Rhamnogalacturonan exolyase

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Rhamnogalacturonan exolyase
Identifiers
EC no.4.2.2.24
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IntEnzIntEnz view
BRENDABRENDA entry
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NCBIproteins

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

  1. ^ 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.
  2. ^ 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.

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