Structural and Functional Characterization of YdjI, an Aldolase of Unknown Specificity in Escherichia coli K12.

ABSTRACT: The ydj gene cluster is found in 80% of sequenced Escherichia coli genomes and other closely related species in the human microbiome. On the basis of the annotations of the enzymes located in this cluster, it is expected that together they catalyze the catabolism of an unknown carbohydrate. The focus of this investigation is on YdjI, which is in the ydj gene cluster of E. coli K-12. It is predicted to be a class II aldolase of unknown function. Here we describe a structural and functional characterization of this enzyme. YdjI catalyzes the hydrogen/deuterium exchange of the pro-S hydrogen at C3 of dihydroxyacetone phosphate (DHAP). In the presence of DHAP, YdjI catalyzes an aldol condensation with a variety of aldo sugars. YdjI shows a strong preference f

SUBMITTER: Huddleston JP 

PROVIDER: S-EPMC6850750 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature