| EC |
3.5.1.78 |
| Accepted name: |
glutathionylspermidine amidase |
| Reaction: |
glutathionylspermidine + H2O = glutathione + spermidine |
|
For diagram of trypanothione biosynthesis, click here |
| Glossary: |
spermidine = N-(3-aminopropyl)butane-1,4-diamine |
| Other name(s): |
glutathionylspermidine amidohydrolase (spermidine-forming) |
| Systematic name: |
γ-L-glutamyl-L-cysteinyl-glycine:spermidine amidase |
| Comments: |
Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 171040-71-4 |
| References: |
| 1. |
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 glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031–14041. [DOI] [PMID: 7775463] |
|
| [EC 3.5.1.78 created 1999] |
| |
|
| |
|
Printable version