{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["289(38)"],"submitter":["Roston RL"],"pubmed_abstract":["SENSITIVE TO FREEZING 2 (SFR2) is classified as a family I glycosyl hydrolase but has recently been shown to have galactosyltransferase activity in Arabidopsis thaliana. Natural occurrences of apparent glycosyl hydrolases acting as transferases are interesting from a biocatalysis standpoint, and knowledge about the interconversion can assist in engineering SFR2 in crop plants to resist freezing. To understand how SFR2 evolved into a transferase, the relationship between its structure and function are investigated by activity assay, molecular modeling, and site-directed mutagenesis. SFR2 has no detectable hydrolase activity, although its catalytic site is highly conserved with that of family 1 glycosyl hydrolases. Three regions disparate from glycosyl hydrolases are identified as required f"],"journal":["The Journal of biological chemistry"],"pagination":["26089-26106"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4176223"],"repository":["biostudies-literature"],"pubmed_title":["Structural determinants allowing transferase activity in SENSITIVE TO FREEZING 2, classified as a family I glycosyl hydrolase."],"pmcid":["PMC4176223"],"pubmed_authors":["Kuhn LA","Roston RL","Benning C","Wang K"],"additional_accession":[]},"is_claimable":false,"name":"Structural determinants allowing transferase activity in SENSITIVE TO FREEZING 2, classified as a family I glycosyl hydrolase.","description":"SENSITIVE TO FREEZING 2 (SFR2) is classified as a family I glycosyl hydrolase but has recently been shown to have galactosyltransferase activity in Arabidopsis thaliana. Natural occurrences of apparent glycosyl hydrolases acting as transferases are interesting from a biocatalysis standpoint, and knowledge about the interconversion can assist in engineering SFR2 in crop plants to resist freezing. To understand how SFR2 evolved into a transferase, the relationship between its structure and function are investigated by activity assay, molecular modeling, and site-directed mutagenesis. SFR2 has no detectable hydrolase activity, although its catalytic site is highly conserved with that of family 1 glycosyl hydrolases. Three regions disparate from glycosyl hydrolases are identified as required f","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Sep","modification":"2026-05-04T23:34:14.321Z","creation":"2019-03-27T01:36:31Z"},"accession":"S-EPMC4176223","cross_references":{"pubmed":["25100720"],"doi":["10.1074/jbc.m114.576694","10.1074/jbc.M114.576694"]}}