Journal
CHEMBIOCHEM
Volume 15, Issue 13, Pages 1882-1886Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201402166
Keywords
catalytic triad; beta-diketone hydrolases; double oxyanion holes; environmental chemistry; hydrolases; microbial assimilation
Funding
- Program for Changjiang Scholars and Innovative Research Team in University [IRT1135]
- National High Technology Research and Development Program of China (863 Program) [2012AA022202]
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- 111 Project [111-2-06]
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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 a/b-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 beta-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the C = C bond of beta-diketone, although it has a catalytic triad similar to that of most alpha/beta-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving beta-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications.
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