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Literature summary for 4.1.1.19 extracted from
- Arginine decarboxylase of oats is clipped from a precursor into two polypeptides found in the soluble enzyme (1992), Plant Physiol., 100, 146-152.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Avena sativa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Avena sativa | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arginine | - |
Avena sativa | agmatine + CO2 | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the full-length 66000 MW arginine decarboxylase polypeptide is synthesized and then cleaved to produce a 42000 MW polypeptide containing the original terminus and a 24000 polypeptide containing the original carboxyl terminus. Both of these are found in the enzyme and held together by disulfide bonds | Avena sativa |
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Release 2023.1 (January 2023)
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