Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.2.30 extracted from

  • Koehler, C.; Carlier, L.; Veggi, D.; Balducci, E.; Di Marcello, F.; Ferrer-Navarro, M.; Pizza, M.; Daura, X.; Soriani, M.; Boelens, R.; Bonvin, A.M.
    Structural and biochemical characterization of NarE, an iron-containing ADP-ribosyltransferase from Neisseria meningitidis (2011), J. Biol. Chem., 286, 14842-14851.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Neisseria meningitidis

Protein Variants

Protein Variants Comment Organism
E111D catalytic activity close to wild-type Neisseria meningitidis
E120D catalytic activity highly decreased Neisseria meningitidis
R7K catalytic activity highly decreased Neisseria meningitidis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme binds iron through a Fe-S center, which is crucial for the catalytic activity Neisseria meningitidis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
16000
-
-
Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NAD+ + (ADP-D-ribosyl)n-acceptor agmatine as ADPribose acceptor is used Neisseria meningitidis nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
?

Synonyms

Synonyms Comment Organism
NarE
-
Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Neisseria meningitidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Neisseria meningitidis