Molecular insight into regioselectivity of transfructosylation catalyzed by GH68 levansucrase and β-fructofuranosidase.

ABSTRACT: Glycoside hydrolase family 68 (GH68) enzymes catalyze β-fructosyltransfer from sucrose to another sucrose, the so-called transfructosylation. Although regioselectivity of transfructosylation is divergent in GH68 enzymes, there is insufficient information available on the structural factor(s) involved in the selectivity. Here, we found two GH68 enzymes, β-fructofuranosidase (FFZm) and levansucrase (LSZm), encoded tandemly in the genome of Zymomonas mobilis, displayed different selectivity: FFZm catalyzed the β-(2→1)-transfructosylation (1-TF), whereas LSZm did both of 1-TF and β-(2→6)-transfructosylation (6-TF). We identified His79^FFZm and Ala343^FFZm and their corresponding Asn84^LSZm and Ser345^LSZm respectively as the structural factors for those

SUBMITTER: Okuyama M 

PROVIDER: S-EPMC7961098 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature