Identification of a novel enzyme and the regulation of key enzymes in mammalian taurine synthesis

J Pharmacol Sci. 2024 Jan;154(1):9-17. doi: 10.1016/j.jphs.2023.11.003. Epub 2023 Nov 21.

Abstract

Taurine has many pharmacological roles on various tissues. The maintenance of abundant taurine content in the mammalian body through endogenous synthesis, in addition to exogenous intake, is the essential factor for morphological and functional maintenances in most tissues. The synthesis of taurine from sulfur-containing amino acids is influenced by various factors. Previous literature findings indicate the influence of the intake of proteins and sulfur-containing amino acids on the activity of the rate-limiting enzymes cysteine dioxygenase and cysteine sulfinate decarboxylase. In addition, the regulation of the activity and expression of taurine-synthesis enzymes by hormones, bile acids, and inflammatory cytokines through nuclear receptors have been reported in liver and reproductive tissues. Furthermore, flavin-containing monooxygenase subtype 1 was recently identified as the taurine-synthesis enzyme that converts hypotaurine to taurine. This review introduces the novel taurine synthesis enzyme and the nuclear receptor-associated regulation of key enzymes in taurine synthesis.

Keywords: Cysteine dioxygenase; Cysteine sulfinate decarboxylase; Flavin-containing monooxygenase subtype 1; Nuclear receptor; Taurine synthesis.

Publication types

  • Review

MeSH terms

  • Amino Acids / analysis
  • Amino Acids / metabolism
  • Animals
  • Cysteine Dioxygenase* / analysis
  • Cysteine Dioxygenase* / metabolism
  • Liver / metabolism
  • Mammals* / metabolism
  • Receptors, Cytoplasmic and Nuclear / metabolism
  • Sulfur / analysis
  • Sulfur / metabolism
  • Taurine / metabolism
  • Taurine / pharmacology

Substances

  • Cysteine Dioxygenase
  • Taurine
  • Receptors, Cytoplasmic and Nuclear
  • Amino Acids
  • Sulfur