IntEnz

EC 2.5.1.18 - Glutathione transferase

IntEnz Enzyme Nomenclature
EC 2.5.1.18

Names

Reactions

• 16437 [IUBMB]
  glutathione

  glutathione

  Name origin: UniProt - CHECKED (C)

  CHEBI:57925

  Formula: C10H16N3O6S
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  RX

  RX

  Name origin: UniProt - CHECKED (C)

  CHEBI:17792

  Formula: RX
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  a halide anion

  a halide anion

  Name origin: UniProt - CHECKED (C)

  CHEBI:16042

  Formula: X
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  an S-substituted glutathione

  an S-substituted glutathione

  Name origin: UniProt - CHECKED (C)

  CHEBI:90779

  Formula: C10H15N3O6SR
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  
• 51220
  1-chloro-2,4-dinitrobenzene

  1-chloro-2,4-dinitrobenzene

  Name origin: UniProt - CHECKED (C)

  CHEBI:34718

  Formula: C6H3ClN2O4
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  glutathione

  glutathione

  Name origin: UniProt - CHECKED (C)

  CHEBI:57925

  Formula: C10H16N3O6S
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  =

  2,4-dinitrophenyl-S-glutathione

  2,4-dinitrophenyl-S-glutathione

  Name origin: UniProt - CHECKED (C)

  CHEBI:133977

  Formula: C16H18N5O10S
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  chloride

  chloride

  Name origin: UniProt - CHECKED (C)

  CHEBI:17996

  Formula: Cl
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

Comments:

A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.

Links to other databases

References

1. Habig, W.H., Pabst, M.J. and Jakoby, W.B.
   Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
   . J. Biol. Chem. 249: 7130-7139 (1974). [PMID: 4436300]
2. Jakoby, W.B.
   The glutathione S-transferases: a group of multifunctional detoxification proteins.
   Adv. Enzymol. Relat. Areas Mol. Biol. 46: 383-383 (1978). [PMID: 345769]
3. Jakoby, W.B.
   Glutathione transferases: an overview.
   Methods Enzymol. 113: 495-499 (1985).
4. Keen, J.H. and Jakoby, W.B.
   Glutathione transferases. Catalysis of nucleophilic reactions of glutathione.
   J. Biol. Chem. 253: 5654-5657 (1978). [PMID: 670218]
5. Sheehan, D., Meade, G., Foley, V.M. and Dowd, C.A.
   Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.
   Biochem. J. 360: 1-16 (2001). [PMID: 11695986]

[EC 2.5.1.18 created 1976 (EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7 created 1972, incorporated 1976)]