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3njv

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Template:STRUCTURE 3njv

Contents

Rhamnogalacturonan lyase from Aspergillus aculeatus K150A substrate complex

Template:ABSTRACT PUBMED 20851126

Function

[RHGB_ASPAC] Pectinolytic enzyme that has a positive effect in the apple hot-mash liquefaction process. This endolyase hydrolyzes the alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage by beta-elimination, thereby generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.[1] [2] [3]

About this Structure

3njv is a 1 chain structure with sequence from Aspergillus aculeatus. Full crystallographic information is available from OCA.

Reference

  • Jensen MH, Otten H, Christensen U, Borchert TV, Christensen LL, Larsen S, Leggio LL. Structural and Biochemical Studies Elucidate the Mechanism of Rhamnogalacturonan Lyase from Aspergillus aculeatus. J Mol Biol. 2010 Sep 17. PMID:20851126 doi:10.1016/j.jmb.2010.09.013
  1. ↑ Mutter M, Colquhoun IJ, Schols HA, Beldman G, Voragen AG. Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan alpha-L-rhamnopyranosyl-(1-->4)-alpha-D-galactopyranosyluronide lyase. Plant Physiol. 1996 Jan;110(1):73-7. PMID:8587995
  2. ↑ Mutter M, Colquhoun IJ, Beldman G, Schols HA, Bakx EJ, Voragen AG. 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 Physiol. 1998 May;117(1):141-52. PMID:9576783
  3. ↑ Jensen MH, Otten H, Christensen U, Borchert TV, Christensen LL, Larsen S, Leggio LL. Structural and Biochemical Studies Elucidate the Mechanism of Rhamnogalacturonan Lyase from Aspergillus aculeatus. J Mol Biol. 2010 Sep 17. PMID:20851126 doi:10.1016/j.jmb.2010.09.013

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