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General Information
Commentary
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physiological function
Escherichia coli is a Gram-negative bacterium that can use nitrate during anaerobic respiration. The catalytic subunit of the involved periplasmic nitrate reductase NapA contains two types of redox cofactor and is exported across the cytoplasmic membrane by the twin-arginine protein transport pathway
physiological function
napAB expression is required for anaerobic growth recovery by DELTAnarXL (a deletion encompassing the bulk of narXL)
physiological function
Salmonella enterica serovar Typhimurium uses the periplasmic nitrate reductase to support its growth on the low nitrate concentrations encountered in the gut, a strategy that may be shared with other enteric pathogens
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap-deficient mutant KD102 shows increased diauxic lag when switched from aerobic to anoxic respiration, suggesting Nap is responsible for shorter lags and helps in adaptation to anoxic metabolism after transition from aerobic conditions
physiological function
the single subunit nitrate reductase (Nap) appears to be involved in both the assimilatory and the dissimilatory denitrification pathways. The role in the former is supported by the methanol growth deficiency of the mutant when nitrate is used as a nitrogen source, and the role in the latter is supported by the lack of accumulation of N2O in the mutant
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modeling of regulation of nap and nos genes by NasST system in Bradyrhizobium japonicum strain USDA110 and nasS and Nos++ mutant strains
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NapD is a small cytoplasmic protein that is essential for the activity of the periplasmic nitrate reductase and binds tightly to the twinarginine signal peptide of NapA. NapA is structured in its unbound form. The NapA signal peptide undergoes conformational rearrangement upon interaction with NapD. NapA is at least partially folded when bound by its NapD partner. The NapD chaperone binds primarily at the NapA signal peptide in this system and points towards a role for NapD in the insertion of the molybdenum cofactor
Results 1 - 10 of 26 > >>