Stereochemical Features of Glutathione-dependent Enzymes in the Sphingobium sp. Strain SYK-6 β-Aryl Etherase Pathway

Gall, Daniel L.; Kim, Hoon; Lu, Fachuang; Donohue, Timothy J.; Noguera, Daniel R.; Ralph, John

doi:10.1074/jbc.m113.536250

Title: Stereochemical Features of Glutathione-dependent Enzymes in the Sphingobium sp. Strain SYK-6 β-Aryl Etherase Pathway

Journal Article · Fri Feb 07 00:00:00 EST 2014 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.m113.536250· OSTI ID:1904221

Gall, Daniel L. ^[1]; Kim, Hoon ^[1]; Lu, Fachuang ^[1]; Donohue, Timothy J. ^[1]; Noguera, Daniel R. ^[1]; Ralph, John ^[1]

University of Wisconsin, Madison, WI (United States)

Glutathione-dependent enzymes play important protective, repair, or metabolic roles in cells. In particular, enzymes in the glutathione S-transferase (GST) superfamily function in stress responses, defense systems, or xenobiotic detoxification. Here, we identify novel features of bacterial GSTs that cleave -aryl ether bonds typically found in plant lignin. Our data reveal several original features of the reaction cycle of these GSTs, including stereospecific substrate recognition and stereoselective formation of -S-thioether linkages. Products of recombinant GSTs (LigE, LigP, and LigF) are -S-glutathionyl--ketothioethers that are degraded by a -S-thioetherase (LigG). All three Lig GSTs produced the ketone product (-S-glutathionyl- -veratrylethanone) from an achiral side chain-truncated model substrate (-guaiacyl--veratrylethanone). However, when -etherase assays were conducted with a racemic model substrate, -guaiacyl--veratrylglycerone, LigE- or LigP-catalyzed reactions yielded only one of two potential product (-Sglutathionyl--veratrylglycerone) epimers, whereas the other diastereomer (differing in configuration at the -position (i.e. its-epimer)) was produced only in the LigF-catalyzed reaction. Thus, -etherase catalysis causes stereochemical inversion of the chiral center, converting a (R)-substrate to a (S)-product (LigE and LigP), and a (S)-substrate to a (R)-product (LigF). Further, LigG catalyzed glutathione-dependent -S-thioether cleavage with-S-glutathionyl--veratrylethanone and with(R)- configured -S-glutathionyl--veratrylglycerone but exhibited no or significantly reduced -S-thioether-cleaving activity with the (S)-epimer, demonstrating that LigG is a stereospecific -thioetherase. We therefore propose that multiple Lig enzymes are needed in this -aryl etherase pathway in order to cleave the racemic -ether linkages that are present in the backbone of the lignin polymer.

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Research Organization:: Univ. of Wisconsin, Madison, WI (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: FC02-07ER64494

OSTI ID:: 1904221

Journal Information:: Journal of Biological Chemistry, Vol. 289, Issue 12; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Lignin Helmich, Kate E.; Pereira, Jose Henrique; Gall, Daniel L. Journal of Biological Chemistry, Vol. 291, Issue 10 https://doi.org/10.1074/jbc.m115.694307	journal	December 2015
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Bacterial Valorization of Lignin: Strains, Enzymes, Conversion Pathways, Biosensors, and Perspectives Lee, Siseon; Kang, Minsik; Bae, Jung-Hoon Frontiers in Bioengineering and Biotechnology, Vol. 7 https://doi.org/10.3389/fbioe.2019.00209	journal	September 2019
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59 BASIC BIOLOGICAL SCIENCES
bacterial metabolism
enzyme catalysis
glutathione
lignin degradation
thiol
beta-S-thioetherase
beta-aryl etherase
glutathione s-transferase
stereoselectivity
stereospecificity

Title: Stereochemical Features of Glutathione-dependent Enzymes in the Sphingobium sp. Strain SYK-6 β-Aryl Etherase Pathway

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