|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
Enzymes and Genes:
|Crithidia fasciculata:||glutathionylspermidine synthetase: gspS|
glutathionylspermidine synthetase: TryS
|Escherichia coli K-12 substr. MG1655:||fused glutathionylspermidine amidase / glutathionylspermidine synthetase: gss|
In Pathway: glutathionylspermidine biosynthesis
The direction shown, i.e. which substrates are on the left and right sides, 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. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 126.96.36.199: glutathionylspermidine synthase
Enzyme Commission Synonyms for 188.8.131.52: glutathione:spermidine ligase (ADP-forming)
Enzyme Commission Primary Name for 184.108.40.206: trypanothione synthase
Enzyme Commission Synonyms for 220.127.116.11: glutathionylspermidine:glutathione ligase (ADP-forming)
Standard Gibbs Free Energy (ΔrG'°): -5.2634583 kcal/mol [Latendresse13]
Enzyme Commission Summary for 18.104.22.168:
Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 22.214.171.124 reaction, resulting in a net hydrolysis of ATP.
Enzyme Commission Summary for 126.96.36.199:
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 188.8.131.52, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 184.108.40.206, 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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