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Literature summary for 2.7.13.3 extracted from

  • Erbil, W.K.; Price, M.S.; Wemmer, D.E.; Marletta, M.A.
    A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation (2009), Proc. Natl. Acad. Sci. USA, 106, 19753-19760.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.3

Cloned(Commentary)

Cloned (Comment) Organism
-
 Shewanella oneidensis

Inhibitors

Inhibitors Comment Organism Structure
Fe(II)-CO complex the Fe(II)-CO complex of the heme nitric oxide/oxygen protein inhibits the autophosphorylation of the operon-associated histidine kinase Shewanella oneidensis
Fe(II)-NO complex the Fe(II)-NO complex of the heme nitric oxide/oxygen protein inhibits the autophosphorylation of the operon-associated histidine kinase, whereas the ligand-free heme nitric oxide/oxygen protein has no effect on the kinase Shewanella oneidensis
additional information not inhibited by Fe2+ Shewanella oneidensis

Organism

Organism UniProt Comment Textmining
Shewanella oneidensis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Shewanella oneidensis

Synonyms

Synonyms Comment Organism
SO2145
-
 Shewanella oneidensis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.009
-
 pH 8.0, 25°C Shewanella oneidensis Fe(II)-NO complex
0.084
-
 pH 8.0, 25°C Shewanella oneidensis Fe(II)-CO complex