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by | Mar 16, 2018 | Hosta

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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. ^ Petersen TN, Kauppinen S, Larsen S (April 1997). "The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix". Structure. 5 (4): 533–44. doi:10.1016/s0969-2126(97)00209-8. PMID 9115442.
  2. ^ Kofod LV, Kauppinen S, Christgau S, Andersen LN, Heldt-Hansen HP, Dörreich K, Dalbøge H (November 1994). "Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus". The Journal of Biological Chemistry. 269 (46): 29182–9. PMID 7961884.
  3. ^ Azadi P, O'Neill MA, Bergmann C, Darvill AG, Albersheim P (December 1995). "The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase". Glycobiology. 5 (8): 783–9. doi:10.1093/glycob/5.8.783. PMID 8720076.
  4. ^ Petersen TN, Christgau S, Kofod LV, Kauppinen S, Johnson AH, Larsen S (January 1997). "Crystallization and preliminary X-ray studies of rhamnogalacturonase A from Aspergillus aculeatus". Acta Crystallographica Section D. 53 (Pt 1): 105–7. doi:10.1107/s0907444996010785. PMID 15299976.
  5. ^ Pitson SM, Mutter M, van den Broek LA, Voragen AG, Beldman G (January 1998). "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. doi:10.1006/bbrc.1997.8009. PMID 9464254.

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