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Literature summary for 1.11.1.24 extracted from

  • Jonsson, A.; Teixeira, P.F.; Nordlund, S.
    A novel peroxiredoxin activity is located within the C-terminal end of Rhodospirillum rubrum adenylyltransferase (2008), J. Bacteriol., 190, 434-437.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.24

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)pLysS cells Rhodospirillum rubrum

Protein Variants

Protein Variants Comment Organism
C102S activity is similar to the wild type enzyme Rhodospirillum rubrum
C48S reduced activity Rhodospirillum rubrum
C48S/C102S reduced activity Rhodospirillum rubrum

Organism

Organism UniProt Comment Textmining
Rhodospirillum rubrum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2 + reduced dithiothreitol
-
 Rhodospirillum rubrum H2O + oxidized dithiothreitol
-
 ?

Synonyms

Synonyms Comment Organism
Ahp peroxiredoxin activity is located within the carboxyl-terminal AhpC/thiol-specific antioxidant domain (Ahp) of Rhodospirillum rubrum adenylyltransferase GlnE Rhodospirillum rubrum

Cofactor

Cofactor Comment Organism Structure
thioredoxin
-
 Rhodospirillum rubrum