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Gene Review

lipA  -  lipoate synthase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0621, JW0623, lip
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Disease relevance of lipA


High impact information on lipA

  • Recently, one substrate for lipoyl synthase has been shown to be the octanoylated derivative of the lipoyl-bearing subunit (E(2)) of the pyruvate dehydrogenase complex [Zhao, S., Miller, J. R., Jian, Y., Marletta, M. A., and Cronan, J. E., Jr. (2003) Chem. Biol. 10, 1293-1302] [5].
  • Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid [5].
  • Genetic and biochemical studies suggest that lipoyl synthase is a member of a newly established class of metalloenzymes that use S-adenosyl-l-methionine (AdoMet) as a source of a 5'-deoxyadenosyl radical (5'-dA(*)), which is an obligate intermediate in each reaction [5].
  • Chromosomal DNA from the auxotrophs was amplified by PCR using primers derived from the DNA sequence of wild-type lipA and then sequenced [6].
  • Upstream of lipA and in the same orientation, an open reading frame, orfA, is found whose deduced protein sequence (519 amino acids) shows similarity to various membrane-localized transporters [3].

Chemical compound and disease context of lipA


Biological context of lipA

  • The slr-7 mutation, which was mapped to min 15.25 of the chromosome, completely suppressed the lipoate requirement of lipA strains and defined a gene of unknown function in the synthesis of lipoic acid [1].
  • Moreover, quantitative analysis of the lipA transcript by RNase protection assays indicated its down-regulation during entry into stationary phase [2].
  • Two lipase-positive clones were identified; each recombinant plasmid had a 5.2-kb MboI insert that contained the complete lipA gene [3].
  • Downstream of lipA and in the opposite orientation, an open reading frame, orfB (encoding a 199-amino-acid protein) is found, which shows no conspicuous sequence similarity to known proteins, other than an NAD and flavin adenine dinucleotide binding-site sequence [3].
  • Co-expression of lipA with the isc operon approximately trebled the isolated yield of soluble LipA and resulted in efficient assembly of the Fe-S cluster [8].

Associations of lipA with chemical compounds

  • Cells grown under strictly anaerobic conditions required the lipA and lipB gene products for the synthesis of a functional glycine cleavage system [9].
  • Lipoyl(octanoyl)transferase (LipB) transfers the octanoyl chain from ACP to the target lysine acceptor, generating the substrate for lipoyl synthase (LS), which subsequently catalyzes insertion of both sulfur atoms into the C-6 and C-8 positions of the octanoyl chain [10].

Other interactions of lipA

  • The translational initiation site of the lipA gene was established, and the lipB gene product was identified as a 25-kDa protein [9].
  • With the objective of improving soluble holo-LipA expression, a series of multi-cistronic plasmids were constructed carrying lipA in combination with one of the three systems: groE/SL, trxA, or the isc operon [8].

Analytical, diagnostic and therapeutic context of lipA


  1. Mutants of Escherichia coli K-12 that are resistant to a selenium analog of lipoic acid identify unknown genes in lipoate metabolism. Reed, K.E., Morris, T.W., Cronan, J.E. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  2. Cloning and transcriptional analysis of the lipA (lipoic acid synthetase) gene from Rhizobium etli. Taté, R., Riccio, A., Iaccarino, M., Patriarca, E.J. FEMS Microbiol. Lett. (1997) [Pubmed]
  3. Genetic and biochemical characterization of a new extracellular lipase from Streptomyces cinnamomeus. Sommer, P., Bormann, C., Götz, F. Appl. Environ. Microbiol. (1997) [Pubmed]
  4. Engineering of baker's yeasts, E. coli and Bacillus hosts for the production of Bacillus subtilis Lipase A. Sánchez, M., Prim, N., Rández-Gil, F., Pastor, F.I., Diaz, P. Biotechnol. Bioeng. (2002) [Pubmed]
  5. Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. Cicchillo, R.M., Iwig, D.F., Jones, A.D., Nesbitt, N.M., Baleanu-Gogonea, C., Souder, M.G., Tu, L., Booker, S.J. Biochemistry (2004) [Pubmed]
  6. Biosynthesis of lipoic acid: characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9. Hayden, M.A., Huang, I.Y., Iliopoulos, G., Orozco, M., Ashley, G.W. Biochemistry (1993) [Pubmed]
  7. A novel lipase from Pseudomonas fluorescens HU380: gene cloning, overproduction, renaturation-activation, two-step purification, and characterization. Kojima, Y., Kobayashi, M., Shimizu, S. J. Biosci. Bioeng. (2003) [Pubmed]
  8. Effect of iron-sulfur cluster assembly proteins on the expression of Escherichia coli lipoic acid synthase. Kriek, M., Peters, L., Takahashi, Y., Roach, P.L. Protein Expr. Purif. (2003) [Pubmed]
  9. Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes. Reed, K.E., Cronan, J.E. J. Bacteriol. (1993) [Pubmed]
  10. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. 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. Protein Expr. Purif. (2005) [Pubmed]
  11. Molecular cloning of a light-inducible gene (lipA) encoding a novel pilin from Arthrobacter photogonimos. Yang, H.S., Hoober, J.K. FEMS Microbiol. Lett. (1998) [Pubmed]
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