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Literature summary for 2.4.2.30 extracted from

  • Galloway, D.R.; Hedstrom, R.C.; McGowan, J.L.; Kessler, S.P.; Wozniak, D.J.
    Biochemical analysis of CRM 66. A nonfunctional Pseudomonas aeruginosa exotoxin A (1989), J. Biol. Chem., 264, 14869-14873.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
additional information in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
Y426H in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
CRM66 Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NAD+ + (ADP-D-ribosyl)n-(EF-2) in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity Pseudomonas aeruginosa nicotinamide + (ADP-D-ribosyl)n+1-(EF-2)
-
 ?

Synonyms

Synonyms Comment Organism
CRM66
-
 Pseudomonas aeruginosa