Production and chitinase-binding ability of lipo-chitopentaose nodulation factor.
The penta-N-acetyl-chitopentaose 2 has been prepared by using recombinant E. coli strains harboring the nodC gene (encoding chitooligosaccharide synthase) from Azorhizobium caulinodans. Then, the deacetylase NodB removed the N-acetyl moiety from the nonreducing terminus of 2 to give tetra-N-acetyl-chitopentaose 3. N-Acylation of 3 with stearyl chloride was performed in DMF containing water and provided the corresponding lipo-chitopentaose nodulation factor 4. A binding chitinase assay indicated that 4 was much more stable than 3.
Huang
Gang-Liang
GL
State Key Laboratory of Microbial Technology (SKLMT), Shandong University, Jinan, Shandong 250100, People's Republic of China. hgl226@126.com
Mei
Xin-Ya
XY
D000215:Acylation; D000581:Amidohydrolases / Q000737:chemistry; D020599:Azorhizobium caulinodans / Q000201:enzymology / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry; D002688:Chitinases / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D005818:Genetic Engineering / Q000379:methods; D005960:Glucosides / Q000096:biosynthesis; D017351:N-Acetylglucosaminyltransferases / Q000235:genetics / Q000378:metabolism; D009844:Oligosaccharides / Q000096:biosynthesis* / Q000737:chemistry*
D001426:Bacterial Proteins; D005960:Glucosides; D009844:Oligosaccharides; C520972:lipo-chitopentaose nodulation factor; C511150:penta-N-acetyl-chitopentaose; C073606:nodB protein, Bacteria; D017351:N-Acetylglucosaminyltransferases; D002688:Chitinases; D000581:Amidohydrolases