Characterization of the Third Glutathione S-Transferase Gene Involved in Enantioselective Cleavage of the β-Aryl Ether by Sphingobium sp. Strain SYK-6

Kazuyuki TANAMURA; Tomokuni ABE; Naofumi KAMIMURA; Daisuke KASAI; Shojiro HISHIYAMA; Yuichiro OTSUKA; Masaya NAKAMURA; Shinya KAJITA; Yoshihiro KATAYAMA; Masao FUKUDA; Eiji MASAI

doi:10.1271/bbb.110525

Microbiology & Fermentation Technology Notes

Characterization of the Third Glutathione S-Transferase Gene Involved in Enantioselective Cleavage of the β-Aryl Ether by Sphingobium sp. Strain SYK-6

Kazuyuki TANAMURA, Tomokuni ABE, Naofumi KAMIMURA, Daisuke KASAI, Shojiro HISHIYAMA, Yuichiro OTSUKA, Masaya NAKAMURA, Shinya KAJITA, Yoshihiro KATAYAMA, Masao FUKUDA, Eiji MASAI

Author information

Kazuyuki TANAMURA
Department of Bioengineering, Nagaoka University of Technology
Tomokuni ABE
Department of Bioengineering, Nagaoka University of Technology
Naofumi KAMIMURA
Department of Bioengineering, Nagaoka University of Technology
Daisuke KASAI
Department of Bioengineering, Nagaoka University of Technology
Shojiro HISHIYAMA
Forestry and Forest Products Research Institute
Yuichiro OTSUKA
Forestry and Forest Products Research Institute
Masaya NAKAMURA
Forestry and Forest Products Research Institute
Shinya KAJITA
Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
Yoshihiro KATAYAMA
College of Bioresource Sciences, Nihon University
Masao FUKUDA
Department of Bioengineering, Nagaoka University of Technology
Eiji MASAI
Department of Bioengineering, Nagaoka University of Technology

Keywords: lignin biodegradation, β-aryl ether, glutathione S-transferase, Sphingobium

JOURNAL FREE ACCESS

2011 Volume 75 Issue 12 Pages 2404-2407

DOI https://doi.org/10.1271/bbb.110525

View "Advance Publication" version (December 7, 2011).

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Abstract

The glutathione S-transferases, LigF and LigE, of Sphingobium sp. strain SYK-6 respectively play a role in cleavage of the β-aryl ether of (+)-(βS)-α-(2-methoxyphenoxy)-β-hydroxypropiovanillone (MPHPV) and (−)-(βR)-MPHPV. The ligP gene, which showed 59% similarity to ligE at the amino acid level, was isolated from SYK-6. LigP produced in Escherichia coli revealed enantioselectivity for (−)-(βR)-MPHPV, and ligE and ligP alone contributed to the degradation of (−)-(βR)-MPHPV in SYK-6.

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