3.5.1.78: Glutathionylspermidine amidase
This is an abbreviated version!
For detailed information about Glutathionylspermidine amidase, go to the full flat file.
Word Map on EC 3.5.1.78
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3.5.1.78
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trypanosomatids
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gsh
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leishmania
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polyamine
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histidine-dependent
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fasciculata
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gamma-glu-cys-gly
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synthetases
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tetrahedral
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n1,n8-bisglutathionylspermidine
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crithidia
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kinetoplastida
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s-thiolation
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anti-parasitic
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thiol-redox
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druggable
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neglected
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sulfenic
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slow-binding
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tripeptide
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phosphonate
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protozoa
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ligases
- 3.5.1.78
-
trypanosomatids
- gsh
- leishmania
- polyamine
-
histidine-dependent
- fasciculata
- gamma-glu-cys-gly
- synthetases
-
tetrahedral
-
n1,n8-bisglutathionylspermidine
-
crithidia
- kinetoplastida
-
s-thiolation
-
anti-parasitic
-
thiol-redox
-
druggable
-
neglected
-
sulfenic
-
slow-binding
- tripeptide
- phosphonate
-
protozoa
- ligases
Reaction
Synonyms
Amidase, glutathionylspermidine, Glutathionylspermidine amidohydrolase (spermidine-forming), Glutathionylspermidine amidohydrolase [spermidine-forming], Glutathionylspermidine synthetase/amidase, GSP amidase, Gsp synthetase/amidase, GspA, GspSA, GSS, trypanothione synthetase-amidase
ECTree
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Inhibitors
Inhibitors on EC 3.5.1.78 - Glutathionylspermidine amidase
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gamma-Glu-Ala-Gly-CHO
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most probably captures Cys59 and accumulates as the tetrahedral adduct in the amidase active site. Binding of phosphinophosphate in the Gsp synthetase active site potentiates the inhibition affinity for the aldehyde at the Gsp amidase active site by two orders of magnitude
L-gamma-glutamyl-5-azido-N-(3-[[(4-methylphenyl)sulfonyl]oxy]-2-oxopropyl)-L-norleucinamide
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L-gamma-glutamyl-5-azido-N-[3-(benzoyloxy)-2-oxopropyl]-L-norleucinamide
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L-gamma-glutamyl-N-[3-(benzoyloxy)-2-oxopropyl]-6-[4-([[5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoyl]amino]methyl)-1H-1,2,3-triazol-1-yl]-L-norleucinamide
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Polyamine-containing phosphopeptides
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potent and selective inhibitors, which selectively inhibit the synthetase domain over the amidase domain
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H2O2
50% inhibition with 0.25 mM. Inactivation is above 95% with 0.5 mM H2O2 for 5 min. Cysteine thiol of the GspSA amidase active-site nucleophile Cys59 is transiently inactivated by H2O2 oxidation to sulfenic acid which leads to an accumulation of glutathionylspermidine and an increased level of glutathionylspermidine S-thiolated proteins after oxidative stress. The hypersensitivities of GspSA and GspSA/glutaredoxin null mutants to H2O2 support the idea that GspSA and glutaredoxin act synergistically to regulate the redox environment of Escherichia coli