligase activity since overexpression rescued growth of LplA1-deficient Escherichia coli strain
-
-
?
additional information
?
-
-
LplA1, lipoylated tripeptide released from proteinase K-digested pyruvate dehydrogenase or synthetic lipoylated tripeptide (aspartate-(lipoyl-)lysine-alanine, DK(L)A, 1 microgram) serves as lipoate substrate
-
-
?
additional information
?
-
-
LplA2, no utilization of host-derived lipoyl peptides as lipoate source
-
-
?
additional information
?
-
-
LplA2, utilization of lipoamide or free lipoate as lipoate source
-
-
?
additional information
?
-
-
lipoate scavenging by enzymes drives mitochondrial lipoylation, while apicoplast lipoylation relies on biosynthesis
-
-
?
additional information
?
-
-
no substrate: pyruvate dehydrogenase subunit E2
-
-
?
additional information
?
-
cell-based lipoylation assays using wild-type and truncated mutant enzymes recombinantly expressed in lipoylation-deficient Escherichia coli strain JEG3
-
-
?
additional information
?
-
-
cell-based lipoylation assays using wild-type and truncated mutant enzymes recombinantly expressed in lipoylation-deficient Escherichia coli strain JEG3
-
-
?
additional information
?
-
-
the Lip3 lipoate protein ligase homologue of Saccharomyces cerevisiae has octanoyl-CoA:protein transferase activity. No amidotransfer activity is detected for Lip3 in vitro
-
-
?
additional information
?
-
it is shown that E2 lipoyl domain peptide, LplA and CTD are physically associated. LplA and CTD exist in a ratio 1:1
-
-
?
additional information
?
-
it is shown that E2 lipoyl domain peptide, LplA and CTD are physically associated. LplA and CTD exist in a ratio 1:1
-
-
?
additional information
?
-
-
it is shown that E2 lipoyl domain peptide, LplA and CTD are physically associated. LplA and CTD exist in a ratio 1:1
-
-
?
additional information
?
-
LplA has no detectable ligase activity in vitro in the absence of LplB
-
-
?
additional information
?
-
-
LplA has no detectable ligase activity in vitro in the absence of LplB
-
-
?
additional information
?
-
when the Thermoplasma acidophilum E2 lipoyl domain peptide is incubated with either HisLplA or HisCTD in the presence of ATP, MgCl2 and lipoic acid, no lipoylation is detected. Incubation with both HisLplA and HisCTD in the one reaction results in the lipoylation of the E2 lipoyl domain peptide as indicated by nondenaturing PAGE
-
-
?
additional information
?
-
when the Thermoplasma acidophilum E2 lipoyl domain peptide is incubated with either HisLplA or HisCTD in the presence of ATP, MgCl2 and lipoic acid, no lipoylation is detected. Incubation with both HisLplA and HisCTD in the one reaction results in the lipoylation of the E2 lipoyl domain peptide as indicated by nondenaturing PAGE
-
-
?
additional information
?
-
-
when the Thermoplasma acidophilum E2 lipoyl domain peptide is incubated with either HisLplA or HisCTD in the presence of ATP, MgCl2 and lipoic acid, no lipoylation is detected. Incubation with both HisLplA and HisCTD in the one reaction results in the lipoylation of the E2 lipoyl domain peptide as indicated by nondenaturing PAGE
-
-
?
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ATP + (R)-lipoate
lipoyl-AMP + diphosphate
-
-
-
-
?
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
ATP + lipoate + apoprotein
AMP + diphosphate + protein N6-(lipoyl)lysine
ATP + lipoate + H-protein
AMP + diphosphate + ?
-
-
-
-
?
lipoic acid + ATP + apoprotein
diphosphate + AMP + N6-(lipoyl)-lysine
lipoyl-AMP + [GLDH1 protein]-L-lysine
[GLDH1 protein]-N6-(lipoyl)lysine + AMP
-
-
-
-
?
additional information
?
-
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
-
?
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
?
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
?
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
-
-
?
ATP + lipoate + apoprotein
AMP + diphosphate + protein N6-(lipoyl)lysine
-
protein lipoylation, salvage pathway
-
-
?
ATP + lipoate + apoprotein
AMP + diphosphate + protein N6-(lipoyl)lysine
-
protein lipoylation, salvage pathway
-
-
?
lipoic acid + ATP + apoprotein
diphosphate + AMP + N6-(lipoyl)-lysine
-
lipoic acid is (R)-5-(1,2-dithiolan-3-yl)pentanoic acid, also called 6,8-dithiooctanoic acid or thioctic acid
-
-
?
lipoic acid + ATP + apoprotein
diphosphate + AMP + N6-(lipoyl)-lysine
-
two-step reaction of protein lipoylation at lysine residues with lipoyl-AMP intermediate
-
-
?
additional information
?
-
-
LipB protein utilizes lipoyl groups generated via endogenous, LipA mediated biosynthesis and causes the accumulation of aberrantly modified octanoyl-proteins in lipoate-deficient cells
-
-
?
additional information
?
-
-
LplA potein attaches octanoate to the dehydrogenase and LipA protein then converts the octanoate to lipoate
-
-
?
additional information
?
-
-
LplA's natural protein substrates have a conserved beta-hairpin structure
-
-
?
additional information
?
-
-
utilization of host-derived lipoyl peptides which is prerequisite for bacterial fitness and intracellular proliferation
-
-
?
additional information
?
-
-
lipoate scavenging by enzymes drives mitochondrial lipoylation, while apicoplast lipoylation relies on biosynthesis
-
-
?
additional information
?
-
it is shown that E2 lipoyl domain peptide, LplA and CTD are physically associated. LplA and CTD exist in a ratio 1:1
-
-
?
additional information
?
-
it is shown that E2 lipoyl domain peptide, LplA and CTD are physically associated. LplA and CTD exist in a ratio 1:1
-
-
?
additional information
?
-
-
it is shown that E2 lipoyl domain peptide, LplA and CTD are physically associated. LplA and CTD exist in a ratio 1:1
-
-
?
additional information
?
-
LplA has no detectable ligase activity in vitro in the absence of LplB
-
-
?
additional information
?
-
-
LplA has no detectable ligase activity in vitro in the absence of LplB
-
-
?
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D122A
D122A mutation results in a marked reduction in the overall, lipoate adenylation, and lipoate transfer reaction activities (0.14, 4, and 4% of those of wild type, respectively)
E116A/E312K/L328F
-
mutations allow a LipB knockout strain to grow on a glucose minimal medium
F15S/T101A/S114I
-
mutations allow a LipB knockout strain to grow on a glucose minimal medium
F35L/V113I
-
mutations allow a LipB knockout strain to grow on a glucose minimal medium
G76S
-
substitution in LplA ligase gene, is identical to slr1 selenolipoate restistance mutation
H149A
mutations does not cause a significant reduction in three reaction activities (overall, lipoate adenylation, and lipoate transfer reaction activities), Km value for ATP and lipoic acid increases to 15 and 5.8fold, respectively, relative to those of wild-type
K133A
K133A mutation almost completely abolishes the overall reaction activity (0.01% of that of wild type) and causes marked reduction in lipoate adenylation and lipoate transfer activities (0.2 and 2.5% of that of wild type, respectively)
N121A
N121A affects only the lipoate adenylation activity and consequently the overall reaction activity (1.4 and 0.19% of those of wild-type, respectively) but retains a significant lipoate transfer activity (24.2%)
R140A
-
12fold increase in Km-value for apoH-protein
R58L/H79N
-
mutations allow a LipB knockout strain to grow on a glucose minimal medium
S8T/N63K/F78Y/A110T
-
mutations allow a LipB knockout strain to grow on a glucose minimal medium
S221P
-
mutant with reduced affinity to octanoic acid
S221P
-
strain FH27, referred as lplA11, mutation allows a LipB knockout strain to grow on a glucose minimal medium
S72A
-
great increase in Km-value for ATP
S72A
mutations does not cause a significant reduction in three reaction activities (overall, lipoate adenylation, and lipoate transfer reaction activities), Km value for ATP and lipoic acid increases to 28 and 2.3fold, respectively, relative to those of wild-type
V19L
-
mutant with reduced affinity to octanoic acid
V19L
-
strain FH26, referred as lplA10, mutation allows a LipB knockout strain to grow on a glucose minimal medium
W37V
site-directed mutagenesis
W37V
-
LplAW37V-mediated surface labeling of HEK293T cells with 6-[[(1S,2R,4S)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid and tetrazine-TAMRA, overview. Necessity of a particular chain length to fit the dimensions of the active site of LplAW37V
additional information
enzyme null mutant, normal transport of lipoic acid, but severe defect in incorporation and utilization of exogenously supplied lipoic acid and lipoic acid analogues. Strain is highly resistant to selenolipoate
additional information
-
enzyme null mutant, normal transport of lipoic acid, but severe defect in incorporation and utilization of exogenously supplied lipoic acid and lipoic acid analogues. Strain is highly resistant to selenolipoate
additional information
-
lipB mutant strain, grows well when supplemented with octanoate in place of lipoate
additional information
-
lplA null mutants display no growth defect unless combined with lipA or lipB lipoate synthesis mutations
additional information
-
establishment of an enzyme-mediated two-step labeling protocol suitable for live-cell labeling: construction of a fusion protein LAP-eDHFR-His6, in which eDHFR bears an N-terminal LAP extension and a C-terminal His-tag for purification. In the first step, substrate 6-[[(1S,2R,4S)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid is coupled to purified recombinant LAP-eDHFR. After removal of excess norbornene substrate with centrifugal filter devices, the modified protein is successfully labeled with tetrazine-fluorescein
additional information
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the enzyme is used for a two-step labeling procedure for the attachment of various fluorescent probes to a small peptide sequence (13 amino acids) via enzyme-mediated peptide labeling in combination with palladium-catalyzed Sonogashira cross-coupling, method, overview. 4-Iodophenyl derivatives from a small library can be covalently attached to a lysine residue within a specific 13-amino-acid peptide sequence by Escherichia coli lipoic acid ligase A (LplA). The derivatization with 4-iodophenyl subsequently serves as a reactive handle for bioorthogonal transition metal-catalyzed Sonogashira cross-coupling with alkyne-functionalized fluorophores on both the peptide as well as on the protein level
additional information
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generation of conditional knockout lplA1 mutants. An anhydrotetracycline (ATc)-inducible transcription system is used to generate transgenic Plasmodium berghei parasites in which the lplA1 gene is conditionally knocked out (LplA1-cKO), phenotype, overview. LplA1-cKO parasites shows severely impaired growth in vivo in the first 8 days of infection, and retarded blood-stage development in vitro, in the absence of ATc. But these parasites resume viability in the late stage of infection and mounted high levels of parasitemia leading to the death of the hosts
additional information
generation of conditional knockout lplA1 mutants. An anhydrotetracycline (ATc)-inducible transcription system is used to generate transgenic Plasmodium berghei parasites in which the lplA1 gene is conditionally knocked out (LplA1-cKO), phenotype, overview. LplA1-cKO parasites shows severely impaired growth in vivo in the first 8 days of infection, and retarded blood-stage development in vitro, in the absence of ATc. But these parasites resume viability in the late stage of infection and mounted high levels of parasitemia leading to the death of the hosts
additional information
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generation of conditional knockout lplA1 mutants. An anhydrotetracycline (ATc)-inducible transcription system is used to generate transgenic Plasmodium berghei parasites in which the lplA1 gene is conditionally knocked out (LplA1-cKO), phenotype, overview. LplA1-cKO parasites shows severely impaired growth in vivo in the first 8 days of infection, and retarded blood-stage development in vitro, in the absence of ATc. But these parasites resume viability in the late stage of infection and mounted high levels of parasitemia leading to the death of the hosts
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additional information
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knockout of Plasmodium falciparum LplA1 failed because the protein is essential for growth of parasite
additional information
construction of truncated mutants of enzyme PfLipL1, PfLipL1DELTA259-269, PfLipL1DELTA254-274, and PfLipL1D249-279
additional information
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construction of truncated mutants of enzyme PfLipL1, PfLipL1DELTA259-269, PfLipL1DELTA254-274, and PfLipL1D249-279
additional information
LplA and CTD encoding genes are expressed as fusion proteins in Escherichia coli by omitting the stop codon of lplA and the start codon of ctd. Fusion protein is shown to be catalytically active
additional information
LplA and CTD encoding genes are expressed as fusion proteins in Escherichia coli by omitting the stop codon of lplA and the start codon of ctd. Fusion protein is shown to be catalytically active
additional information
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LplA and CTD encoding genes are expressed as fusion proteins in Escherichia coli by omitting the stop codon of lplA and the start codon of ctd. Fusion protein is shown to be catalytically active
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Zhao, X.; Miller, J.R.; Jiang, Y.; Marletta, M.A.; Cronan, J.E.
Assembly of the covalent linkage between lipoic acid and its cognate enzymes
Chem. Biol.
10
1293-1302
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
brenda
Green, D.E.; Morris, T.W.; Green, J.; Cronan, J.E., Jr.; Guest, J.R.
Purification and properties of the lipoate protein ligase of Escherichia coli
Biochem. J.
309
853-862
1995
Escherichia coli
brenda
Brookfield, D.E.; Green, J.; Ali, S.T.; Machado, R.S.; Guest, J.R.
Evidence for two protein-lipoylation activities in Escherichia coli
FEBS Lett.
295
13-16
1991
Escherichia coli
brenda
Morris, T.W.; Reed, K.E.; Cronan, J.E., Jr.
Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein
J. Bacteriol.
177
1-10
1995
Escherichia coli
brenda
Morris, T.W.; Reed, K.E.; Cronan, J.E., Jr.
Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product
J. Biol. Chem.
269
16091-16100
1994
Escherichia coli (P32099), Escherichia coli
brenda
Fujiwara, K.; Toma, S.; Okamura-Ikeda, K.; Motokawa, Y.; Nakagawa, A.; Taniguchi, H.
Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site
J. Biol. Chem.
280
33645-33651
2005
Escherichia coli
brenda
Kim do, J.; Kim, K.H.; Lee, H.H.; Lee, S.J.; Ha, J.Y.; Yoon, H.J.; Suh, S.W.
Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains
J. Biol. Chem.
280
38081-38089
2005
Thermoplasma acidophilum (Q9HKT1), Thermoplasma acidophilum
brenda
Allary, M.; Lu, J.Z.; Zhu, L.; Prigge, S.T.
Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum
Mol. Microbiol.
63
1331-1344
2007
Plasmodium falciparum
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
brenda
Kang, S.G.; Jeong, H.K.; Lee, E.; Natarajan, S.
Characterization of a lipoate-protein ligase A gene of rice (Oryza sativa L.)
Gene
393
53-61
2007
Oryza sativa
brenda
Keeney, K.M.; Stuckey, J.A.; ORiordan, M.X.
LplA1-dependent utilization of host lipoyl peptides enables Listeria cytosolic growth and virulence
Mol. Microbiol.
66
758-770
2007
Listeria monocytogenes
brenda
Fujiwara, K.; Hosaka, H.; Nakagawa, A.; Motokawa, Y.
Lipoate-protein ligase A: Structure and function
Oxid. Stress Dis.
24
217-233
2008
Escherichia coli, Thermoplasma acidophilum
-
brenda
Posner, M.G.; Upadhyay, A.; Bagby, S.; Hough, D.W.; Danson, M.J.
A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma acidophilum requires two proteins
FEBS J.
276
4012-4022
2009
Thermoplasma acidophilum (Q9HKT1), Thermoplasma acidophilum (Q9HKT2), Thermoplasma acidophilum
brenda
Puthenveetil, S.; Liu, D.S.; White, K.A.; Thompson, S.; Ting, A.Y.
Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase
J. Am. Chem. Soc.
131
16430-16438
2009
Escherichia coli
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
Christensen, Q.H.; Cronan, J.E.
The Thermoplasma acidophilum LplA-LplB complex defines a new class of bipartite lipoate-protein ligases
J. Biol. Chem.
284
21317-21326
2009
Thermoplasma acidophilum (Q9HKT1), Thermoplasma acidophilum
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 berghei, Plasmodium falciparum
brenda
Ramaswamy, A.V.; Maurelli, A.T.
Chlamydia trachomatis serovar L2 can utilize exogenous lipoic acid through the action of the lipoic acid ligase LplA1
J. Bacteriol.
192
6172-6181
2010
Chlamydia trachomatis
brenda
Fujiwara, K.; Maita, N.; Hosaka, H.; Okamura-Ikeda, K.; Nakagawa, A.; Taniguchi, H.
Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A
J. Biol. Chem.
285
9971-9980
2010
Escherichia coli (P32099), Escherichia coli
brenda
Cao, X.; Cronan, J.E.
The Streptomyces coelicolor lipoate-protein ligase is a circularly permuted version of the Escherichia coli enzyme composed of discrete interacting domains
J. Biol. Chem.
290
7280-7290
2015
Streptomyces coelicolor
brenda
Billones, J.; Carrillo, M.; Organo, V.; MacAlino, S.; Emnacen, I.; Sy, J.
Virtual screening against Mycobacterium tuberculosis lipoate protein ligase B (MtbLipB) and in Silico ADMET evaluation of top hits
Orient. J. Chem.
29
1457-1468
2013
Mycobacterium tuberculosis (P9WK83), Mycobacterium tuberculosis ATCC 25618 (P9WK83)
-
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
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
Drake, C.R.; Sevillano, N.; Truillet, C.; Craik, C.S.; VanBrocklin, H.F.; Evans, M.J.
Site-specific radiofluorination of biomolecules with 8-[(18)F]-fluorooctanoic acid catalyzed by lipoic acid ligase
ACS Chem. Biol.
11
1587-1594
2016
Homo sapiens
brenda
Hauke, S.; Best, M.; Schmidt, T.T.; Baalmann, M.; Krause, A.; Wombacher, R.
Two-step protein labeling utilizing lipoic acid ligase and Sonogashira cross-coupling
Bioconjug. Chem.
25
1632-1637
2014
Escherichia coli
brenda
Best, M.; Degen, A.; Baalmann, M.; Schmidt, T.T.; Wombacher, R.
Two-step protein labeling by using lipoic acid ligase with norbornene substrates and subsequent inverse-electron demand Diels-Alder reaction
ChemBioChem
16
1158-1162
2015
Escherichia coli
brenda
Wang, M.; Wang, Q.; Gao, X.; Su, Z.
Conditional knock-out of lipoic acid protein ligase 1 reveals redundancy pathway for lipoic acid metabolism in Plasmodium berghei malaria parasite
Parasit. Vectors
10
315
2017
Plasmodium berghei, Plasmodium berghei (A0A113RHS8), Plasmodium berghei ANKA, Plasmodium berghei ANKA (A0A113RHS8)
brenda
Guerra, A.; Afanador, G.; Prigge, S.
Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum
Proteins
85
1777-1783
2017
Plasmodium falciparum (Q8IEG9), Plasmodium falciparum
brenda
Florian, P.; Petrareanu, G.; Ruta, S.; Roseanu, A.
Optimization of recombinant lipoic acid ligase expression from bacterial cells
Rom. Biotechnol. Lett.
21
11539-11542
2016
Escherichia coli (P32099)
-
brenda