<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>289(38)</volume><submitter>Roston RL</submitter><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>26089-26106</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4176223</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Structural determinants allowing transferase activity in SENSITIVE TO FREEZING 2, classified as a family I glycosyl hydrolase.</pubmed_title><pmcid>PMC4176223</pmcid><pubmed_authors>Kuhn LA</pubmed_authors><pubmed_authors>Roston RL</pubmed_authors><pubmed_authors>Benning C</pubmed_authors><pubmed_authors>Wang K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structural determinants allowing transferase activity in SENSITIVE TO FREEZING 2, classified as a family I glycosyl hydrolase.</name><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</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Sep</publication><modification>2026-05-04T23:34:14.321Z</modification><creation>2019-03-27T01:36:31Z</creation></dates><accession>S-EPMC4176223</accession><cross_references><pubmed>25100720</pubmed><doi>10.1074/jbc.m114.576694</doi><doi>10.1074/jbc.M114.576694</doi></cross_references></HashMap>