Promiscuous enzymes generating D-amino acids in mammals: Why they may still surprise us?

Herman Wolosker, Inna Radzishevsky

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)1175-1178
Number of pages4
JournalBiochemical Journal
Issue number5
StatePublished - 12 Mar 2021


  • Amino Acids
  • Animals
  • Glutamic Acid
  • L-Serine Dehydratase
  • Mammals
  • Pyridoxal Phosphate


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