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

doi:10.1002/cbic.201402166

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 journal › Article › peer-review

20 Citations (Scopus)

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/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 language	English
Pages (from-to)	1882-1886
Number of pages	5
Journal	ChemBioChem
Volume	15
Issue number	13
DOIs	https://doi.org/10.1002/cbic.201402166
Publication status	Published - Sept 5 2014
Externally published	Yes

Keywords

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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10.1002/cbic.201402166

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title = "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/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.",

keywords = "beta-diketone hydrolases, catalytic triad, double oxyanion holes, environmental chemistry, hydrolases, microbial assimilation",

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

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year = "2014",

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doi = "10.1002/cbic.201402166",

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AU - Yang, Yu

AU - Ko, Tzu Ping

AU - Liu, Long

AU - Li, Jianghua

AU - Huang, Chun Hsiang

AU - Chan, Hsiu Chien

AU - Ren, Feifei

AU - Jia, Dongxu

AU - Wang, Andrew H.J.

AU - Guo, Rey Ting

AU - Chen, Jian

AU - Du, Guocheng

PY - 2014/9/5

Y1 - 2014/9/5

N2 - 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.

AB - 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.

KW - beta-diketone hydrolases

KW - catalytic triad

KW - double oxyanion holes

KW - environmental chemistry

KW - hydrolases

KW - microbial assimilation

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Structural insights into enzymatic degradation of oxidized polyvinyl alcohol

Abstract

Keywords

ASJC Scopus subject areas

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