{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Al-Hinai TZS"],"funding":["Ministry of Higher Education","Biotechnology and Biological Sciences Research Council"],"pagination":["547-558"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11037484"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["133(4)"],"pubmed_abstract":["<h4>Background and aims</h4>The softening of ripening fruit involves partial depolymerization of cell-wall pectin by three types of reaction: enzymic hydrolysis, enzymic elimination (lyase-catalysed) and non-enzymic oxidative scission. Two known lyase activities are pectate lyase and rhamnogalacturonan lyase (RGL), potentially causing mid-chain cleavage of homogalacturonan and rhamnogalacturonan-I (RG-I) domains of pectin respectively. However, the important biological question of whether RGL exhibits action in vivo had not been tested.<h4>Methods</h4>We developed a method for specifically and sensitively detecting in-vivo RGL products, based on Driselase digestion of cell walls and detection of a characteristic unsaturated 'fingerprint' product (tetrasaccharide) of RGL action.<h4>Key resu"],"journal":["Annals of botany"],"pubmed_title":["Fruit softening: evidence for rhamnogalacturonan lyase action in vivo in ripe fruit cell walls."],"pmcid":["PMC11037484"],"funding_grant_id":["BB/N002458/1"],"pubmed_authors":["Mackay CL","Fry SC","Al-Hinai TZS"],"additional_accession":[]},"is_claimable":false,"name":"Fruit softening: evidence for rhamnogalacturonan lyase action in vivo in ripe fruit cell walls.","description":"<h4>Background and aims</h4>The softening of ripening fruit involves partial depolymerization of cell-wall pectin by three types of reaction: enzymic hydrolysis, enzymic elimination (lyase-catalysed) and non-enzymic oxidative scission. Two known lyase activities are pectate lyase and rhamnogalacturonan lyase (RGL), potentially causing mid-chain cleavage of homogalacturonan and rhamnogalacturonan-I (RG-I) domains of pectin respectively. However, the important biological question of whether RGL exhibits action in vivo had not been tested.<h4>Methods</h4>We developed a method for specifically and sensitively detecting in-vivo RGL products, based on Driselase digestion of cell walls and detection of a characteristic unsaturated 'fingerprint' product (tetrasaccharide) of RGL action.<h4>Key resu","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2025-04-26T23:12:36.54Z","creation":"2025-04-06T17:31:15.582Z"},"accession":"S-EPMC11037484","cross_references":{"pubmed":["38180460"],"doi":["10.1093/aob/mcad197"]}}