Cloned (Comment) | Organism |
---|---|
gene ADC1, sequence comparisons | Synechocystis sp. PCC 6803 |
gene ADC2, sequence comparisons | Synechocystis sp. PCC 6803 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine | Synechocystis sp. PCC 6803 | - |
agmatine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. PCC 6803 | P72587 | - |
- |
Synechocystis sp. PCC 6803 | P74576 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine | - |
Synechocystis sp. PCC 6803 | agmatine + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the enzyme dimer is stablized by the disulfide bridge involving Cys196 | Synechocystis sp. PCC 6803 |
Synonyms | Comment | Organism |
---|---|---|
ADC | - |
Synechocystis sp. PCC 6803 |
ADC 1 | - |
Synechocystis sp. PCC 6803 |
ADC 2 | - |
Synechocystis sp. PCC 6803 |
biosynthetic arginine decarboxylase 1 | UniProt | Synechocystis sp. PCC 6803 |
biosynthetic arginine decarboxylase 2 | UniProt | Synechocystis sp. PCC 6803 |
slr0662 | - |
Synechocystis sp. PCC 6803 |
slr1312 | - |
Synechocystis sp. PCC 6803 |
SpeA | - |
Synechocystis sp. PCC 6803 |
speA1 | - |
Synechocystis sp. PCC 6803 |
speA2 | - |
Synechocystis sp. PCC 6803 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | PLP, the PLP-binding domain is linked to the C-terminal domain by the N-terminus, structure modeling | Synechocystis sp. PCC 6803 |
General Information | Comment | Organism |
---|---|---|
metabolism | arginine decarboxylase (ADC) is the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway, biosynthetic polyamine pathway, overview | Synechocystis sp. PCC 6803 |
additional information | residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates, Asp521A, Asp548B, and Asp550B in ADC1 | Synechocystis sp. PCC 6803 |
additional information | residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs, formed by a highly conserved cysteine residue, needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates. Asp548B and Asp550B are probably important for substrate binding in ADCs | Synechocystis sp. PCC 6803 |
physiological function | the enzyme specific activity or the steady-state accumulation of ADC transcripts are markedly changed by photo-heterotrophic growth mode, salt stress under normal growth light or high-light intensity and stresses due to high temperature or iron deficiency. There is no general relationship between steady-state transcript accumulation and enzyme activity under the conditions studied, since both parameters are not regulated in a similar manner. The enzymatic activity of Synechocystis ADCs is posttranslationally regulated | Synechocystis sp. PCC 6803 |