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Rhamnogalacturonan endolyase
Identifiers
EC no.4.2.2.23
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The enzyme Rhamnogalacturonan endolyase (EC 4.2.2.23, rhamnogalacturonase B, α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronide lyase, Rgase B, rhamnogalacturonan α-Lrhamnopyranosyl-(1,4)-α-D-galactopyranosyluronide lyase, RG-lyase, YesW, RGL4, Rgl11A, Rgl11Y, RhiE) is an enzyme with systematic name α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronate endolyase.[1][2][3][4][5][6][7][8] catalyses the following process:

Endotype eliminative cleavage of L-α-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated Dgalactopyranosyluronic acid at the non-reducing end.

The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168 and Aspergillus aculeatus.

References

  1. ^ Mutter M, Colquhoun IJ, Schols HA, Beldman G, Voragen AG (January 1996). "Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan alpha-L-rhamnopyranosyl-(1-->4)-alpha-D-galactopyranosyluronide lyase". Plant Physiology. 110 (1): 73–7. doi:10.1104/pp.110.1.73. PMC 157695. PMID 8587995.
  2. ^ 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.
  3. ^ Mutter M, Colquhoun IJ, Beldman G, Schols HA, Bakx EJ, Voragen AG (May 1998). "Characterization of recombinant rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase from Aspergillus aculeatus. An enzyme that fragments rhamnogalacturonan I regions of pectin". Plant Physiology. 117 (1): 141–52. doi:10.1104/pp.117.1.141. PMC 34997. PMID 9576783.
  4. ^ Kadirvelraj R, Harris P, Poulsen JC, Kauppinen S, Larsen S (August 2002). "A stepwise optimization of crystals of rhamnogalacturonan lyase from Aspergillus aculeatus". Acta Crystallographica Section D. 58 (Pt 8): 1346–9. doi:10.1107/s0907444902009137. PMID 12136151.
  5. ^ Laatu M, Condemine G (March 2003). "Rhamnogalacturonate lyase RhiE is secreted by the out system in Erwinia chrysanthemi". Journal of Bacteriology. 185 (5): 1642–9. doi:10.1128/jb.185.5.1642-1649.2003. PMC 148073. PMID 12591882.
  6. ^ Pagès S, Valette O, Abdou L, Bélaïch A, Bélaïch JP (August 2003). "A rhamnogalacturonan lyase in the Clostridium cellulolyticum cellulosome". Journal of Bacteriology. 185 (16): 4727–33. doi:10.1128/jb.185.16.4727-4733.2003. PMC 166469. PMID 12896991.
  7. ^ Ochiai A, Yamasaki M, Itoh T, Mikami B, Hashimoto W, Murata K (May 2006). "Crystallization and preliminary X-ray analysis of the rhamnogalacturonan lyase YesW from Bacillus subtilis strain 168, a member of polysaccharide lyase family 11". Acta Crystallographica Section F. 62 (Pt 5): 438–40. doi:10.1107/s1744309106011894. PMC 2219969. PMID 16682770.
  8. ^ Jensen MH, Otten H, Christensen U, Borchert TV, Christensen LL, Larsen S, Leggio LL (November 2010). "Structural and biochemical studies elucidate the mechanism of rhamnogalacturonan lyase from Aspergillus aculeatus". Journal of Molecular Biology. 404 (1): 100–11. doi:10.1016/j.jmb.2010.09.013. PMID 20851126.

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Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
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