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Rhamnogalacturonan lyase from Aspergillus aculeatus
Structural highlights
FunctionRGLA_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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves alpha-1,4 glycosidic bonds between L-rhamnose and D-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. The three-dimensional structure of RG-lyase from Aspergillus aculeatus has been determined to 1.5 A resolution representing the first known structure from polysaccharide lyase family 4 and of an enzyme with this catalytic specificity. The 508-amino acid polypeptide displays a unique arrangement of three distinct modular domains. Each domain shows structural homology to non-catalytic domains from other carbohydrate active enzymes. Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4.,McDonough MA, Kadirvelraj R, Harris P, Poulsen JC, Larsen S FEBS Lett. 2004 May 7;565(1-3):188-94. PMID:15135077[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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