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Literature summary extracted from

  • Rocha, C.L.; Coburn, J.; Rucks, E.A.; Olson, J.C.
    Characterization of Pseudomonas aeruginosa exoenzyme S as a bifunctional enzyme in J774A.1 macrophages (2003), Infect. Immun., 71, 5296-5305.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.30 NAD+ + (ADP-D-ribosyl)n-RalA Pseudomonas aeruginosa ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex nicotinamide + (ADP-D-ribosyl)n+1-RalA
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Organism

EC Number Organism UniProt Comment Textmining
2.4.2.30 Pseudomonas aeruginosa
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Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.30 NAD+ + (ADP-D-ribosyl)n-RalA
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Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-RalA
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2.4.2.30 NAD+ + (ADP-D-ribosyl)n-RalA ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-RalA
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?

Synonyms

EC Number Synonyms Comment Organism
2.4.2.30 ADPRT
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Pseudomonas aeruginosa
2.4.2.30 exoenzyme S
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Pseudomonas aeruginosa