{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["70(48)"],"submitter":["Pijning T"],"funding":["Royal Avebe","Rijksuniversiteit Groningen"],"pubmed_abstract":["GtfC-type 4,6-α-glucanotransferase (α-GT) enzymes from Glycoside Hydrolase Family 70 (GH70) are of interest for the modification of starch into low-glycemic index food ingredients. Compared to the related GH70 GtfB-type α-GTs, found exclusively in lactic acid bacteria (LAB), GtfCs occur in non-LAB, share low sequence identity, lack circular permutation of the catalytic domain, and feature a single-segment auxiliary domain IV and auxiliary C-terminal domains. Despite these differences, the first crystal structure of a GtfC, GbGtfC-ΔC from <i>Geobacillus</i> 12AMOR1, and the first one representing a non-permuted GH70 enzyme, reveals high structural similarity in the core domains with most GtfBs, featuring a similar tunneled active site. We propose that GtfC (and related GtfD) enzymes evolved"],"journal":["Journal of agricultural and food chemistry"],"pagination":["15283-15295"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9732880"],"repository":["biostudies-literature"],"pubmed_title":["Crystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from Thermophilic <i>Geobacillus</i> 12AMOR1: Starch Transglycosylation in Non-Permuted GH70 Enzymes."],"pmcid":["PMC9732880"],"pubmed_authors":["Te Poele EM","Pijning T","de Leeuw TC","Dijkhuizen L","Guskov A"],"additional_accession":[]},"is_claimable":false,"name":"Crystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from Thermophilic <i>Geobacillus</i> 12AMOR1: Starch Transglycosylation in Non-Permuted GH70 Enzymes.","description":"GtfC-type 4,6-α-glucanotransferase (α-GT) enzymes from Glycoside Hydrolase Family 70 (GH70) are of interest for the modification of starch into low-glycemic index food ingredients. Compared to the related GH70 GtfB-type α-GTs, found exclusively in lactic acid bacteria (LAB), GtfCs occur in non-LAB, share low sequence identity, lack circular permutation of the catalytic domain, and feature a single-segment auxiliary domain IV and auxiliary C-terminal domains. Despite these differences, the first crystal structure of a GtfC, GbGtfC-ΔC from <i>Geobacillus</i> 12AMOR1, and the first one representing a non-permuted GH70 enzyme, reveals high structural similarity in the core domains with most GtfBs, featuring a similar tunneled active site. We propose that GtfC (and related GtfD) enzymes evolved","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-29T14:58:26.822Z","creation":"2025-04-04T23:37:00.219Z"},"accession":"S-EPMC9732880","cross_references":{"pubmed":["36442227"],"doi":["10.1021/acs.jafc.2c06394"]}}