| http://purl.uniprot.org/citations/20851126 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20851126 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20851126 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/20851126 | http://www.w3.org/2000/01/rdf-schema#comment | "We present here the first experimental evidence for bound substrate in the active site of a rhamnogalacturonan lyase belonging to family 4 of polysaccharide lyases, Aspergillus aculeatus rhamnogalacturonan lyase (RGL4). RGL4 is involved in the degradation of rhamnogalacturonan-I, an important pectic plant cell wall polysaccharide. Based on the previously determined wild-type structure, enzyme variants RGL4_H210A and RGL4_K150A have been produced and characterized both kinetically and structurally, showing that His210 and Lys150 are key active-site residues. Crystals of the RGL4_K150A variant soaked with a rhamnogalacturonan digest gave a clear picture of substrate bound in the -3/+3 subsites. The crystallographic and kinetic studies on RGL4, and structural and sequence comparison to other enzymes in the same and other PL families, enable us to propose a detailed reaction mechanism for the β-elimination on [-,2)-α-l-rhamno-(1,4)-α-d-galacturonic acid-(1,-]. The mechanism differs significantly from the one established for pectate lyases, in which most often calcium ions are engaged in catalysis."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2010.09.013"xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2010.09.013"xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Jensen M.H."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Jensen M.H."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Leggio L.L."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Leggio L.L."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Borchert T.V."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Borchert T.V."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Christensen U."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Christensen U."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Larsen S."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Larsen S."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Otten H."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Otten H."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Christensen L.L."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/author | "Christensen L.L."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/20851126 | http://purl.uniprot.org/core/pages | "100-111"xsd:string |