EC Number   |
General Information |
Reference |
|---|
   3.2.1.187 | evolution |
the enzyme belongs to the glycosyl hydrolase family 121, GH121 |
-, 755177 |
| 3.2.1.187 | malfunction |
single deletion mutants of genes XCV2724, XCV2728, and XCV2729 and the triple deletion mutant remain pathogenic, and mutations of the operon or the single genes have no effect on nonhost resistance, indicating that the enzyme is not involved in either pathogenicity or nonhost resistance reactions |
-, 755177 |
| 3.2.1.187 | metabolism |
the enzyme plays a key role in Bifidobacterium longum for beta-L-arabinooligosaccharides usage |
-, 725546 |
| 3.2.1.187 | physiological function |
enzymes XCV2724, XCV2728, and XCV2729 in Xanthomonas euvesicatoria degrade the arabinofuranooligosaccharides present on hydroxyproline (Hyp)-rich glycoproteins (HRGPs) such as extensin and solanaceous lectins in plant cell walls. These enzymes work coordinately to degrade the oligosaccharides. The main oligosaccharide structure of Ara4-Hyp on the HRGPs is degraded to Ara3-Hyp, then to Ara-Hyp, and finally to Ara monosaccharides by the action of these three enzymes. Structure of arabino-oligosaccharides on extensin and solanaceous lectins in plant cell walls, overview. HRGPs containing oligosaccharide substrates have been reported to contribute to plant defense. The enzyme are not involved in either pathogenicity or nonhost resistance reactions |
-, 755177 |
