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Literature summary for 4.3.2.7 extracted from

  • Fujiwara, S.; Kawazoe, T.; Ohnishi, K.; Kitagawa, T.; Popa, C.; Valls, M.; Genin, S.; Nakamura, K.; Kuramitsu, Y.; Tanaka, N.; Tabuchi, M.
    RipAY, a plant pathogen effector protein, exhibits robust gamma-glutamyl cyclotransferase activity when stimulated by eukaryotic thioredoxins (2016), J. Biol. Chem., 291, 6813-6830 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli and Saccharomyces cerevisiae Ralstonia solanacearum

Organism

Organism UniProt Comment Textmining
Ralstonia solanacearum
-
-
-
Ralstonia solanacearum OE1-1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione
-
 Ralstonia solanacearum L-cysteinylglycine + 5-oxo-L-proline
-
 ?
glutathione
-
 Ralstonia solanacearum OE1-1 L-cysteinylglycine + 5-oxo-L-proline
-
 ?

Synonyms

Synonyms Comment Organism
RipAY
-
 Ralstonia solanacearum
RSp1022
-
 Ralstonia solanacearum

General Information

General Information Comment Organism
physiological function expression of RipAY causes growth inhibition of yeast Saccharomyces cerevisiae, and a decrease of 70% of the intracellular glutathione level. Addition of exogenous glutathione does not restore RipAY-dependent growth inhibition. Inoculation of Ralstonia solanacearum into eggplant leaves causes a decrease in intracellular glutathione. In vitro, RipAY protein purified from a bacterial expression system does not exhibit any GGCT activity, whereas robust GGCT activity is seen upon its interaction with eukaryotic thioredoxins Ralstonia solanacearum