The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

lipB  -  octanoyltransferase; octanoyl...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0623, JW5089, cde
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of lipB

  • In the course of these experiments the ATG initiation codon commonly assigned to lipB genes in genomic databases was shown to produce a nonfunctional E. coli LipB protein, whereas initiation at an upstream TTG codon gave a stable and enzymatically active protein [1].
  • An accessory gene, lipB, required for the production of active Pseudomonas glumae lipase [2].
  • The three genes lipB, lipC, and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide [3].
  • Comparisons of the deduced amino acid sequences of the lipB, lipC, and lipD genes with those of the Erwinia chrysanthemi prtDEC, prtEEC, and prtFEC genes encoding the secretion apparatus of the E. chrysanthemi protease showed 55, 46, and 42% identity, respectively [3].
  • A novel gene lipB, which encodes an extracellular lipolytic enzyme, was identified in the Bacillus subtilis genomic DNA sequence [4].
 

High impact information on lipB

 

Chemical compound and disease context of lipB

  • Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein [7].
  • The lipB gene of Escherichia coli encodes an enzyme (LipB) that transfers the octanoyl moiety of octanoyl-acyl carrier protein (octanoyl-ACP) to the lipoyl domains of the 2-oxo acid dehydrogenases and the H subunit of glycine cleavage enzyme [8].
 

Biological context of lipB

 

Anatomical context of lipB

 

Associations of lipB with chemical compounds

  • The lipB-dependent ligase was further shown to cause the accumulation of aberrantly modified octanoyl-proteins in lipoate-deficient cells [7].
  • Cells grown under strictly anaerobic conditions required the lipA and lipB gene products for the synthesis of a functional glycine cleavage system [10].
  • A K. lactis strain carrying a disrupted lipB allele is severely compromised for growth on glycerol medium [14].
 

Other interactions of lipB

  • LipA was assayed for lipoate or lipoyl-ACP formation using E. coli lipoate-protein ligase A (LplA) or lipoyl-[acyl-carrier-protein]-protein-N-lipoyltransferase (LipB), respectively, to lipoylate apo-pyruvate dehydrogenase complex (apo-PDC) [Jordan, S. W., and Cronan, J. E. (1997) Methods Enzymol. 279, 176-183] [15].
  • Thus, lipA and lipB do not encode proteins responsible for diacylglycerophosphatidic acid substitution of the meningococcal capsule polymer; rather, they are required for proper translocation and surface expression of the lipidated polymer [9].
  • Mutants carrying a null mutation in the lipB gene retained a partial ability to synthesize lipoic acid and produced low levels of pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase activities [10].
  • The expression of fusions of lipB fragments with phoA revealed an N(in)-C(out) topology for the LipB protein, which was confirmed by protease accessibility studies on EDTA-permeabilized cells and on inverted inner membrane vesicles [2].
 

Analytical, diagnostic and therapeutic context of lipB

References

  1. The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase. Jordan, S.W., Cronan, J.E. J. Bacteriol. (2003) [Pubmed]
  2. An accessory gene, lipB, required for the production of active Pseudomonas glumae lipase. Frenken, L.G., Bos, J.W., Visser, C., Müller, W., Tommassen, J., Verrips, C.T. Mol. Microbiol. (1993) [Pubmed]
  3. The three genes lipB, lipC, and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide. Akatsuka, H., Kawai, E., Omori, K., Shibatani, T. J. Bacteriol. (1995) [Pubmed]
  4. A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase. Eggert, T., Pencreac'h, G., Douchet, I., Verger, R., Jaeger, K.E. Eur. J. Biochem. (2000) [Pubmed]
  5. Cloning and expression of a cDNA encoding bovine lipoyltransferase. Fujiwara, K., Okamura-Ikeda, K., Motokawa, Y. J. Biol. Chem. (1997) [Pubmed]
  6. Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform. Fujiwara, K., Okamura-Ikeda, K., Motokawa, Y. J. Biol. Chem. (1992) [Pubmed]
  7. Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. Morris, T.W., Reed, K.E., Cronan, J.E. J. Bacteriol. (1995) [Pubmed]
  8. The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate. Zhao, X., Miller, J.R., Cronan, J.E. Biochemistry (2005) [Pubmed]
  9. Translocation and surface expression of lipidated serogroup B capsular Polysaccharide in Neisseria meningitidis. Tzeng, Y.L., Datta, A.K., Strole, C.A., Lobritz, M.A., Carlson, R.W., Stephens, D.S. Infect. Immun. (2005) [Pubmed]
  10. 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]
  11. Characterization of lipase-deficient mutants of Acinetobacter calcoaceticus BD413: identification of a periplasmic lipase chaperone essential for the production of extracellular lipase. Kok, R.G., van Thor, J.J., Nugteren-Roodzant, I.M., Vosman, B., Hellingwerf, K.J. J. Bacteriol. (1995) [Pubmed]
  12. The LipB protein is a negative regulator of dam gene expression in Escherichia coli. Vaisvila, R., Rasmussen, L.J., Lobner-Olesen, A., von Freiesleben, U., Marinus, M.G. Biochim. Biophys. Acta (2000) [Pubmed]
  13. Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids. Wada, M., Yasuno, R., Wada, H. FEBS Lett. (2001) [Pubmed]
  14. Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits. Chen, X.J. Mol. Gen. Genet. (1997) [Pubmed]
  15. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Miller, J.R., Busby, R.W., Jordan, S.W., Cheek, J., Henshaw, T.F., Ashley, G.W., Broderick, J.B., Cronan, J.E., Marletta, M.A. Biochemistry (2000) [Pubmed]
  16. Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase. Wada, M., Yasuno, R., Jordan, S.W., Cronan, J.E., Wada, H. Plant Cell Physiol. (2001) [Pubmed]
 
WikiGenes - Universities