|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
Enzymes and Genes:
fused glutathionylspermidine amidase / glutathionylspermidine synthetase : gss
In Pathway: glutathionylspermidine biosynthesis
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 220.127.116.11: glutathionylspermidine synthase
Enzyme Commission Synonyms for 18.104.22.168: glutathione:spermidine ligase (ADP-forming)
Enzyme Commission Primary Name for 22.214.171.124: trypanothione synthase
Enzyme Commission Synonyms for 126.96.36.199: glutathionylspermidine:glutathione ligase (ADP-forming)
This reaction synthesizes glutathionylspermidine.
Enzyme Commission Summary for 188.8.131.52:
Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 184.108.40.206 reaction, resulting in a net hydrolysis of ATP.
Enzyme Commission Summary for 220.127.116.11:
The enzyme, characterized from several trypanosomatids (e.g. Trypanosoma cruzi) catalyses two subsequent reactions, leading to production of trypanothione from glutathione and spermidine. Some trypanosomatids (e.g. Crithidia species and some Leishmania species) also contain an enzyme that only carries out the first reaction (cf. EC 18.104.22.168, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 22.214.171.124, glutathionylspermidine amidase).
Bollinger95: Bollinger JM, Kwon DS, Huisman GW, Kolter R, Walsh CT (1995). "Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase." J Biol Chem 1995;270(23);14031-41. PMID: 7775463
Smith92: Smith K, Nadeau K, Bradley M, Walsh C, Fairlamb AH (1992). "Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata." Protein Sci 1(7);874-83. PMID: 1304372
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