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Literature summary for 6.3.1.9 extracted from
- Trypanothione synthesis in Crithidia revisited (2005), J. Biol. Chem., 280, 6850-6860.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA sequence determination and analysis, expression of wild-type enzyme and mutants in Escherichia coli as His-tagged or Nus-fusion proteins | Crithidia fasciculata |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R553E | site-directed mutagenesis | Crithidia fasciculata |
| R553K | site-directed mutagenesis | Crithidia fasciculata |
| R553L | site-directed mutagenesis | Crithidia fasciculata |
| R553Q | site-directed mutagenesis | Crithidia fasciculata |
| R613E | site-directed mutagenesis | Crithidia fasciculata |
| R613K | site-directed mutagenesis | Crithidia fasciculata |
| R613L | site-directed mutagenesis | Crithidia fasciculata |
| R613Q | site-directed mutagenesis | Crithidia fasciculata |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | limited proteolysis with trypsin or factor Xa result in cleavage of wild-type and mutant enzymes at R553 followed by loss of activity, cleavage of wild-type and mutant R553Q can be delayed by presence of substrates | Crithidia fasciculata |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics for the multiple enzyme activities, Dalziel equation, overview | Crithidia fasciculata | |
| 0.222 | - |
MgATP2- | pH 7.2, 25°C, recombinant trypanothione synthase | Crithidia fasciculata |  |
| 0.407 | - |
glutathione | pH 7.2, 25°C, recombinant trypanothione synthase | Crithidia fasciculata | |
| 0.48 | - |
glutathionylspermidine | pH 7.2, 25°C, recombinant trypanothione synthase | Crithidia fasciculata | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | as MgATP2- | Crithidia fasciculata | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glutathione + glutathionylspermidine + ATP | Crithidia fasciculata | - |
N1,N8-bis(glutathionyl)spermidine + ADP + phosphate | - |
? | |
| additional information | Crithidia fasciculata | the trypanothione synthase also catalyzes the reaction of glutathionylspermidine synthase, EC 6.3.1.8 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Crithidia fasciculata | Q5DM89 | trypanothione synthase; a dual specificity enzyme | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type enzyme and mutants from Escherichia coli by nickel affinity chromatography | Crithidia fasciculata |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate | the reaction is catalyzed by trypanothione synthase, which also catalyzes the reaction of glutathionyspermidine synthase, EC 6.3.1.8, in Crithidia fasciculata, trypanothione synthase further exhibits amidase and marginal ATPase activities | Crithidia fasciculata |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Crithidia fasciculata |
| 2.1 | 2.2 | purified recombinant trypanothione synthase performing the trypanothione synthase reaction, average of the activity of recombinant enzymes expressed from different constructs, overview | Crithidia fasciculata |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 glutathione + spermidine + 2 ATP | trypanothione synthase overall reaction | Crithidia fasciculata | N1,N8-bis(glutathionyl)spermidine + 2 ADP + 2 phosphate | - |
? | |
| glutathione + glutathionylspermidine + ATP | - |
Crithidia fasciculata | N1,N8-bis(glutathionyl)spermidine + ADP + phosphate | - |
? | |
| glutathione + glutathionylspermidine + ATP | dynamic interactions of remote domains in substrate binding and catalysis | Crithidia fasciculata | N1,N8-bis(glutathionyl)spermidine + ADP + phosphate | - |
? | |
| glutathione + N8-acetylspermidine + ATP | - |
Crithidia fasciculata | N1-glutathionyl-N8-acetylspermidine + ADP + phosphate | - |
? | |
| glutathione + spermidine + ATP | ATP in form of MgATP2- | Crithidia fasciculata | glutathionylspermidine + ADP + phosphate | - |
? | |
| additional information | the trypanothione synthase also catalyzes the reaction of glutathionylspermidine synthase, EC 6.3.1.8 | Crithidia fasciculata | ? | - |
? | |
| additional information | the trypanothione synthase also catalyzes the reaction of glutathionylspermidine synthase, EC 6.3.1.8, and exhibits amidase and marginal ATPase activities | Crithidia fasciculata | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TryS | - |
Crithidia fasciculata |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Crithidia fasciculata |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Crithidia fasciculata | |
| 8.7 | - |
glutathionylspermidine | pH 7.2, 25°C, recombinant trypanothione synthase | Crithidia fasciculata | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | 7.5 | assay at | Crithidia fasciculata |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | as MgATP2- | Crithidia fasciculata | |
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Release 2023.1 (January 2023)
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