Inhibition of two family 18 chitinases by various allosamidin derivatives
✍ Scribed by Spindler-Barth, Margarethe; Blattner, Regine; Vorgias, Constantine E.; Spindler, Klaus Dieter
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 328 KB
- Volume
- 52
- Category
- Article
- ISSN
- 1526-498X
No coin nor oath required. For personal study only.
✦ Synopsis
The inhibitory activities of several allosamidin derivatives on two family 18 chitinases, an insect enzyme from the epithelial cell line from Chironomus tentans, and a bacterial enzyme, chitinase A from Serratia marcescens, were evaluated. The following structural requirements are necessary for inhibition of the Chironomus enzyme :
- One N-acetylallosamine residue can be omitted without impairment of enzyme inhibition. 2. At least one N-acetylallosamine sugar must be present. 3. Glucosamine can replace the allosamine moiety without a negative e †ect on the inhibitory activity. 4. The spatial arrangement of the allosamizoline moiety is important for inhibition. 5. If one sugar is omitted and the arrangement of the cyclitol residue is changed, the inhibitory e †ect is diminished further.
For puriÐed chitinase A from Serratia marcescens the arrangement of the aglycone moiety is equally important, but recognition of the sugar is di †erent :
- Omission of one allosamine residue decreases the inhibitory activity considerably. 2. Inhibition is improved if the remaining N-acetylallosamine is replaced by the epimer N-acetylglucosamine.
Only endochitinase activity is a †ected, since chitin formation (up to 10~4 M) and N-acetylglucosaminidase activity (up to 10~3 M) are not impaired, at least in Chironomus cells.