EC Number   |
General Information |
Reference |
|---|
  3.2.1.200 | physiological function |
chitinase B is predicted to contain two glycoside hydrolase family 18 (GH18) catalytic domains, both of which are catalytically active against chitin. The aminoterminal catalytic domain (GH18N) releases methylumbelliferone from 4'-methylumbelliferyl-N,N'-diacetylchitobiose and releases chitobiose from the nonreducing end of chitooligosaccharides. The C-terminal domain shows endochitinolytic activity. The domains function cooperatively to degrade chitin |
-, 740603 |
| 3.2.1.200 | physiological function |
digestion of beta-chitin by ChiB occurs from the nonreducing end to the reducing end. Chitinases ChiA and ChiB show synergistic interactions in simultaneous degradation of beta-chitin, but not of glycol chitin |
-, 740010 |
| 3.2.1.200 | physiological function |
reactions containing both ChiB and endochitinase ChiC show significantly increased N-acetylglucosamine trimer and dimer formation, but decreased monomer formation, compared to reactions with either enzyme alone. ChiB and ChiC attack different sites and together degrade chitin more efficiently than either enzyme separately. Chitobiase and chitin binding protein in combination with ChiB and ChiC (individually or together) increase their chitinase activity |
-, 741469 |
| 3.2.1.200 | physiological function |
the enzyme has a multidomain structure containing dual catalytic domains and triple chitin-binding domains.The N-terminal catalytic domain mainly hydrolyzes the second glycosidic bond from the nonreducing end of the oligomers, whereas the C-terminal domain randomly hydrolyzes glycosidic bonds other than the first bond from the nonreducing end. Both catalytic domains form diacetylchitobiose as a major end product and possess transglycosylation activity. The N-terminal catalytic domain exclusively liberates diacetylchitobiose, whereas reactions with the C-terminal domain lead to N-acetyl-chitooligosaccharides of various lengths. A synergistic effect is observed when chitin is degraded in the presence of both catalytic domains |
656022 |
| 3.2.1.200 | physiological function |
the enzyme shows antifungal activity against Aspergillus niger and Trichoderma sp. |
750827 |
