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Literature summary for 2.4.2.31 extracted from
- Auto ADP-ribosylation of NarE, a Neisseria meningitidis ADP-ribosyltransferase, regulates its catalytic activities (2013), FASEB J., 27, 4723-4730.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Neisseria meningitidis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C11S | the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme | Neisseria meningitidis |
| C128S | the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity | Neisseria meningitidis |
| C130S | the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme | Neisseria meningitidis |
| C67S | the mutant does not have a stable Fe-S cluster and reduced auto-ADP-ribosylation activity | Neisseria meningitidis |
| E109D | the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme | Neisseria meningitidis |
| E111D | the mutation results in an auto-ADP-ribosylation comparable to the wild type enzyme | Neisseria meningitidis |
| E120D | the mutant has no auto-ADP-ribosylation ability | Neisseria meningitidis |
| R7K | the mutant has no auto-ADP-ribosylation ability | Neisseria meningitidis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| novobiocin | - |
Neisseria meningitidis |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | required for activity | Neisseria meningitidis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 18000 | - |
x * 18000, SDS-PAGE | Neisseria meningitidis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Neisseria meningitidis | the enzyme can perform auto-ADP-ribosylation. The auto-ADP-ribosylation site occurs preferentially on the R7 residue | ? | - |
? | |
| NAD+ + polyarginine | Neisseria meningitidis | - |
nicotinamide + Nomega-(ADP-D-ribosyl)-polyarginine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Neisseria meningitidis | Q9JZ10 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA column chromatography | Neisseria meningitidis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme can perform auto-ADP-ribosylation. The auto-ADP-ribosylation site occurs preferentially on the R7 residue | Neisseria meningitidis | ? | - |
? | |
| additional information | the enzyme also exhibits NADase activity which produces free ADP-ribose that can covalently bind to lysine | Neisseria meningitidis | ? | - |
? | |
| NAD+ + polyarginine | - |
Neisseria meningitidis | nicotinamide + Nomega-(ADP-D-ribosyl)-polyarginine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 18000, SDS-PAGE | Neisseria meningitidis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADP-ribosyltransferase | - |
Neisseria meningitidis |
| NarE | - |
Neisseria meningitidis |
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Release 2023.1 (January 2023)
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