Promiscuous enzymes generating d-amino acids in mammals: Why they may still surprise us?
| Autor: | Wolosker H; Department of Biochemistry, Technion-Israel Institute of Technology, Rappaport Faculty of Medicine, Haifa 31096, Israel., Radzishevsky I; Department of Biochemistry, Technion-Israel Institute of Technology, Rappaport Faculty of Medicine, Haifa 31096, Israel. |
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| Jazyk: | angličtina |
| Zdroj: | The Biochemical journal [Biochem J] 2021 Mar 12; Vol. 478 (5), pp. 1175-1178. |
| DOI: | 10.1042/BCJ20200988 |
| Abstrakt: | Promiscuous catalysis is a common property of enzymes, particularly those using pyridoxal 5'-phosphate as a cofactor. In a recent issue of this journal, Katane et al. Biochem. J. 477, 4221-4241 demonstrate the synthesis and accumulation of d-glutamate in mammalian cells by promiscuous catalysis mediated by a pyridoxal 5'-phosphate enzyme, the serine/threonine dehydratase-like (SDHL). The mechanism of SDHL resembles that of serine racemase, which synthesizes d-serine, a well-established signaling molecule in the mammalian brain. d-Glutamate is present in body fluids and is degraded by the d-glutamate cyclase at the mitochondria. This study demonstrates a biochemical pathway for d-glutamate synthesis in mammalian cells and advances our knowledge on this little-studied d-amino acid in mammals. d-Amino acids may still surprise us by their unique roles in biochemistry, intercellular signaling, and as potential biomarkers of disease. (© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.) |
| Databáze: | MEDLINE |
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