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Literature summary for 3.2.2.19 extracted from
- Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket (2009), J. Mol. Biol., 390, 737-746.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | structure-function relationship, overview | Homo sapiens | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | structure comparison to the Azospirillum brasilense enzyme DraG | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADP-ribosylhydrolase | - |
Homo sapiens |
| ADP-ribosylhydrolase 3 | - |
Homo sapiens |
| ARH3 | - |
Homo sapiens |
| More | the enzyme is a member of the ADP-ribosylhydrolase family | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | protein-reversible ADP-ribosylation is an important posttranslational modification used to control enzymatic and protein activity in different biological systems. This modification regulates nitrogenase activity in several nitrogen-fixing bacterial species. ADP-ribosylation is catalyzed by ADP-ribosyltransferases and is reversed by ADP-ribosylhydrolases | Homo sapiens |
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Release 2023.1 (January 2023)
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