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Literature summary for 2.4.2.30 extracted from

  • Masignani, V.; Balducci, E.; Di Marcello, F.; Savino, S.; Serruto, D.; Veggi, D.; Bambini, S.; Scarselli, M.; Arico, B.; Comanducci, M.; Adu-Bobie, J.; Giuliani, M.M.; Rappuoli, R.; Pizza, M.
    NarE: a novel ADP-ribosyltransferase from Neisseria meningitidis (2003), Mol. Microbiol., 50, 1055-1067.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli as a histidine-tag fusion protein Neisseria meningitidis

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm despite the absence of a signal peptide, the protein is efficiently exported into periplasm Neisseria meningitidis
-
-

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information narE possesses ADP-ribosylating and NAD-glycohydrolase activities Neisseria meningitidis ?
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?

Synonyms

Synonyms Comment Organism
NarE
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Neisseria meningitidis