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Literature summary extracted from
- Indications for post-translational regulation of Vitis vinifera L. arginine decarboxylase (2001), Plant Mol. Biol., 45, 669-678.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.1.19 | expression in Escherichia coli | Vitis vinifera |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.19 | L-arginine | Vitis vinifera | level and/or activity is posttranslationally regulated | agmatine + CO2 | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.19 | Vitis vinifera | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 4.1.1.19 | proteolytic modification | existence of an autocatalytic proteolytic property of ADC protein, which possibly regulates posttranslationally the levels and/or the activity of ADC enzyme | Vitis vinifera |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.19 | L-arginine | level and/or activity is posttranslationally regulated | Vitis vinifera | agmatine + CO2 | - |
? | |
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Release 2023.1 (January 2023)
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