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Literature summary for 7.1.1.3 extracted from

  • Shepherd, M.; Sanguinetti, G.; Cook, G.M.; Poole, R.K.
    Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism (2010), J. Biol. Chem., 285, 18464-18472.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Escherichia coli BW25113
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Synonyms

Synonyms Comment Organism
AppBC
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Escherichia coli
CydAB
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Escherichia coli
cytochrome bd-I quinol oxidase
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Escherichia coli
cytochrome bd-II quinol oxidase
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme
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Escherichia coli

General Information

General Information Comment Organism
malfunction loss of cytochrome bd-I oxidase subunit II (gene cydB) causes diminished respiration rates, impaired motility and enhanced acid resistance. CydB cells contain elevated heme d, particularly at low pH. The GABA/glutamate gadC antiporter is highly up-regulated in cydB cells. Eschrichia coli can compensate for the loss of cytochrome bd-I activity Escherichia coli
physiological function cytochrome bd-II-mediated quinol oxidation prevents the accumulation of NADH, whereas GABA synthesis/antiport maintains the proton motive force for ATP production Escherichia coli