Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Cyanothece sp. PCC 7425 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | presence of potassium ions is essential for enzymic activity | Trichormus variabilis | |
K+ | presence of potassium ions is essential for enzymic activity | Cyanothece sp. PCC 7425 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
265000 | - |
gel filtration, untagged protein | Trichormus variabilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cyanothece sp. PCC 7425 | - |
- |
- |
Trichormus variabilis | Q3MGC5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [L-Asp(4-L-Arg)]n + alpha-L-Asp-L-Arg | - |
Trichormus variabilis | ADP + phosphate + [L-Asp(4-L-Arg)]n+1 | - |
? | |
ATP + [L-Asp(4-L-Arg)]n + beta-L-Asp-L-Arg | - |
Trichormus variabilis | ADP + phosphate + [L-Asp(4-L-Arg)]n+1 | - |
? | |
ATP + [L-Asp(4-L-Arg)]n + beta-L-Asp-L-Arg | - |
Cyanothece sp. PCC 7425 | ADP + phosphate + [L-Asp(4-L-Arg)]n+1 | - |
? | |
additional information | enzyme is specific for the dipeptide beta-aspartyl-arginine and ATP as substrates. To incorporate 1 mol beta-aspartyl-arginine into cyanophycin, the hydrolysis of about 1 mol ATP is required. No substrates: beta-aspartyl-lysine, alpha-aspartyl-glycine, beta-aspartyl-glycine, alpha-aspartyl-leucine, beta-aspartyl-leucine, beta-aspartyl-alanine, beta-aspartyl-phenylalanine, alpha-glutamyl-leucine, alpha-alanyl-glycine, L-aspartate, L-arginine | Trichormus variabilis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | or tetramer, 3 or 4 x * 75000, SDS-PAGE, recombinant protein including His-tag | Trichormus variabilis |
Synonyms | Comment | Organism |
---|---|---|
Ava_0335 | - |
Trichormus variabilis |
CphA2 | - |
Trichormus variabilis |
CphA2 | - |
Cyanothece sp. PCC 7425 |
General Information | Comment | Organism |
---|---|---|
physiological function | a CphA2 disruption mutant shows impaired growth under high-light conditions and nitrogen deprivation, suggesting that CphA2 plays an important role in nitrogen metabolism under N2-fixing conditions. The mutant has fewer cyanophycin granules, but no alteration in the distribution of granules in its cells is observed | Trichormus variabilis |