Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.1.8 extracted from

  • 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 (2010), J. Biol. Chem., 285, 25345-25353.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
additional information H2O2 leads to inhibition of the amidase activity, while the glutathionylspermidine synthase activity is almost unaffected Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AES0 bifunctional glutathionylspermidine synthetase/amidase
-

Synonyms

Synonyms Comment Organism
GspSA
-
Escherichia coli

General Information

General Information Comment Organism
physiological function hypersensitivities of the GspSA/glutaredoxin null mutants to H2O2 support the idea that GspSA and Grx synergistically defend against oxidative damage Escherichia coli