EC 6.3.1.8 - Glutathionylspermidine synthase

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IntEnz Enzyme Nomenclature
EC 6.3.1.8

Names

Accepted name:
glutathionylspermidine synthase
Other names:
glutathione:spermidine ligase (ADP-forming)
γ-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming)
glutathionylspermidine synthetase
GSP synthetase
Systematic name:
γ-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]

Reaction

Cofactor

Comments:

Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008885
CAS Registry Number: 9077-09-2
UniProtKB/Swiss-Prot:

References

  1. Smith, K., Nadeau, K., Bradley, M., Walsh, C.T., Fairlamb, A.H.
    Purification of glutathionylspermidine and trypanothione synthase from Crithidia fasciculata.
    Protein Sci. 1: 874-883 (1992). [PMID: 1304372]
  2. Bollinger, J.M., Kwon, D.S., Huisman, G.W., Kolter, R., Walsh, C.T.
    Glutathionylspermidine metabolism in E. coli. Purification, cloning, overproduction and characterization of a bifunctional glutathionyl spermidine synthetase/amidase.
    J. Biol. Chem. 270: 14031-14041 (1995). [PMID: 7775463]

[EC 6.3.1.8 created 1999]