Identification of functionally important residues and structural features in a bacterial lignostilbene dioxygenase.

ABSTRACT: Lignostilbene-α,β-dioxygenase A (LsdA) from the bacterium Sphingomonas paucimobilis TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules. To examine LsdA's substrate specificity, we heterologously produced the dimeric enzyme with the help of chaperones. When tested on several substituted stilbenes, LsdA exhibited the greatest specificity for lignostilbene (k_cat^app = 1.00 ± 0.04 × 10⁶ m^-1 s^-1). These experiments further indicated that the substrate's 4-hydroxy moiety is required for catalysis and that this moiety cannot be replaced with a methoxy group. Phenylazophenol inhibited the LsdA-catalyzed cleavage of lignostilbene i

SUBMITTER: Kuatsjah E 

PROVIDER: S-EPMC6721942 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature