Biology:Rhamnogalacturonan hydrolase

From HandWiki
Revision as of 01:15, 11 February 2024 by Jslovo (talk | contribs) (update)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Rhamnogalacturonan hydrolase
Identifiers
EC number3.2.1.171
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Rhamnogalacturonan hydrolase (EC 3.2.1.171, rhamnogalacturonase A, RGase A, RG-hydrolase) is an enzyme with systematic name rhamnogalacturonan alpha-D-GalA-(1->2)-alpha-L-Rha hydrolase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end.

The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus.

References

  1. "The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix". Structure 5 (4): 533–44. April 1997. doi:10.1016/s0969-2126(97)00209-8. PMID 9115442. 
  2. "Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus". The Journal of Biological Chemistry 269 (46): 29182–9. November 1994. PMID 7961884. 
  3. "The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase". Glycobiology 5 (8): 783–9. December 1995. doi:10.1093/glycob/5.8.783. PMID 8720076. 
  4. "Crystallization and preliminary X-ray studies of rhamnogalacturonase A from Aspergillus aculeatus". Acta Crystallographica Section D 53 (Pt 1): 105–7. January 1997. doi:10.1107/s0907444996010785. PMID 15299976. 
  5. "Stereochemical course of hydrolysis catalysed by alpha-L-rhamnosyl and alpha-D-galacturonosyl hydrolases from Aspergillus aculeatus". Biochemical and Biophysical Research Communications 242 (3): 552–9. January 1998. doi:10.1006/bbrc.1997.8009. PMID 9464254. 

External links