chitotetrose and allosamidin

chitotetrose has been researched along with allosamidin* in 1 studies

Other Studies

1 other study(ies) available for chitotetrose and allosamidin

Article	Year
Enzyme kinetics of hevamine, a chitinase from the rubber tree Hevea brasiliensis. FEBS letters, 2000, Jul-28, Volume: 478, Issue:1-2 The enzyme kinetics of hevamine, a chitinase from the rubber tree Hevea brasiliensis, were studied in detail with a new enzyme assay. In this assay, the enzyme reaction products were derivatized by reductive coupling to a chromophore. Products were separated by HPLC and the amount of product was calculated by peak integration. Penta-N-acetylglucosamine (penta-nag) and hexa-N-acetylglucosamine (hexa-nag) were used as substrates. Hexa-nag was more efficiently converted than penta-nag, which is an indication that hevamine has at least six sugar binding sites in the active site. Tetra-N-acetylglucosamine (tetra-nag) and allosamidin were tested as inhibitors. Allosamidin was found to be a competitive inhibitor with a K(i) of 3.1 microM. Under the conditions tested, tetra-nag did not inhibit hevamine. Topics: Acetylglucosamine; Binding, Competitive; Chitinases; Chromatography, High Pressure Liquid; Coloring Agents; Euphorbiaceae; Kinetics; Muramidase; Oligosaccharides; Oxidation-Reduction; Plant Proteins; Thermodynamics; Trisaccharides	2000

Article

Year

Enzyme kinetics of hevamine, a chitinase from the rubber tree Hevea brasiliensis.

FEBS letters, 2000, Jul-28, Volume: 478, Issue:1-2

The enzyme kinetics of hevamine, a chitinase from the rubber tree Hevea brasiliensis, were studied in detail with a new enzyme assay. In this assay, the enzyme reaction products were derivatized by reductive coupling to a chromophore. Products were separated by HPLC and the amount of product was calculated by peak integration. Penta-N-acetylglucosamine (penta-nag) and hexa-N-acetylglucosamine (hexa-nag) were used as substrates. Hexa-nag was more efficiently converted than penta-nag, which is an indication that hevamine has at least six sugar binding sites in the active site. Tetra-N-acetylglucosamine (tetra-nag) and allosamidin were tested as inhibitors. Allosamidin was found to be a competitive inhibitor with a K(i) of 3.1 microM. Under the conditions tested, tetra-nag did not inhibit hevamine.

Topics: Acetylglucosamine; Binding, Competitive; Chitinases; Chromatography, High Pressure Liquid; Coloring Agents; Euphorbiaceae; Kinetics; Muramidase; Oligosaccharides; Oxidation-Reduction; Plant Proteins; Thermodynamics; Trisaccharides

2000