6.3.1.20: lipoate-protein ligase
This is an abbreviated version!
For detailed information about lipoate-protein ligase, go to the full flat file.
Word Map on EC 6.3.1.20
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6.3.1.20
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lipoylation
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ligases
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octanoyl-acyl
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lipoate-dependent
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apicoplast
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octanoylation
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2-oxoacids
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lipoyl-amp
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octanoic
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bioorthogonal
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lipoyltransferase
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h-protein
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octanoyltransferase
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13-amino
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biotechnology
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synthesis
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molecular biology
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drug development
- 6.3.1.20
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lipoylation
- ligases
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octanoyl-acyl
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lipoate-dependent
- apicoplast
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octanoylation
- 2-oxoacids
- lipoyl-amp
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octanoic
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bioorthogonal
- lipoyltransferase
- h-protein
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octanoyltransferase
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13-amino
- biotechnology
- synthesis
- molecular biology
- drug development
Reaction
Synonyms
CTD, EC 2.7.7.63, LIP3, LipB, LipL1, lipoate ligase, lipoate ligase like protein, lipoate protein ligase, lipoate protein ligase B, lipoate-bound lipoate ligase 1, lipoate-protein ligase, lipoate-protein ligase A, lipoic acid ligase, lipoic acid ligase A, lipoic acid protein ligase, lipoic acid protein ligase A1, lipoyl ligase, lipoyl-protein ligase A, LPLA, LplA-LplB complex, LplA1, LplA1Ct, Lpla2, LplB, Oryza s. lipoate-protein ligase A, OsLPLA, PfLipL1
ECTree
6.3.1.20 lipoate-protein ligaseAdvanced search results
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results (Engineering
Engineering on EC 6.3.1.20 - lipoate-protein ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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mutations allow a LipB knockout strain to grow on a glucose minimal medium
F15S/T101A/S114I
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mutations allow a LipB knockout strain to grow on a glucose minimal medium
F35L/V113I
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mutations allow a LipB knockout strain to grow on a glucose minimal medium
G76S
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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%)
R58L/H79N
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mutations allow a LipB knockout strain to grow on a glucose minimal medium
S221P
S72A
S8T/N63K/F78Y/A110T
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mutations allow a LipB knockout strain to grow on a glucose minimal medium
V19L
W37V
additional information
S221P
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strain FH27, referred as lplA11, mutation allows a LipB knockout strain to grow on a glucose minimal medium
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
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strain FH26, referred as lplA10, mutation allows a LipB knockout strain to grow on a glucose minimal medium
W37V
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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
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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
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lipB mutant strain, grows well when supplemented with octanoate in place of lipoate
additional information
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lplA null mutants display no growth defect unless combined with lipA or lipB lipoate synthesis mutations
additional information
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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
