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Literature summary for 7.4.2.5 extracted from

  • Huang, Y.J.; Wang, H.; Gao, F.B.; Li, M.; Yang, H.; Wang, B.; Tai, P.C.
    Fluorescein analogues inhibit SecA ATPase: the first sub-micromolar inhibitor of bacterial protein translocation (2012), ChemMedChem, 7, 571-577.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
eosin Y
-
Escherichia coli
erythrosin B the potency in inhibiting the truncated SecA ATPase correlates with the ability to inhibit the biologically relevant protein translocation activity of SecA and also translates into antibacterial effects Escherichia coli
Rose bengal the potency in inhibiting the truncated SecA ATPase correlates with the ability to inhibit the biologically relevant protein translocation activity of SecA and also translates into antibacterial effects Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0005
-
truncated SecA without the C-terminal regulatory domain, pH 7.6, 40°C Escherichia coli Rose bengal
0.002
-
truncated SecA without the C-terminal regulatory domain, 40°C, pH 7.6 Escherichia coli erythrosin B
0.025
-
truncated SecA without the C-terminal regulatory domain, 40°C, pH 7.6 Escherichia coli eosin Y