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lipoyl(octanoyl) transferase activity

Known as: lipoyl (octanoyl)-acyl carrier protein:protein transferase activity, octanoyl-acyl-carrier-protein-protein N-octanoyltransferase activity, octanoyl-acyl carrier protein-protein N-octanoyltransferase activity 
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein. [EC:2.3.1.181]
National Institutes of Health

Papers overview

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2018
2018
  • Gertie van Pouderoyenb, Bauke W. Dijkstrab, Erich Jaegera
  • 2018
  • Corpus ID: 3863319
Bacillus subtilis secretes the lipolytic enzymes LipA and LipB. We show here that they are differentially expressed depending on… Expand
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2009
2009
LipA and LipB of Thermosyntropha lipolytica DSM 11003 as previously published are the most alkalithermophilic (pHopt25°C = 9.4–9… Expand
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2007
2007
Two thermostable lipases were isolated and characterized from Thermosyntropha lipolytica DSM 11003, an anaerobic, thermophilic… Expand
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2005
2005
The capsule of N. meningitidis serogroup B, (alpha2-->8)-linked polysialic acid and the capsules of other meningococcal… Expand
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2001
2001
Bacillus subtilis secretes the lipolytic enzymes LipA and LipB. We show here that they are differentially expressed depending on… Expand
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Highly Cited
2000
Highly Cited
2000
The Escherichia coli lipA gene product has been genetically linked to carbon-sulfur bond formation in lipoic acid biosynthesis… Expand
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Highly Cited
1995
Highly Cited
1995
Lipoic acid is a covalently bound disulfide-containing cofactor required for function of the pyruvate dehydrogenase, alpha… Expand
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Highly Cited
1993
Highly Cited
1993
Pseudomonas glumae PG1 is able to secrete lipase into the extracellular medium. The lipase is produced as a precursor protein… Expand
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1993
1993
The LipB protein of Pseudomonas glumae is essential for the production of active extracellular lipase encoded by the lipA gene… Expand
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1986
1986
Li(17)Pb(83) and LiPb were prepared from the pure elements in amounts of severa1 hundred grams. The reso1idified samp1es were… Expand
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