Structural insights into enzymatic degradation of oxidized polyvinyl alcohol.

ABSTRACT

The ever-increasing production and use of polyvinyl alcohol (PVA) threaten our environment. Yet PVA can be assimilated by microbes in two steps: oxidation and cleavage. Here we report novel α/ß-hydrolase structures of oxidized PVA hydrolase (OPH) from two known PVA-degrading organisms, Sphingopyxis sp. 113P3 and Pseudomonas sp. VM15C, including complexes with substrate analogues, acetylacetone and caprylate. The active site is covered by a lid-like ß-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of ß-diketone, although it has a catalytic triad similar to that of most α/ß-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving ß-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications.