ArticleExtremophiles : life under extreme conditions2025
O-Acetyl-L-homoserine sulfhydrylase from Thermotoga maritima has five enzyme activities.
Article in Extremophiles : life under extreme conditions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Elucidation of D-amino acid metabolic activity of ornithine decarboxylase from the hyperthermophile Thermotoga maritima.Extremophiles : life under extreme conditions · 2026Article
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Abstract
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 (k
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