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Literature summary extracted from

  • Picchianti, M.; Del Vecchio, M.; Di Marcello, F.; Biagini, M.; Veggi, D.; Norais, N.; Rappuoli, R.; Pizza, M.; Balducci, E.
    Auto ADP-ribosylation of NarE, a Neisseria meningitidis ADP-ribosyltransferase, regulates its catalytic activities (2013), FASEB J., 27, 4723-4730.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.31 expressed in Escherichia coli BL21(DE3) cells Neisseria meningitidis

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.31 C11S the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme Neisseria meningitidis
2.4.2.31 C128S the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity Neisseria meningitidis
2.4.2.31 C130S the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme Neisseria meningitidis
2.4.2.31 C67S the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity Neisseria meningitidis
2.4.2.31 E109D the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme Neisseria meningitidis
2.4.2.31 E111D the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme Neisseria meningitidis
2.4.2.31 E120D the mutant has no auto-ADP-ribosylation ability Neisseria meningitidis
2.4.2.31 R7K the mutant has no auto-ADP-ribosylation ability Neisseria meningitidis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.31 novobiocin
-
 Neisseria meningitidis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.31 Iron required for activity Neisseria meningitidis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.31 18000
-
 x * 18000, SDS-PAGE Neisseria meningitidis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.31 additional information Neisseria meningitidis the enzyme can perform auto-ADP-ribosylation. The auto-ADP-ribosylation site occurs preferentially on the R7 residue ?
-
 ?
2.4.2.31 NAD+ + polyarginine Neisseria meningitidis
-
 nicotinamide + Nomega-(ADP-D-ribosyl)-polyarginine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.31 Neisseria meningitidis Q9JZ10
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.31 Ni-NTA column chromatography Neisseria meningitidis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.31 additional information the enzyme can perform auto-ADP-ribosylation. The auto-ADP-ribosylation site occurs preferentially on the R7 residue Neisseria meningitidis ?
-
 ?
2.4.2.31 additional information the enzyme also exhibits NADase activity which produces free ADP-ribose that can covalently bind to lysine Neisseria meningitidis ?
-
 ?
2.4.2.31 NAD+ + polyarginine
-
 Neisseria meningitidis nicotinamide + Nomega-(ADP-D-ribosyl)-polyarginine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.31 ? x * 18000, SDS-PAGE Neisseria meningitidis

Synonyms

EC Number Synonyms Comment Organism
2.4.2.31 ADP-ribosyltransferase
-
 Neisseria meningitidis
2.4.2.31 NarE
-
 Neisseria meningitidis