Multifunctionality of a low-specificity L-threonine aldolase from the hyperthermophile Thermotoga maritima.

Autor: Miyamoto T; Graduate School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-Ku, Tokyo, 108-8641, Japan. miyamotot@pharm.kitasato-u.ac.jp.; School of Pharmacy, Kitasato University, 5-9-1 Shirokane, Minato-Ku, Tokyo, 108-8641, Japan. miyamotot@pharm.kitasato-u.ac.jp., Kobayashi F; School of Pharmacy, Kitasato University, 5-9-1 Shirokane, Minato-Ku, Tokyo, 108-8641, Japan., Emori K; School of Pharmacy, Kitasato University, 5-9-1 Shirokane, Minato-Ku, Tokyo, 108-8641, Japan., Sakai-Kato K; Graduate School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-Ku, Tokyo, 108-8641, Japan.; School of Pharmacy, Kitasato University, 5-9-1 Shirokane, Minato-Ku, Tokyo, 108-8641, Japan.
Jazyk: angličtina
Zdroj: Extremophiles : life under extreme conditions [Extremophiles] 2024 Aug 27; Vol. 28 (3), pp. 41. Date of Electronic Publication: 2024 Aug 27.
DOI: 10.1007/s00792-024-01357-z
Abstrakt: 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.
(© 2024. The Author(s), under exclusive licence to Springer Nature Japan KK.)
Databáze: MEDLINE
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