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
Rhamnogalacturonan exolyase | |||||||||
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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 | ||||||||
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- 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 19193638.10181-9&rft.date=2009-04&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2665072#id-name=PMC&rft_id=info:pmid/19193638&rft_id=info:doi/10.1074/jbc.m807799200&rft.aulast=Ochiai&rft.aufirst=A&rft.au=Itoh, T&rft.au=Mikami, B&rft.au=Hashimoto, W&rft.au=Murata, K&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2665072&rfr_id=info:sid/en.wikipedia.org:Rhamnogalacturonan exolyase" class="Z3988">
- ^ 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 17449691.3803-13&rft.date=2007-06&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1932723#id-name=PMC&rft_id=info:pmid/17449691&rft_id=info:doi/10.1128/aem.00147-07&rft_id=info:bibcode/2007ApEnM..73.3803O&rft.aulast=Ochiai&rft.aufirst=A&rft.au=Itoh, T&rft.au=Kawamata, A&rft.au=Hashimoto, W&rft.au=Murata, K&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1932723&rfr_id=info:sid/en.wikipedia.org:Rhamnogalacturonan exolyase" class="Z3988">
External links
edit- Rhamnogalacturonan exolyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)