Title : Structural insights into enzymatic degradation of oxidized polyvinyl alcohol - Yang_2014_Chembiochem_15_1882 |
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 |
Ref : Chembiochem , 15 :1882 , 2014 |
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. |
PubMedSearch : Yang_2014_Chembiochem_15_1882 |
PubMedID: 25044912 |
Gene_locus related to this paper: psesp-OPH , sphs1-OPH |
Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH, Guo RT, Chen J, Du G (2014)
Structural insights into enzymatic degradation of oxidized polyvinyl alcohol
Chembiochem
15 :1882
Yang Y, Ko TP, Liu L, Li J, Huang CH, Chan HC, Ren F, Jia D, Wang AH, Guo RT, Chen J, Du G (2014)
Chembiochem
15 :1882