Glutathione thiolesterase

glutathione thiolesterase
Identifiers
EC no.3.1.2.7
CAS no.9025-99-4
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BRENDAenzyme data
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MetaCycmetabolic pathway
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The enzyme glutathione thiolesterase (EC 3.1.2.7) catalyzes the reaction

S-acylglutathione + H2O glutathione + a carboxylate

This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is S-acylglutathione hydrolase. It is also called citryl-glutathione thioesterhydrolase.

Glutathione thiolesterase has also been found to catalyze the reaction

S-lactoylglutathione + H2O glutathione + a lactate

The catalyzation of hydrolysis of S-lactoylglutathione by glutathione thiolesterase has been noted in Saccharomyces cerevisiae[1]. Additionally, human red blood cells have been found to contain at least four separate glutathione thiol esterases[2]. The enzymes found supported the potential substrate activity of S-lactoylglutathione and S-propionylglutathione[2].

References

  1. ↑ Murata, Kousaku; Sato, Nobuyuki; Rhee, Hae-ik; Watanabe, Kunihiko; Kimura, Akira (July 1987). "Purification and Characterization of Glutathione Thiol Esterase from Saccharomyces cerevisiae". Agricultural and Biological Chemistry. 51 (7): 1901–1907. doi:10.1080/00021369.1987.10868321. ISSN 0002-1369.
  2. 1 2 Uotila, Lasse (1979-10-24). "Glutathione thiol esterases of human red blood cells: Fractionation by gel electrophoresis and isoelectric focusing". Biochimica et Biophysica Acta (BBA) - Protein Structure. 580 (2): 277–288. doi:10.1016/0005-2795(79)90140-5. ISSN 0005-2795.
  • Murata K., & Sato N., & Rhee H., & Watanabe K., & Kimura A. (1987) "Purification and Characterization of Glutathione Thiol Esterase from Saccharomyces cerevisiae" Agricultural and Biological Chemistry, 51(7), 1901-1907. https://doi.org/10.1080/00021369.1987.10868321
  • Uotila, Lasse. (1979) "Glutathione thiol esterases of human red blood cells: Fractionation by gel electrophoresis and isoelectric focusing" Biochimica et Biophysica Acta (BBA) - Protein Structure, 580(2), 277-288. https://doi.org/10.1016/0005-2795(79)90140-5