Multifunctional enzymes related to amino acid metabolism in bacteria.
| Autor: | Miyamoto T; Graduate School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan. |
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| Jazyk: | angličtina |
| Zdroj: | Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 2024 May 22; Vol. 88 (6), pp. 585-593. |
| DOI: | 10.1093/bbb/zbae027 |
| Abstrakt: | In bacteria, d-amino acids are primarily synthesized from l-amino acids by amino acid racemases, but some bacteria use d-amino acid aminotransferases to synthesize d-amino acids. d-Amino acids are peptidoglycan components in the cell wall involved in several physiological processes, such as bacterial growth, biofilm dispersal, and peptidoglycan metabolism. Therefore, their metabolism and physiological roles have attracted increasing attention. Recently, we identified novel bacterial d-amino acid metabolic pathways, which involve amino acid racemases, with broad substrate specificity, as well as multifunctional enzymes with d-amino acid-metabolizing activity. Here, I review these multifunctional enzymes and their related d- and l-amino acid metabolic pathways in Escherichia coli and the hyperthermophile Thermotoga maritima. (© The Author(s) 2024. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.) |
| Databáze: | MEDLINE |
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