Structural Insights into 4,5-DOPA Extradiol Dioxygenase from <i>Beta vulgaris</i>: Unraveling the Key Step in Versatile Betalain Biosynthesis.

ABSTRACT: Betalains, a group of pigments widely distributed in various plants, are extensively applied in the food, beverage, and medicinal industries. The biosynthesis of betalains involves the enzymatic action of 4,5-DOPA-dioxygenase, which catalyzes the key ring-opening reaction of DOPA to produce betalamic acid, a crucial intermediate in the pathway. The crystal structure of a 4,5-DOPA-dioxygenase from Beta vulgaris (BvDOD) was determined in this study. The structural analysis revealed that BvDOD exhibited a structural fold similar to that of other members of the extradiol dioxygenase family. Moreover, the Fe-ligand residues His15, His53, and His229 indicated the enzyme's reliance on nonheme iron for catalyzing the ring-opening reaction. Molecular docking and mutational analysis identifie

SUBMITTER: Chiang CC 

PROVIDER: S-EPMC11926856 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature