Rhamnogalacturonan exolyase
| Rhamnogalacturonan exolyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.2.24 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Rhamnogalacturonan exolyase (EC 4.2.2.24, YesX) is an enzyme with systematic name α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronate exolyase.[1][2] This enzyme catalyses the following chemical reaction
- Exotype eliminative cleavage of α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosaccharides containing α-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. The products are the disaccharide 2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-Lrhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168.
References
[edit]- ^ Ochiai A, Itoh T, Mikami B, Hashimoto W, Murata K (April 2009). "Structural determinants responsible for substrate recognition and mode of action in family 11 polysaccharide lyases". The Journal of Biological Chemistry. 284 (15): 10181–9. doi:10.1074/jbc.m807799200. PMC 2665072. PMID 19193638.
- ^ Ochiai A, Itoh T, Kawamata A, Hashimoto W, Murata K (June 2007). "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene clusters responsible for rhamnogalacturonan depolymerization". Applied and Environmental Microbiology. 73 (12): 3803–13. Bibcode:2007ApEnM..73.3803O. doi:10.1128/aem.00147-07. PMC 1932723. PMID 17449691.
External links
[edit]- Rhamnogalacturonan+exolyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
