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Literature summary for 2.4.2.31 extracted from

  • Tsurumura, T.; Tsumori, Y.; Qiu, H.; Oda, M.; Sakurai, J.; Nagahama, M.; Tsuge, H.
    Arginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complex (2013), Proc. Natl. Acad. Sci. USA, 110, 4267-4272.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Clostridium perfringens

Crystallization (Commentary)

Crystallization (Comment) Organism
high-resolution structures of NAD(+)-iota toxin-actin and iota toxin-ADPR-actin obtained by soaking apo-iota toxin-actin crystal with NAD(+) under different conditions and structures of mutants E378S, E380A, E380S in complex with actin. The structures of NAD(+)-iota toxin-actin and iota toxin-ADPR-actin represent the pre- and postreaction states. A simple strain-alleviation model explains arginine ADP ribosylation occuring via two oxocarbenium ion intermediates Clostridium perfringens

Protein Variants

Protein Variants Comment Organism
E378S mutation eliminates ADP-ribosylation activity and reduces the weak NAD+ glycohydrolase activity in absence of actin to 50% Clostridium perfringens
E380A mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin Clostridium perfringens
E380S mutation eliminates both ADP-ribosylation activity and the weak NAD+ glycohydrolase activity in absence of actin Clostridium perfringens

Organism

Organism UniProt Comment Textmining
Clostridium perfringens Q46220
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in absence of actin, enzyme displays weak NAD+ glycohydrolase activity Clostridium perfringens ?
-
?
NAD+ + [actin]-L-arginine177
-
Clostridium perfringens nicotinamide + [actin]-N-(ADP-D-ribosyl)-L-arginine177 + H+
-
?