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Literature summary for 7.1.1.7 extracted from

  • Shepherd, M.; Achard, M.E.; Idris, A.; Totsika, M.; Phan, M.D.; Peters, K.M.; Sarkar, S.; Ribeiro, C.A.; Holyoake, L.V.; Ladakis, D.; Ulett, G.C.; Sweet, M.J.; Poole, R.K.; McEwan, A.G.; Schembri, M.A.
    The cytochrome bd-I respiratory oxidase augments survival of multidrug-resistant Escherichia coli during infection (2016), Sci. Rep., 6, 35285 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.1.7

Application

Application Comment Organism
medicine cytochrome bd-I respiratory oxidase is the main contributor to NO tolerance and host colonisation under microaerobic conditions. Uropathogenic Escherichia coli strains have acquired a host of specialized mechanisms to evade nitrosative stresses Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Escherichia coli P0ABJ9 and P0ABK2 and P56100 P0ABJ9 i.e. subunit cydA, P0ABK2 i.e. subunit cydB, P56100 i.e. subunit cydX
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Escherichia coli EC958
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-
-

Synonyms

Synonyms Comment Organism
CydAB
-
 Escherichia coli
cytochrome bd-I respiratory oxidase
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme contributes to Escherichia coli survival in the mouse bladder Escherichia coli
physiological function loss of the flavohemoglobin Hmp and cytochrome bd-I elicit high sensitivity to NO-mediated growth inhibition. The subunits cydAB mutant displays an attenuated colonisation phenotype in a mouse model after 2 days Escherichia coli