ArticleExtremophiles : life under extreme conditions2024
Multifunctionality of a low-specificity L-threonine aldolase from the hyperthermophile Thermotoga maritima.
Article in Extremophiles : life under extreme conditions, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Elucidation of D-amino acid metabolic activity of ornithine decarboxylase from the hyperthermophile Thermotoga maritima.Extremophiles : life under extreme conditions · 2026Article
- Enhancing Diastereoselectivity of l‑Threonine Aldolase by Strengthening Kinetic Control To Mitigate Thermodynamic Equilibrium.Chem & bio engineering · 2026Article
- O-Acetyl-L-homoserine sulfhydrylase from Thermotoga maritima has five enzyme activities.Extremophiles : life under extreme conditions · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
The peptidoglycan of the hyperthermophile Thermotoga maritima contains an unusual D-lysine in addition to the typical D-alanine and D-glutamate. Previously, we identified the D-lysine and D-glutamate biosynthetic pathways of T. maritima. Additionally, we reported some multifunctional enzymes involved in amino acid metabolism. In the present study, we characterized the enzymatic properties of TM1744 (threonine aldolase) to probe both its potential multifunctionality and D-amino acid metabolizing activities. TM1744 displayed aldolase activity toward both L-allo-threonine and L-threonine, and exhibited higher activity toward L-threo-phenylserine. It did not function as an aldolase toward D-allo-threonine or D-threonine. Furthermore, TM1744 had racemase activity toward two amino acids, although its racemase activity was lower than its aldolase activity. TM1744 did not have other amino acid metabolizing activities. Therefore, TM1744 is a low-specificity L-threonine aldolase with limited racemase activity.
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Registered trials
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