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Chemical Compound Review

AGN-PC-001GVB     2,6-diaminoheptanedioate

Synonyms: AC1NUTJ4, CHEBI:23671, diaminopimelate, diaminoheptanedioate, (2S,6S)-2,6-diaminoheptanedioate
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Disease relevance of DIAMINOPIMELIC ACID

  • Two recent reports add to the growing list of these pattern-recognition receptors by showing that the intracellular nucleotide-binding oligomerization domain 1 (NOD1) protein recognizes a diaminopimelate-containing muropeptide, a cell-wall component of Gram-negative bacteria [1].
  • An Escherichia coli K12 diaminopimelate auxotroph made invasive by cloning the invasin gene from Yersinia pseudotuberculosis transfers DNA after simple co-incubation, into a variety of mammalian cell lines [2].
  • Here, we present the crystal structures of diaminopimelate (DAP) epimerase from Haemophilus influenzae with two different isomers of the irreversible inhibitor and substrate mimic aziridino-DAP at 1.35- and 1.70-A resolution [3].
  • L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine [4].
  • As a result, meso-lanthionine and L-allo-cystathionine were produced endogenously and incorporated in the peptidoglycan, thereby enabling E. coli strains auxotrophic for diaminopimelate to grow in its absence [5].

High impact information on DIAMINOPIMELIC ACID


Chemical compound and disease context of DIAMINOPIMELIC ACID


Biological context of DIAMINOPIMELIC ACID


Associations of DIAMINOPIMELIC ACID with other chemical compounds




Analytical, diagnostic and therapeutic context of DIAMINOPIMELIC ACID


  1. Detection of peptidoglycans by NOD proteins. Royet, J., Reichhart, J.M. Trends Cell Biol. (2003) [Pubmed]
  2. Functional gene transfer from intracellular bacteria to mammalian cells. Grillot-Courvalin, C., Goussard, S., Huetz, F., Ojcius, D.M., Courvalin, P. Nat. Biotechnol. (1998) [Pubmed]
  3. Structural insights into stereochemical inversion by diaminopimelate epimerase: an antibacterial drug target. Pillai, B., Cherney, M.M., Diaper, C.M., Sutherland, A., Blanchard, J.S., Vederas, J.C., James, M.N. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  4. L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine. McCoy, A.J., Adams, N.E., Hudson, A.O., Gilvarg, C., Leustek, T., Maurelli, A.T. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. Directed evolution of biosynthetic pathways. Recruitment of cysteine thioethers for constructing the cell wall of Escherichia coli. Richaud, C., Mengin-Lecreulx, D., Pochet, S., Johnson, E.J., Cohen, G.N., Marlière, P. J. Biol. Chem. (1993) [Pubmed]
  6. Nod1 participates in the innate immune response to Pseudomonas aeruginosa. Travassos, L.H., Carneiro, L.A., Girardin, S.E., Boneca, I.G., Lemos, R., Bozza, M.T., Domingues, R.C., Coyle, A.J., Bertin, J., Philpott, D.J., Plotkowski, M.C. J. Biol. Chem. (2005) [Pubmed]
  7. Peptidoglycan molecular requirements allowing detection by Nod1 and Nod2. Girardin, S.E., Travassos, L.H., Hervé, M., Blanot, D., Boneca, I.G., Philpott, D.J., Sansonetti, P.J., Mengin-Lecreulx, D. J. Biol. Chem. (2003) [Pubmed]
  8. Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis. Born, T.L., Blanchard, J.S. Current opinion in chemical biology. (1999) [Pubmed]
  9. Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. Chen, N.Y., Jiang, S.Q., Klein, D.A., Paulus, H. J. Biol. Chem. (1993) [Pubmed]
  10. MosA, a protein implicated in rhizopine biosynthesis in Sinorhizobium meliloti L5-30, is a dihydrodipicolinate synthase. Tam, P.H., Phenix, C.P., Palmer, D.R. J. Mol. Biol. (2004) [Pubmed]
  11. Chromosomal location and nucleotide sequence of the Escherichia coli dapA gene. Richaud, F., Richaud, C., Ratet, P., Patte, J.C. J. Bacteriol. (1986) [Pubmed]
  12. An unusual mutation results in the replacement of diaminopimelate with lanthionine in the peptidoglycan of a mutant strain of Mycobacterium smegmatis. Consaul, S.A., Wright, L.F., Mahapatra, S., Crick, D.C., Pavelka, M.S. J. Bacteriol. (2005) [Pubmed]
  13. The three-dimensional structure of the ternary complex of Corynebacterium glutamicum diaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate. Cirilli, M., Scapin, G., Sutherland, A., Vederas, J.C., Blanchard, J.S. Protein Sci. (2000) [Pubmed]
  14. Structural motifs for pyridoxal-5'-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase. Momany, C., Ghosh, R., Hackert, M.L. Protein Sci. (1995) [Pubmed]
  15. Involvement of the relA gene product and feedback inhibition in the regulation of DUP-N-acetylmuramyl-peptide synthesis in Escherichia coli. Ishiguro, E.E., Ramey, W.D. J. Bacteriol. (1978) [Pubmed]
  16. Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene. Stragier, P., Richaud, F., Borne, F., Patte, J.C. J. Mol. Biol. (1983) [Pubmed]
  17. Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum. Scapin, G., Reddy, S.G., Blanchard, J.S. Biochemistry (1996) [Pubmed]
  18. Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase. Scapin, G., Cirilli, M., Reddy, S.G., Gao, Y., Vederas, J.C., Blanchard, J.S. Biochemistry (1998) [Pubmed]
  19. Sulfur and nitrogen limitation in Escherichia coli K-12: specific homeostatic responses. Gyaneshwar, P., Paliy, O., McAuliffe, J., Popham, D.L., Jordan, M.I., Kustu, S. J. Bacteriol. (2005) [Pubmed]
  20. Identification of a lysA-like gene required for tabtoxin biosynthesis and pathogenicity in Pseudomonas syringae pv. tabaci strain PTBR2.024. Engst, K., Shaw, P.D. Mol. Plant Microbe Interact. (1992) [Pubmed]
  21. Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase. Hadfield, A., Shammas, C., Kryger, G., Ringe, D., Petsko, G.A., Ouyang, J., Viola, R.E. Biochemistry (2001) [Pubmed]
  22. Crystal structure of YHI9, the yeast member of the phenazine biosynthesis PhzF enzyme superfamily. Liger, D., Quevillon-Cheruel, S., Sorel, I., Bremang, M., Blondeau, K., Aboulfath, I., Janin, J., van Tilbeurgh, H., Leulliot, N. Proteins (2005) [Pubmed]
  23. Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan. Girardin, S.E., Boneca, I.G., Carneiro, L.A., Antignac, A., Jéhanno, M., Viala, J., Tedin, K., Taha, M.K., Labigne, A., Zähringer, U., Coyle, A.J., DiStefano, P.S., Bertin, J., Sansonetti, P.J., Philpott, D.J. Science (2003) [Pubmed]
  24. Molecular cloning and analysis of nucleotide sequence of the Bacillus subtilis lysA gene region using B. subtilis phage vectors and a multi-copy plasmid, pUB110. Yamamoto, J., Shimizu, M., Yamane, K. Agric. Biol. Chem. (1991) [Pubmed]
  25. Characterization of a bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N-succinyl-L,L-DAP aminotransferase. Fuchs, T.M., Schneider, B., Krumbach, K., Eggeling, L., Gross, R. J. Bacteriol. (2000) [Pubmed]
  26. Analysis of different DNA fragments of Corynebacterium glutamicum complementing dapE of Escherichia coli. Wehrmann, A., Eggeling, L., Sahm, H. Microbiology (Reading, Engl.) (1994) [Pubmed]
  27. A high-performance liquid chromatography method for the simultaneous assay of diaminopimelate epimerase and decarboxylase. Weir, A.N., Bucke, C., Holt, G., Lilly, M.D., Bull, A.T. Anal. Biochem. (1989) [Pubmed]
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