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

The glutathione S-transferases, LigF and LigE, of Sphingobium sp. strain SYK-6 respectively play a role in cleavage of the beta-aryl ether of (+)-(beta S)-alpha-(2-methoxyphenoxy)-beta-hydroxypropiovanillone (MPHPV) and (-)(-beta R)-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 (-)-(beta R)-MPHPV, and ligE and ligP alone contributed to the degradation of (-)-(beta R)-MPHPV in SYK-6.