Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 glutathione + spermidine + 2 ATP
N1,N8-bis(glutathionyl)spermidine + 2 ADP + 2 phosphate
trypanothione synthase overall reaction
-
-
?
gamma-Glu-Gly-Gly + spermidine + ATP
N1-(gamma-Glu-Gly-Gly)-spermidine + ADP + phosphate
-
at 14% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-Glu-L-Cys(S-butyl)-Gly + spermidine + ATP
N1-(gamma-Glu-L-Cys(S-butyl)-Gly)-spermidine + ADP + phosphate
-
at 24% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-Glu-L-Cys(S-ethyl)-Gly + spermidine + ATP
N1-(gamma-Glu-L-Cys(S-ethyl)-Gly)-spermidine + ADP + phosphate
-
at 77% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-Glu-L-Cys(S-propyl)-Gly + spermidine + ATP
N1-(gamma-Glu-L-Cys(S-propyl)-Gly)-spermidine + ADP + phosphate
-
at 56% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-Glu-L-Ser-Gly + spermidine + ATP
N1-(gamma-Glu-L-Ser-Gly)-spermidine + ADP + phosphate
-
at 16% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-L-Glu-L-Ala-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Ala-Gly)-spermidine + ADP + phosphate
-
at 28% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-L-Glu-L-alpha-aminobutyryl-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-alpha-aminobutyryl-Gly)-spermidine
-
gamma-L-Glu-L-alpha-aminobutyryl-Gly i.e. ophthalmic acid
-
-
?
gamma-L-Glu-L-Cys(S-methyl)-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys(S-methyl)-Gly)-spermidine + ADP + phosphate
-
at 74% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
gamma-L-Glu-L-Cys-Gly + spermidine + MgATP2-
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + MgADP- + phosphate
gamma-L-Glu-L-Ile-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Ile-Gly)-spermidine + ADP + phosphate
-
at 70% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-L-Glu-L-Val-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Val-Gly)-spermidine + ADP + phosphate
-
at 88% of the activity with gamma-L-Glu-L-Cys-Gly
-
-
?
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
glutathionylspermidine + H2O
glutathione + spermidine
amidase activity
-
?
additional information
?
-
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + MgATP2-
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + MgADP- + phosphate
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + MgATP2-
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + MgADP- + phosphate
-
-
?
gamma-L-Glu-L-Cys-Gly + spermidine + MgATP2-
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + MgADP- + phosphate
-
substitution of the glycine part abolishes activity
-
?
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
synthesis of trypanothione, which is involved in maintaining intracellular thiol redox and in defense against oxidants
-
-
?
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
-
the enzyme is involved in the biosynthesis of the trypanosomatid-specific dithiol trypanothione
-
-
?
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
-
key enzyme that participates in the first of two similar steps of trypanothione biosynthesis
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
trypanothione synthase
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
specific for, the enzyme is distinct from the trypanothione synthase, which also catalyzes the reaction but converts glutathionylsperimidine further to trypanothione
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
glutathionylspermidine is an intermediate formed in the biosynthesis of trypanothione, an essential metabolite in defence against chemical and oxidative stress in the kinetoplastida
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
trypanothione synthase catalyzes both the reaction of glutathionylspermidine synthase, EC 6.3.1.8, and of trypanothione synthase, EC 6.3.1.9, in Trypanosoma brucei
-
-
?
additional information
?
-
the trypanothione synthase also converts glutathionylspermidine further to trypanothione catalyzing the reaction of EC 6.3.1.9
-
-
?
additional information
?
-
the trypanothione synthase also converts glutathionylspermidine further to trypanothione catalyzing the reaction of EC 6.3.1.9
-
-
?
additional information
?
-
-
the trypanothione synthase also converts glutathionylspermidine further to trypanothione catalyzing the reaction of EC 6.3.1.9
-
-
?
additional information
?
-
model of ter-reactant mechanism of GspS catalysis and postulated overview
-
-
?
additional information
?
-
-
model of ter-reactant mechanism of GspS catalysis and postulated overview
-
-
?
additional information
?
-
Escherichia coli proteins YgiC and YjfC, encoded by genes ygiC and yjfC, cannot synthesize G-Sp, GSH, or GSH intermediates, they are no glutathionylspermidine synthetase/amidases, but show ATP-hydrolysis activity
-
-
?
additional information
?
-
-
important reaction in defense against chemical and oxidant stress, thiol redox homeostasis, ribonucleotide metabolism, and drug resistance in parasitic kinetoplastids
-
-
?
additional information
?
-
-
the enzyme is important for several functions, e.g. for detoxification of H2O2 and organic hyperoxids, and ribonucleotide reduction
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
additional information
?
-
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
synthesis of trypanothione, which is involved in maintaining intracellular thiol redox and in defense against oxidants
-
-
?
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
-
the enzyme is involved in the biosynthesis of the trypanosomatid-specific dithiol trypanothione
-
-
?
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
?
-
key enzyme that participates in the first of two similar steps of trypanothione biosynthesis
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
trypanothione synthase
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
glutathionylspermidine is an intermediate formed in the biosynthesis of trypanothione, an essential metabolite in defence against chemical and oxidative stress in the kinetoplastida
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
-
-
?
glutathione + spermidine + ATP
glutathionylspermidine + ADP + phosphate
-
trypanothione synthase catalyzes both the reaction of glutathionylspermidine synthase, EC 6.3.1.8, and of trypanothione synthase, EC 6.3.1.9, in Trypanosoma brucei
-
-
?
additional information
?
-
the trypanothione synthase also converts glutathionylspermidine further to trypanothione catalyzing the reaction of EC 6.3.1.9
-
-
?
additional information
?
-
the trypanothione synthase also converts glutathionylspermidine further to trypanothione catalyzing the reaction of EC 6.3.1.9
-
-
?
additional information
?
-
-
the trypanothione synthase also converts glutathionylspermidine further to trypanothione catalyzing the reaction of EC 6.3.1.9
-
-
?
additional information
?
-
Escherichia coli proteins YgiC and YjfC, encoded by genes ygiC and yjfC, cannot synthesize G-Sp, GSH, or GSH intermediates, they are no glutathionylspermidine synthetase/amidases, but show ATP-hydrolysis activity
-
-
?
additional information
?
-
-
important reaction in defense against chemical and oxidant stress, thiol redox homeostasis, ribonucleotide metabolism, and drug resistance in parasitic kinetoplastids
-
-
?
additional information
?
-
-
the enzyme is important for several functions, e.g. for detoxification of H2O2 and organic hyperoxids, and ribonucleotide reduction
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2-[[([2-[(4-amino-4-carboxybutanoyl)amino]propanoyl]amino)methyl](hydroxy)phosphoryl]ethyl)(hydroxy)dioxophosphate(1-)
inhibits the reaction in the presence of spermidine
4-[(14-ammonio-5-hydroxy-1-methyl-5-oxido-2-oxo-6-oxa-3,10-diaza-5-phosphatetradec-1-yl)amino]-1-carboxy-4-oxobutan-1-aminium
-
4-[[2-([[[4-[(4-ammoniobutyl)amino]butyl](hydroxy)phosphoryl]methyl]amino)-1-methyl-2-oxoethyl]amino]-1-carboxy-4-oxobutan-1-aminium
-
buthionine sulfoximine
-
-
gamma-Aminobutyryl-L-Ala-Gly
-
5 mM, 10% inhibition
gamma-glutamyl-N-[[(3-aminopropoxy)(2-phosphonoethyl)phosphoryl]methyl]alaninamide
-
gamma-L-Glu-D-Phe-Gly
-
5 mM, 10% inhibition
gamma-L-Glu-L-Leu
-
5 mM, 10% inhibition
gamma-L-Glu-L-Leu-Gly
-
5 mM, 58% inhibition
gamma-L-Glu-L-leu-L-Ala
-
5 mM, 95% inhibition
gamma-L-Glu-L-Phe-Gly
-
5 mM, 73% inhibition
gamma-L-Glu-L-Ser-Gly
-
5 mM, 50% inhibition
gamma-L-Glu-L-Val
-
5 mM, 10% inhibition
gamma-L-Glu-L-Val-L-Ala
-
5 mM, 58% inhibition
gamma-L-glutamyl-L-cysteinyl-diaminopropionic acid
-
-
Glutaryl-L-Val-Gly
-
5 mM, 10% inhibition
Hydrogen O-[3-[N-(4-Aminobutyl)amino]propyl][[(gamma-glutamylalanyl)amino]methyl]phosphonate
-
-
L-beta-Asp-L-Leu-Gly
-
5 mM, 42% inhibition
L-beta-Asp-L-Val-Gly
-
5 mM, 15% inhibition
L-Cys-Gly
-
5 mM, 20% inhibition
N1-glutathionylspermidine analogs
-
selective inhibitors against EC 6.3.1.8 and EC 3.5.1.78 activities provide evidence of interdomain communication in the bifunctional enzyme
Non-polyamine-containing phosphoamidate
-
-
-
Phosphinate
behaves as a slow-binding bisubstrate inhibitor, competitive with respect to GSH and spermidine
phosphinate analogue of glutathionylspermidine
slow tight-binding inhibition
phosphonate
acts as a a simple ground state analogue of glutathione
phosphonate analogue of glutathionylspermidine
classical, linear competitive inhibition with respect to GSH
Polyamine-containing phosphapeptides
-
potent and selective
-
reduced trypanothione
-
-
additional information
-
a series of glutathione analogs where the glycine moiety is substituted for other amino acids can act as inhibitors
-
additional information
H2O2 leads to inhibition of the amidase activity, while the glutathionylspermidine synthase activity is almost unaffected
-
additional information
-
design, synthesis, and biochemical evaluation of phosphonate and phosphonamidate analogs of glutathionylspermidine as inhibitors
-
additional information
-
the enzyme mediates resistance to H2O2 and organic hyperoxids, and to trypanocidic drugs
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C79A
mutant retains synthetase activity, but loses amidase activity
C338A
increased Km compared to the wild type enzyme
E391A
increased Km compared to the wild type enzyme
E392A
increased Km compared to the wild type enzyme
K607A
increased Km compared to the wild type enzyme
R538A
increased Km compared to the wild type enzyme
R598A
decreased Km compared to the wild type enzyme
S335A
increased Km compared to the wild type enzyme
S337A
increased Km compared to the wild type enzyme
T441A
increased Km compared to the wild type enzyme
additional information
generation of a knockout GSPS mutant line by gene targeting, the mutant is viable and capable of replicating in both life cycle stages of the parasite, the extracellular promastigotes residing in the insect vector and the intracellular amastigotes thriving in mammalian hosts
additional information
-
generation of a knockout GSPS mutant line by gene targeting, the mutant is viable and capable of replicating in both life cycle stages of the parasite, the extracellular promastigotes residing in the insect vector and the intracellular amastigotes thriving in mammalian hosts
additional information
-
generation of a knockout GSPS mutant line by gene targeting, the mutant is viable and capable of replicating in both life cycle stages of the parasite, the extracellular promastigotes residing in the insect vector and the intracellular amastigotes thriving in mammalian hosts
-
additional information
-
enzyme downregulation leads to decreased growth rate of the parasite, increased H2O2 and tert-butylhydroperoxide sensitivity, enzyme knockdown leads to depletion of both trypanothione and glutathionylspermidine, and glutathione and polyamine accumulation, RNA interference method, overview
additional information
-
enzyme downregulation leads to increased trypanocidic drug sensitivity, enzyme knockdown leads to depletion of both trypanothione and glutathionylspermidine and glutathione accumulation, RNA interference method, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Tabor, H.; Tabor, C.W.
Glutathionylspermidine synthetase
Methods Enzymol.
17
815-817
1971
Escherichia coli
-
brenda
Nadeau, K.C.
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
-
brenda
Smith, K.; Nadeau, K.; Bradley, M.; Walsh, C.; Fairlamb, A.H.
Purification of glutathionylspermidine and trypanothione synthetase from Crithidia fasciculata
Protein Sci.
1
874-883
1992
Crithidia fasciculata
brenda
Tetaud, E.; Manai, F.; Barrett, M.P.; Nadeau, K.; Walsh, C.T.; Fairlamb, A.H.
Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata
J. Biol. Chem.
273
19383-19390
1998
Crithidia fasciculata, Crithidia fasciculata (P90518)
brenda
De Craecker, S.; Verbruggen, C.; Rajan, P.; Smith, K.; Haemers, A.; Fairlamb, A.H.
Characterization of the peptide substrate specificity of glutathionylspermidine synthetase from Crithidia fasciculata
Mol. Biochem. Parasitol.
84
25-32
1997
Crithidia fasciculata
brenda
Lin, C.H.; Chen, S.; Kwon, D.S.; Coward, J.K.; Walsh, C.T.
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
brenda
Chen, S.; Lin, C.H.; Kwon, D.S.; Walsh, C.T.; Coward, J.K.
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
brenda
Bollinger, J.M.; Kwon, D.S.; Huisman, G.W.; Kolter, R.; Walsh, C.T.
Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase
J. Biol. Chem.
270
14031-14041
1995
Escherichia coli
brenda
Oza, S.L.; Ariyanayagam, M.R.; Fairlamb, A.H.
Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata
Biochem. J.
364
679-686
2002
Crithidia fasciculata (P90518), Crithidia fasciculata
brenda
Amssoms, K.; Oza, S.L.; Augustyns, K.; Yamani, A.; Lambeir, A.M.; Bal, G.; Van der Veken, P.; Fairlamb, A.H.; Haemers, A.
Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2: Substitution of the glycine part
Bioorg. Med. Chem. Lett.
12
2703-2705
2002
Crithidia fasciculata
brenda
Ariyanayagam, M.R.; Oza, S.L.; Guther, M.L.S.; Fairlamb, A.H.
Phenotypic analysis of trypanothione synthetase knockdown in the African trypanosome
Biochem. J.
391
425-432
2005
Trypanosoma brucei
brenda
Comini, M.A.; Guerrero, S.A.; Haile, S.; Menge, U.; Lunsdorf, H.; Flohe, L.
Valdiation of Trypanosoma brucei trypanothione synthetase as drug target
Free Radic. Biol. Med.
36
1289-1302
2004
Trypanosoma brucei
brenda
Comini, M.; Menge, U.; Wissing, J.; Flohe, L.
Trypanothione synthesis in Crithidia revisited
J. Biol. Chem.
280
6850-6860
2005
Crithidia fasciculata (P90518), Crithidia fasciculata (Q5DM89), Crithidia fasciculata
brenda
Oza, S.L.; Shaw, M.P.; Wyllie, S.; Fairlamb, A.H.
Trypanothione biosynthesis in Leishmania major
Mol. Biochem. Parasitol.
139
107-116
2005
Leishmania major (AJ748279), Leishmania major
brenda
Pai, C.H.; Chiang, B.Y.; Ko, T.P.; Chou, C.C.; Chong, C.M.; Yen, F.J.; Chen, S.; Coward, J.K.; Wang, A.H.; Lin, C.H.
Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase
EMBO J.
25
5970-5982
2006
Escherichia coli (P0AES0), Escherichia coli
brenda
Oza, S.L.; Chen, S.; Wyllie, S.; Coward, J.K.; Fairlamb, A.H.
ATP-dependent ligases in trypanothione biosynthesis - kinetics of catalysis and inhibition by phosphinic acid pseudopeptides
FEBS J.
275
5408-5421
2008
Crithidia fasciculata (P90518), Crithidia fasciculata
brenda
Chiang, B.Y.; Chen, T.C.; Pai, C.H.; Chou, C.C.; Chen, H.H.; Ko, T.P.; Hsu, W.H.; Chang, C.Y.; Wu, W.F.; Wang, A.H.; Lin, C.H.
Protein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetase/amidase in redox regulation
J. Biol. Chem.
285
25345-25353
2010
Escherichia coli (P0AES0)
brenda
Pai, C.H.; Wu, H.J.; Lin, C.H.; Wang, A.H.
Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases
Protein Sci.
20
557-566
2011
Escherichia coli (P0AES0)
brenda
Chattopadhyay, M.K.; Chen, W.; Tabor, H.
Escherichia coli glutathionylspermidine synthetase/amidase: phylogeny and effect on regulation of gene expression
FEMS Microbiol. Lett.
338
132-140
2013
Escherichia coli K-12 (P0AES0)
brenda
Sui, L.; Warren, J.C.; Russell, J.P.; Stourman, N.V.
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 (P0AES0)
brenda
Sousa, A.F.; Gomes-Alves, A.G.; Benitez, D.; Comini, M.A.; Flohe, L.; Jaeger, T.; Passos, J.; Stuhlmann, F.; Tomas, A.M.; Castro, H.
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 (A4I1T8), Leishmania infantum, Leishmania infantum MHOM / MA / 67 / ITMAP263 (A4I1T8)
brenda