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Literature summary for 6.3.2.30 extracted from

  • Klemke, F.; Nuernberg, D.J.; Ziegler, K.; Beyer, G.; Kahmann, U.; Lockau, W.; Volkmer, T.
    CphA2 is a novel type of cyanophycin synthetase in N2-fixing cyanobacteria (2016), Microbiology, 162, 526-536 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cyanothece sp. PCC 7425

Metals/Ions

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 [Da] Molecular Weight Maximum [Da] Comment Organism
265000
-
gel filtration, untagged protein Trichormus variabilis

Organism

Organism UniProt Comment Textmining
Cyanothece sp. PCC 7425
-
-
-
Trichormus variabilis Q3MGC5
-
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
trimer or tetramer, 3 or 4 x * 75000, SDS-PAGE, recombinant protein including His-tag Trichormus variabilis

Synonyms

Synonyms Comment Organism
Ava_0335
-
Trichormus variabilis
CphA2
-
Trichormus variabilis
CphA2
-
Cyanothece sp. PCC 7425

General Information

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