biostudies-literatureUnknown70(48)Pijning TRoyal AvebeRijksuniversiteit GroningenGtfC-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 evolvedJournal of agricultural and food chemistry15283-15295https://www.ebi.ac.uk/biostudies/studies/S-EPMC9732880biostudies-literatureCrystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from Thermophilic <i>Geobacillus</i> 12AMOR1: Starch Transglycosylation in Non-Permuted GH70 Enzymes.PMC9732880Te Poele EMPijning Tde Leeuw TCDijkhuizen LGuskov AfalseCrystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from Thermophilic <i>Geobacillus</i> 12AMOR1: Starch Transglycosylation in Non-Permuted GH70 Enzymes.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 evolved2022-01-01T00:00:00Z2022 Dec2026-05-29T14:58:26.822Z2025-04-04T23:37:00.219ZS-EPMC97328803644222710.1021/acs.jafc.2c06394