Structural insights into enzymatic degradation of oxidized polyvinyl alcohol

Yu Yang, Tzu Ping Ko, Long Liu, Jianghua Li, Chun Hsiang Huang, Hsiu Chien Chan, Feifei Ren, Dongxu Jia, Andrew H.J. Wang, Rey Ting Guo, Jian Chen, Guocheng Du

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


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/β-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 β-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of β-diketone, although it has a catalytic triad similar to that of most α/β-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving β-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications.

Original languageEnglish
Pages (from-to)1882-1886
Number of pages5
Issue number13
Publication statusPublished - Sept 5 2014
Externally publishedYes


  • beta-diketone hydrolases
  • catalytic triad
  • double oxyanion holes
  • environmental chemistry
  • hydrolases
  • microbial assimilation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry


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