Insights into Broad-Specificity Starch Modification from the Crystal Structure of <i>Limosilactobacillus Reuteri</i> NCC 2613 4,6-α-Glucanotransferase GtfB
Tjaard Pijning, Joana Gangoiti, Evelien M. te Poele, Tim Börner, Lubbert Dijkhuizen
Abstract
NCC 2970) and show that they are able to convert both linear and branched starch substrates. Compared to the previously described GtfB structure, these two enzymes feature a much more open binding groove, reminiscent of and evolutionary closer to starch-converting GH13 α-amylases. Sequence analysis of 287 putative GtfBs suggests that only 20% of them are similarly "open" and thus suitable as broad-specificity starch-converting enzymes.
Topics & Concepts
StarchGlycoside hydrolaseEnzymeBiochemistryAmylaseLactobacillus reuteriChemistryGlycosideStereochemistryBiologyFermentationLactobacillusEnzyme Production and CharacterizationMicrobial Metabolites in Food BiotechnologyBiofuel production and bioconversion