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

• The X-ray structure of the Asp125Ala/Glu127Ala double mutant soaked with chitotetraose shows that, compared with wild-type hevamine, the carbonyl oxygen atom of the N-acetyl group of the -1 sugar residue has rotated away from the C1 atom of that residue [9].
• In the present study, the time courses of the lysozyme-catalyzed reactions with the substrates chitotetraose [(GlcNAc)4], chitopentaose [(GlcNAc)5], and chitohexaose [(GlcNAc)6], of 2-acetamido-2-deoxy-D-glucopyranose (GlcNAc), were obtained experimentally with high-performance liquid chromatography [10].
• Hydrolysis of chitosan with 99% DDA by ChiN released chitobiose, chitotriose and chitotetraose as the major products [11].
• The thermal stability as well as inhibition profiles by the substrate analogues, N-acetylglucosamine (NAG) and chitotetraose (NAG)4 are comparable to those of chicken lysozyme [12].

Gene context of Chitotetrose

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

References