A novel peroxiredoxin activity is located within the C-terminal end of Rhodospirillum rubrum adenylyltransferase.
Adenylyltransferase (GlnE) catalyzes the reversible adenylylation of glutamine synthetase. In this report we present, for the first time, evidence for a peroxiredoxin activity of Rhodospirillum rubrum GlnE, through the carboxyl-terminal AhpC/thiol-specific antioxidant (TSA) domain. The combination of GlnE and AhpC/TSA domains within the same polypeptide constitutes a unique domain architecture that has not previously been identified among proteobacteria.
Jonsson
Anders
A
Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Teixeira
Pedro Filipe
PF
Nordlund
Stefan
S
D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D007700:Kinetics; D009612:Nicotinamide-Nucleotide Adenylyltransferase / Q000737:chemistry / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism; D054464:Peroxiredoxins / Q000378:metabolism*; D010788:Photosynthesis; D017382:Reactive Oxygen Species / Q000378:metabolism; D012247:Rhodospirillum rubrum / Q000201:enzymology*
D017382:Reactive Oxygen Species; D006861:Hydrogen Peroxide; D010544:Peroxidases; D054464:Peroxiredoxins; D009612:Nicotinamide-Nucleotide Adenylyltransferase; D005974:Glutamate-Ammonia Ligase