Structure Report for: 3WLA

Yang, Y., Ko, T.P., Li, J.H., Liu, L., Huang, C.H., Chan, H.C., Ren, F.F., Jia, D.X., Wang, A.H.-J., Guo, R.T., Chen, J., Du, G.C.

Title: Structural insights into enzymatic degradation of oxidized polyvinyl alcohol
Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH and Du G <2 more author(s)> Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH, Guo RT, Chen J, Du G (- 2)
Ref: Chembiochem, 15:1882, 2014 : PubMed
Abstract


ESTHER: Yang_2014_Chembiochem_15_1882
PubMedSearch: Yang 2014 Chembiochem 15 1882
PubMedID: 25044912
Gene_locus related to this paper: psesp-OPH, sphs1-OPH
Inhibitor(s) related to this paper: Diethylene-glycol-monoethyl-ether, Acetylacetone, Octanoate

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 alpha/beta-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 CC 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.