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
-
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
- 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
Advanced search results
General Information
General Information on EC 3.5.1.78 - Glutathionylspermidine amidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
metabolism
microarray studies comparing gss+ and DELTAgss strains of Escherichia coli show that a large number of genes are either upregulated (76 genes more than 3fold) or downregulated (35 genes more than 3fold) by the loss of the gss gene. Most significant categories of up-regulated genes include sulfur utilization, glutamine and succinate metabolism, polyamine and arginine metabolism, and purine and pyrimidine metabolism
additional information
phylogenetic distribution of Gss: Gss sequences are largely limited to certain bacteria and kinetoplastids, and are absent in a variety of invertebrate and vertebrate species, archaea, plants and some eubacteria
evolution
the synthetase domain of GspSA belongs to the class of ATP-grasp structural domains. Proteins YgiC and YjfC proteins show 51% identity between themselves and 28% identity to the synthetase domain of the GspSA enzyme, but do not show any glutathionylspermidine synthetase/amidase enzyme activity
comparison of catalytic properties of recombinant purified proteins GspSA, YgiC, and YjfC, overview
additional information
-
comparison of catalytic properties of recombinant purified proteins GspSA, YgiC, and YjfC, overview