Promiscuous enzymes generating d-amino acids in mammals: Why they may still surprise us?
| Autor: | Inna Radzishevsky, Herman Wolosker |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
L-Serine Dehydratase
Glutamic Acid Biochemistry Cyclase Serine 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Animals Threonine Amino Acids Molecular Biology Pyridoxal 030304 developmental biology chemistry.chemical_classification Mammals 0303 health sciences Cell Biology Amino acid Metabolic pathway Enzyme chemistry Serine racemase Pyridoxal Phosphate 030217 neurology & neurosurgery |
| Zdroj: | The Biochemical journal. 478(5) |
| ISSN: | 1470-8728 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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