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Literature summary for 3.2.2.24 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DraG, expression in Escherichia coli strain BL21(DE3) | Azospirillum brasilense |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| recombinant DraG bound to substrate Azospirillum brasilense dinitrogenase, mixing of protein solution with reservoir solution, containing 0.1M HEPES, pH 7.5, 15% w/v PEG 20000, in a 1:1 ratio,2-3 days X-ray diffraction structure determination and analysis at 2.5 resolution, modelling | Azospirillum brasilense |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mn2+ | the enzyme shows an all-alpha-helix structure with two magnesium ions located in the active site | Azospirillum brasilense |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP-ribosyl-[dinitrogen reductase] + H2O | Azospirillum brasilense | - |
ADP-ribose + [dinitrogen reductase] | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Azospirillum brasilense | A7XNI2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant DraG from Escherichia coli strain BL21(DE3) | Azospirillum brasilense |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP-ribosyl-[dinitrogen reductase] + H2O | - |
Azospirillum brasilense | ADP-ribose + [dinitrogen reductase] | - |
? | |
| ADP-ribosyl-[dinitrogen reductase] + H2O | substrate is the Azospirillum brasilense dinitrogenase, DraG on Arg101, modeling of the binding of the substrate ADP-ribosyl moiety to DraG, active site structure, overview | Azospirillum brasilense | ADP-ribose + [dinitrogen reductase] | - |
? | |
| additional information | the enzyme acts specifically towards a mono-ADP-ribosylated substrate, structure-function relationship, overview | Azospirillum brasilense | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme hows an all-alpha-helix structure with two magnesium ions located in the active site. Structure comparison to the human ARH3 | Azospirillum brasilense |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADP-ribosylhydrolase | - |
Azospirillum brasilense |
| dinitrogenase reductase-activating glycohydrolase | - |
Azospirillum brasilense |
| More | the enzyme is a member of the ADP-ribosylhydrolase family | Azospirillum brasilense |
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 | Azospirillum brasilense |
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