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Chemical Compound Review

Chitotetrose     (2R,3R,4R,5R)-2-amino-3,4,5- tris[[(2S,3R...

Synonyms: Chitotetraose, Chitintetraose, AC1MIVD3
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Disease relevance of Chitotetrose

  • The effect can be mimicked by a chitotetraose or chitinase from Streptomyces griseus [1].
  • This enzyme was found to be active in E. coli cultured at 18 degrees C but not 37 degrees C. NodH could also transfer the sulphate group from PAPS to a model substrate, tetra-N-acetyl chitotetraose, with apparent Km values of 56 and 70 microM respectively, and exhibited an apparent Km value for non-sulphated Nod factors of 28 microM [2].

High impact information on Chitotetrose

  • Amelogenin agglutination of murine erythrocytes was specifically inhibited by N-acetylglucosamine (GlcNAc), chitobiose, and chitotetraose and by ovalbumin with terminal GlcNAc [3].
  • Chit A also had a 10-fold lower binding constant (Kd) against the substrate analogue N,N',N'',N'''-tetraacetyl chitotetrose than Chit B, indicating that the two enzyme may differ in their affinities for binding to the substrate chitin [4].
  • The chain length of the oligosaccharide was important in feedback regulation, with chitotetraose molecules the best modulators of nod gene expression [5].
  • Three novel nodulation (Nod) factors were synthesized from chitotetraose and three structurally different fluorescent BODIPY-tagged fatty acids [6].
  • A novel bioactive fluorescent nodulation (Nod) factor, NodRlv-IV(BODIPY FL-C16), has been synthesized by attaching a BODIPY FL-C16 acyl chain to the primary amino group of chitotetraose deacetylated at the nonreducing terminus by recombinant NodB [7].

Biological context of Chitotetrose

  • High-performance liquid chromatography analysis of the hydrolysis products from N-acetyl chitotetraose revealed that chitinase C-1 catalyzes hydrolysis of the glycosidic bond with inversion of the anomeric configuration, in agreement with the previously reported inverting mechanism of plant class I chitinases [8].

Associations of Chitotetrose with other chemical compounds


Gene context of Chitotetrose

  • The clearest difference was observed between strains with R. meliloti and R. loti NodC, producing chitintetraose and chitinpentaose, respectively [13].


  1. Endogenous Nod-factor-like signal molecules promote early somatic embryo development in Norway spruce. Dyachok, J.V., Wiweger, M., Kenne, L., von Arnold, S. Plant Physiol. (2002) [Pubmed]
  2. Enzymatic radiolabelling to a high specific activity of legume lipo-oligosaccharidic nodulation factors from Rhizobium meliloti. Bourdineaud, J.P., Bono, J.J., Ranjeva, R., Cullimore, J.V. Biochem. J. (1995) [Pubmed]
  3. Tyrosyl motif in amelogenins binds N-acetyl-D-glucosamine. Ravindranath, R.M., Moradian-Oldak, J., Fincham, A.G. J. Biol. Chem. (1999) [Pubmed]
  4. Antifungal proteins from plants. Purification, molecular cloning, and antifungal properties of chitinases from maize seed. Huynh, Q.K., Hironaka, C.M., Levine, E.B., Smith, C.E., Borgmeyer, J.R., Shah, D.M. J. Biol. Chem. (1992) [Pubmed]
  5. Feedback regulation of the Bradyrhizobium japonicum nodulation genes. Loh, J.T., Stacey, G. Mol. Microbiol. (2001) [Pubmed]
  6. Nod factors integrate spontaneously in biomembranes and transfer rapidly between membranes and to root hairs, but transbilayer flip-flop does not occur. Goedhart, J., Röhrig, H., Hink, M.A., van Hoek, A., Visser, A.J., Bisseling, T., Gadella, T.W. Biochemistry (1999) [Pubmed]
  7. Microspectroscopic imaging of nodulation factor-binding sites on living Vicia sativa roots using a novel bioactive fluorescent nodulation factor. Gadella, T.W., Vereb, G., Hadri, A.E., Röhrig, H., Schmidt, J., John, M., Schell, J., Bisseling, T. Biophys. J. (1997) [Pubmed]
  8. A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037. Ohno, T., Armand, S., Hata, T., Nikaidou, N., Henrissat, B., Mitsutomi, M., Watanabe, T. J. Bacteriol. (1996) [Pubmed]
  9. Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis. Bokma, E., Rozeboom, H.J., Sibbald, M., Dijkstra, B.W., Beintema, J.J. Eur. J. Biochem. (2002) [Pubmed]
  10. Substrate size dependence of lysozyme-catalyzed reaction. Fukamizo, T., Minematsu, T., Yanase, Y., Hayashi, K., Goto, S. Arch. Biochem. Biophys. (1986) [Pubmed]
  11. Purification and Characterization of Two Types of Chitosanase from a Microbacterium sp. Sun, Y., Liu, W., Han, B., Zhang, J., Liu, B. Biotechnol. Lett. (2006) [Pubmed]
  12. Electrophoretic polymorphism in rabbit tear lysozyme. Saleh, A.M., Ibrahimi, I.M. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1995) [Pubmed]
  13. Rhizobium nodulation protein NodC is an important determinant of chitin oligosaccharide chain length in Nod factor biosynthesis. Kamst, E., Pilling, J., Raamsdonk, L.M., Lugtenberg, B.J., Spaink, H.P. J. Bacteriol. (1997) [Pubmed]
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