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EC 2.5.1.18 - Glutathione transferase

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IntEnz Enzyme Nomenclature
EC 2.5.1.18

Names

Accepted name:

glutathione transferase

Other names:

S-(hydroxyalkyl)glutathione lyase
glutathione S-alkyl transferase
glutathione S-alkyltransferase
glutathione S-aralkyltransferase
glutathione S-aryltransferase
glutathione S-transferase

Systematic name:

RX:glutathione R-transferase

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway

Structural data: CSA , EC2PDB

Gene Ontology: GO:0004364

CAS Registry Number: 50812-37-8

UniProtKB/Swiss-Prot: (353) [show] [UniProt]

References

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]
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]
Jakoby, W.B.

Glutathione transferases: an overview.

Methods Enzymol. 113 : 495-499 (1985).
Keen, J.H. and Jakoby, W.B.

Glutathione transferases. Catalysis of nucleophilic reactions of glutathione.

J. Biol. Chem. 253 : 5654-5657 (1978). [PMID: 670218]
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)]

EC 2 - Transferases