Analysis Kinetics of Docking Domains (DDs) by BLI (CAT#: STEM-MB-0288-CJ)

Introduction

Short amino acid regions at the N- and C-termini of each subunit, termed docking domains (DDs), often occur in complementary pairs, which interact to facilitate substrate transfer and maintain pathway fidelity. For example, 6-deoxyerythronolide B synthase (DEBS) is a prototypical modular megasynthase assembling the polyketide core of macrocyclic aglycone of erythromycin, which contains three large subunits (DEBS1, -2, and -3), with each one housing two unique modules. The subunits are connected by short DDs. DEBS1 and DEBS2 interaction DDs are composed of 86 and 31 amino acids, respectively, while DEBS2 and DEBS3 DDs (D4 CDD-D5 NDD in this study) comprise 80 and 39 amino acids, respectively, and form the complete PKS complex of DEBS and facilitate efficient pipeline-like erythromycin biosynthesis. More than three thousand type I modular PKSs with diverse structures containing different DDs have been characterized in nature, such as rapamycin polyketide synthase (RAPS), spinosad polyketide synthase, and salinomycin polyketide synthase containing two, four, and eight pairs of DDs, respectively.