Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.
Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.
products of the coupled reaction of Gsp amidase and glutathione reductase: spermidine, glutathionylspermidine-glutathione mixed disulfide, and glutathione disulfide are generated
bifunctional enzyme that catalyzes the ATP-dependent formation and hydrolysis of glutathionylspermidine, a conjugate of glutathione and spermidine. Proteins YgiC and YjfC, encoded by genes ygiC and yjfC, show ATPase activity, but are not glutathionylspermidine synthetases
bifunctional enzyme that catalyzes the ATP-dependent formation and hydrolysis of glutathionylspermidine, a conjugate of glutathione and spermidine. Proteins YgiC and YjfC, encoded by genes ygiC and yjfC, show ATPase activity, but are not glutathionylspermidine synthetases
glutathionylspermidine S-thiolated peptides and proteins are tested as substrates. The protein substrates are treated with disulfide or biotinated glutathionylspermidine to generate biotin-labeled glutathionylspermidine S-thiolated proteins for the detection with an anti-biotin antibody after the reaction with the GspSA. A variety of glutathionylspermidine-derivatized substrates are hydrolyzed yielding spermidine and glutathione S-thiolated protein/peptides
bifunctional enzyme that catalyzes the ATP-dependent formation and hydrolysis of glutathionylspermidine, a conjugate of glutathione and spermidine. Proteins YgiC and YjfC, encoded by genes ygiC and yjfC, show ATPase activity, but are not glutathionylspermidine synthetases
bifunctional enzyme that catalyzes the ATP-dependent formation and hydrolysis of glutathionylspermidine, a conjugate of glutathione and spermidine. Proteins YgiC and YjfC, encoded by genes ygiC and yjfC, show ATPase activity, but are not glutathionylspermidine synthetases
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
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
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
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
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
2 * 45000, SDS-PAGE, homodimer in which each monomer consists of two distinct domains. The C-terminal domain is responsible for the synthesis of glutathionylspermidine while the N-terminal domain catalyzes the hydrolysis of the conjugate
2 * 45000, SDS-PAGE, homodimer in which each monomer consists of two distinct domains. The C-terminal domain is responsible for the synthesis of glutathionylspermidine while the N-terminal domain catalyzes the hydrolysis of the conjugate
hanging gamma-drop vapor diffusion method, structure of Leishmania major trypanothione synthetase-amidase, determined in three crystal forms, reveals two catalytic domains
gene gsp, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene gss, phylogenetic and global transcriptome analyses, 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
Aldehyde and phosphinate analogs of glutathione and glutathionylspermidine: potent, selective binding inhibitors of the E. coli bifunctional glutathionylspermidine synthetase/amidase
Design, synthesis, and biochemical evaluation of phosphonate and phosphonamidate analogs of glutathionylspermidine as inhibitors of glutathionylspermidine synthetase/amidase from Escherichia coli
Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase
Evidence for a glutathionyl-enzyme intermediate in the amidase activity of the bifunctional glutathionylspermidine synthetase/amidase from Escherichia coli
Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases