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Literature summary for 4.1.1.19 extracted from
- Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms (2003), Structure, 11, 285-294.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Methanocaldococcus jannaschii |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallization of enzyme labeled with selenomethionine, enzyme-agmatine complex and S53A mutant structure, hanging drop method, determination of structure at 1.4 A, crystals belong to space group P2, with cell dimensions a = 56.77 A, b = 92.99 A, c = 87.23 A, and beta = 94.84° | Methanocaldococcus jannaschii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S53A | nonprocessing mutant enzyme | Methanocaldococcus jannaschii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanocaldococcus jannaschii | Q57764 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains. Asn47, Ser52, Ser53, Ile54, and Glu109 are proposed to play roles in the self-processing reaction | Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arginine | - |
Methanocaldococcus jannaschii | agmatine + CO2 | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| trimer | - |
Methanocaldococcus jannaschii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PvlArgDC | - |
Methanocaldococcus jannaschii |
| pyruvoyl-dependent arginine decraboxylase | - |
Methanocaldococcus jannaschii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains | Methanocaldococcus jannaschii |
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