EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
6.3.1.8 | 744964 |
Genetic and chemical analyses reveal that trypanothione synthetase but not glutathionylspermidine synthetase is essential for Leishmania infantum |
Free Radic. Biol. Med. |
73 |
229-238 |
2014 |
Leishmania infantum |
24853758 |
6.3.1.8 | 744964 |
Genetic and chemical analyses reveal that trypanothione synthetase but not glutathionylspermidine synthetase is essential for Leishmania infantum |
Free Radic. Biol. Med. |
73 |
229-238 |
2014 |
Leishmania infantum MHOM / MA / 67 / ITMAP263 |
24853758 |
6.3.1.8 | 967 |
Aldehyde and phosphinate analogs of glutathione and glutathionylspermidine: potent, selective binding inhibitors of the E. coli bifunctional glutathionylspermidine synthetase/amidase |
Chem. Biol. |
4 |
859-866 |
1997 |
Escherichia coli |
9384533 |
6.3.1.8 | 692316 |
ATP-dependent ligases in trypanothione biosynthesis - kinetics of catalysis and inhibition by phosphinic acid pseudopeptides |
FEBS J. |
275 |
5408-5421 |
2008 |
Crithidia fasciculata |
18959765 |
6.3.1.8 | 963 |
Biochemical studies on protein folding chaperones (HSP90 and cyclophilin) and on trypanosomal enzymes (trypanothione and glutathionylspermidine synthetases) (heat shock protein) |
Diss. Abstr. Int. B |
56 |
3744 |
1995 |
Crithidia fasciculata |
- |
6.3.1.8 | 649733 |
Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata |
Biochem. J. |
364 |
679-686 |
2002 |
Crithidia fasciculata |
12049631 |
6.3.1.8 | 966 |
Characterization of the peptide substrate specificity of glutathionylspermidine synthetase from Crithidia fasciculata |
Mol. Biochem. Parasitol. |
84 |
25-32 |
1997 |
Crithidia fasciculata |
9041518 |
6.3.1.8 | 965 |
Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata |
J. Biol. Chem. |
273 |
19383-19390 |
1998 |
Crithidia fasciculata |
9677355 |
6.3.1.8 | 727627 |
Comparison of the functions of glutathionylspermidine synthetase/amidase from E. coli and its predicted homologues YgiC and YjfC |
Int. J. Biochem. Mol. Biol. |
3 |
302-312 |
2012 |
Escherichia coli |
23097746 |
6.3.1.8 | 968 |
Design, synthesis, and biochemical evaluation of phosphonate and phosphonamidate analogs of glutathionylspermidine as inhibitors of glutathionylspermidine synthetase/amidase from Escherichia coli |
J. Med. Chem. |
40 |
3842-3850 |
1997 |
Escherichia coli |
9371250 |