EC Number   |
General Information |
Reference |
|---|
   7.1.1.7 | physiological function |
besides its oxidase activity, cytochrome bd is a genuine quinol peroxidase that reduces hydrogen peroxide to water. The enzyme does not display catalase activity |
752197 |
| 7.1.1.7 | physiological function |
both cytochrome bd-type CydAB, EDC 7.1.1.7, and cytochrome aa3-type menaquinol QoxAB oxidase, EC 7.1.1.5, are used for respiration under different oxygen tensions. Possession of both terminal oxidases is important in infection. In air, the CydAB bd-type oxidase is essential for aerobic respiration and intracellular replication, and cydAB mutants are highly attenuated in mice. At 1% O2 (vol/vol), both oxidases are functional, and the presence of either is sufficient for aerobic respiration and intracellular replication. At 0.2% O2 (vol/vol), both oxidases are necessary for maximum growth |
-, 750736 |
| 7.1.1.7 | physiological function |
in respiratory mutants, both O2-consumption and aerobic growth are unaffected by up to 200 microM sulfide when cytochrome bd-I or bd-II enzyme actes as the only terminal oxidase. Wild-type Escherichia coli shows sulfide-insensitive respiration and growth under conditions favouring the expression of bd oxidases |
752188 |
| 7.1.1.7 | physiological function |
inactivation of cydA or cydB by gene disruption results in loss of d-heme absorbance at 631 nm. Inactivation of cydA has no effect on the ability of Mycobacterium smegmatis to exit from stationary phase at 37 or 42°C. No discernible growth defect of the mutant is observed under moderately aerobic conditions, while the mutant displays a significant growth disadvantage when cocultured with the wild type under extreme microaerophilia. The cydA mutant displays a competitive growth disadvantage in the presence of the terminal oxidase inhibitor, cyanide, when cocultured with wild type at 21% air saturation in an oxystat |
727738 |
| 7.1.1.7 | physiological function |
inactivation of cydA or cydB gene disruption results in loss of d-heme absorbance at 631 nm |
727738 |
| 7.1.1.7 | physiological function |
induction of cytochrome bd helps Salmonella grow and respire in the presence of inhibitory nitric oxide |
743207 |
| 7.1.1.7 | 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 |
743822 |
| 7.1.1.7 | physiological function |
the bd oxidase functions in controlling electron flux. A mutant lacking the cytochrome bd oxidase shows developmental defects during growth on buffered rich medium plates with glucose as the energy substrate. Cytochrome bd oxidase is essential for the bacterium to grow and complete its developmental cycle under oxygen limitation |
-, 750975 |
| 7.1.1.7 | physiological function |
the enzyme contributes to bacterial resistance to nitric oxide and hydrogen peroxide |
741966 |
| 7.1.1.7 | physiological function |
the enzyme contributes to Escherichia coli survival in the mouse bladder |
-, 743822 |
