Urinary l -erythro-β-hydroxyasparagine—a novel serine racemase inhibitor and substrate of the Zn2+-dependent d -serine dehydratase
| Autor: | Mayuka Tono, Tohru Yoshimura, Yasuyuki Kitaura, Tomokazu Ito, Hisashi Hemmi |
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| Rok vydání: | 2021 |
| Předmět: |
Male
0301 basic medicine L-Serine Dehydratase Racemases and Epimerases Biophysics Urine Biochemistry Rats Sprague-Dawley 03 medical and health sciences Glutamatergic chemistry.chemical_compound Commentaries Chemical Biology serine racemase Animals Humans Enzyme Inhibitors Pyridoxal phosphate Receptor Molecular Biology Diagnostics & Biomarkers chemistry.chemical_classification amino acids 030102 biochemistry & molecular biology Chemistry Succinates Cell Biology Rats Amino acid 030104 developmental biology d-serine Dehydratase Serine racemase NMDA receptor Asparagine |
| Zdroj: | Bioscience Reports |
| ISSN: | 1573-4935 0144-8463 |
| Popis: | The analysis of the urine contents can be informative of physiological homoeostasis, and it has been speculated that the levels of urinary d-serine (d-ser) could inform about neurological and renal disorders. By analysing the levels of urinary d-ser using a d-ser dehydratase (DSD) enzyme, Ito et al. (Biosci. Rep.(2021) 41, BSR20210260) have described abundant levels of l-erythro-β-hydroxyasparagine (l-β-EHAsn), a non-proteogenic amino acid which is also a newly described substrate for DSD. The data presented support the endogenous production l-β-EHAsn, with its concentration significantly correlating with the concentration of creatinine in urine. Taken together, these results could raise speculations that l-β-EHAsn might have unexplored important biological roles. It has been demonstrated that l-β-EHAsn also inhibits serine racemase with Ki values (40 μM) similar to its concentration in urine (50 μM). Given that serine racemase is the enzyme involved in the synthesis of d-ser, and l-β-EHAsn is also a substrate for DSD, further investigations could verify if this amino acid would be involved in the metabolic regulation of pathways involving d-ser. |
| Databáze: | OpenAIRE |
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