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<p>We previously demonstrated that the hyperthermophilic bacterium <i>Thermotoga maritima</i> has unique metabolic pathways for <span>d</span>- and <span>l</span>-amino acids. In the present study, we characterized <i>O</i>-acetyl-<span>l</span>-homoserine sulfhydrylase (MetY) TM0882 associated with <span>l</span>-methionine biosynthesis. MetY catalyzes the production of <span>l</span>-homocysteine from <i>O</i>-acetyl-<span>l</span>-homoserine and hydrogen sulfide. We found that TM0882 also possesses β-lyase, racemase/α-epimerase, aminotransferase, and decarboxylase activities. This enzyme displayed <span>l</span>-cysteine β-lyase activity as well as racemase/α-epimerase activity toward glutamate and threonine. Furthermore, TM0882 exhibited aminotransferase and <span>l</span>-aspartate 4-decarboxylase activities. Catalytic efficiency (<i>k</i><sub>cat</sub>/<i>K</i><sub>m</sub>) for β-lyase activity was highest among the four additional activities. TM0882 is therefore a multifunctional enzyme possessing four different activities in addition to sulfhydrylase activity.</p>

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O-Acetyl-l-homoserine sulfhydrylase from Thermotoga maritima has five enzyme activities

  • 期刊论文

  • 发表日期：

    2025年11月15日

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  • Tetsuya Miyamoto,
  • Kumiko Sakai-Kato

摘要

We previously demonstrated that the hyperthermophilic bacterium Thermotoga maritima has unique metabolic pathways for d- and l-amino acids. In the present study, we characterized O-acetyl-l-homoserine sulfhydrylase (MetY) TM0882 associated with l-methionine biosynthesis. MetY catalyzes the production of l-homocysteine from O-acetyl-l-homoserine and hydrogen sulfide. We found that TM0882 also possesses β-lyase, racemase/α-epimerase, aminotransferase, and decarboxylase activities. This enzyme displayed l-cysteine β-lyase activity as well as racemase/α-epimerase activity toward glutamate and threonine. Furthermore, TM0882 exhibited aminotransferase and l-aspartate 4-decarboxylase activities. Catalytic efficiency (kcat/Km) for β-lyase activity was highest among the four additional activities. TM0882 is therefore a multifunctional enzyme possessing four different activities in addition to sulfhydrylase activity.