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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.13.3
-
 Shewanella oneidensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.13.3 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
2.7.13.3 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
2.7.13.3 additional information not inhibited by Fe2+ Shewanella oneidensis

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Shewanella oneidensis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.13.3
-
 Shewanella oneidensis

Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 SO2145
-
 Shewanella oneidensis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.13.3 0.009
-
 pH 8.0, 25°C Shewanella oneidensis Fe(II)-NO complex
2.7.13.3 0.084
-
 pH 8.0, 25°C Shewanella oneidensis Fe(II)-CO complex