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Gene Review

LYS5  -  Lys5p

Saccharomyces cerevisiae S288c

Synonyms: AASD-PPT, G1867, L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, YGL154C
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Disease relevance of LYS5

  • Recombinant Lys5p expressed in Escherichia coli activates C. albicans Lys2p for the AAR activity and also activates AARs from S. cerevisiae and to a lesser extent Schizosaccharomyces pombe [1].
  • Genes encoding PPTases Sfp and Gsp from Bacillus spp., which are involved in non-ribosomal peptide antibiotic synthesis, complemented the lys5 deletion, whereas ydcB of Bacillus subtilis, which encodes the acyl carrier protein synthase involved in fatty acid synthesis, could not [2].

High impact information on LYS5


Biological context of LYS5


Associations of LYS5 with chemical compounds


Other interactions of LYS5


Analytical, diagnostic and therapeutic context of LYS5

  • Sequence alignment of Lys5p with other PPTases reveals highly conserved putative PPTase domains including the Core 3, WXXKESXXK (residues 194-202) [1].
  • Both LYS1 and LYS5 DNA-specific PCR primers SG1, SG2 and SG3, SG4, respectively, amplified predicted 483 and 648-bp fragments from Candida albicans genomic DNA but not from other selected fungal, bacterial, or human DNA [14].


  1. Molecular characterization of the Candida albicans LYS5 gene and site-directed mutational analysis of the PPTase (Lys5p) domains for lysine biosynthesis. Guo, S., Bhattacharjee, J.K. FEMS Microbiol. Lett. (2003) [Pubmed]
  2. Functional characterization of 4'-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae lys5. Mootz, H.D., Schörgendorfer, K., Marahiel, M.A. FEMS Microbiol. Lett. (2002) [Pubmed]
  3. CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. Adams, A.E., Johnson, D.I., Longnecker, R.M., Sloat, B.F., Pringle, J.R. J. Cell Biol. (1990) [Pubmed]
  4. Cell cycle-dependent induction of mutations along a yeast chromosome. Kee, S.G., Haber, J.E. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  5. IME4, a gene that mediates MAT and nutritional control of meiosis in Saccharomyces cerevisiae. Shah, J.C., Clancy, M.J. Mol. Cell. Biol. (1992) [Pubmed]
  6. Overlapping reading frames at the LYS5 locus in the yeast Yarrowia lipolytica. Xuan, J.W., Fournier, P., Declerck, N., Chasles, M., Gaillardin, C. Mol. Cell. Biol. (1990) [Pubmed]
  7. Cloning and biochemical characterization of LYS5 gene of Saccharomyces cerevisiae. Borell, C.W., Bhattacharjee, J.K. Curr. Genet. (1988) [Pubmed]
  8. Physical and biochemical characterization of the cloned LYS5 gene required for alpha-aminoadipate reductase activity in the lysine biosynthetic pathway of Saccharomyces cerevisiae. Rajnarayan, S., Vaughn, J.C., Bhattacharjee, J.K. Curr. Genet. (1992) [Pubmed]
  9. Positive and negative selection LYS5MX gene replacement cassettes for use in Saccharomyces cerevisiae. Ito-Harashima, S., McCusker, J.H. Yeast (2004) [Pubmed]
  10. Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Ehmann, D.E., Gehring, A.M., Walsh, C.T. Biochemistry (1999) [Pubmed]
  11. alpha-Aminoadipate as a primary nitrogen source for Saccharomyces cerevisiae mutants. Zaret, K.S., Sherman, F. J. Bacteriol. (1985) [Pubmed]
  12. Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe. Guo, S., Bhattacharjee, J.K. Yeast (2004) [Pubmed]
  13. Novel posttranslational activation of the LYS2-encoded alpha-aminoadipate reductase for biosynthesis of lysine and site-directed mutational analysis of conserved amino acid residues in the activation domain of Candida albicans. Guo, S., Evans, S.A., Wilkes, M.B., Bhattacharjee, J.K. J. Bacteriol. (2001) [Pubmed]
  14. Novel lysine biosynthetic gene sequences (LYS1 and LYS5) used as PCR targets for the detection of the pathogenic Candida yeast. Guo, S., Bhattacharjee, J.K. Appl. Microbiol. Biotechnol. (2006) [Pubmed]
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