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Literature summary for 6.3.2.29 extracted from

  • Arai, T.; Kino, K.
    A cyanophycin synthetase from Thermosynechococcus elongatus BP-1 catalyzes primer-independent cyanophycin synthesis (2008), Appl. Microbiol. Biotechnol., 81, 69-78.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information no activation by DTT Thermosynechococcus vestitus

Cloned(Commentary)

Cloned (Comment) Organism
gene cphA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional overexpression of His-tagged Tlr2170 in Escherichia coli BL21(DE3) Thermosynechococcus vestitus

Metals/Ions

Metals/Ions Comment Organism Structure
KCl activates Thermosynechococcus vestitus
Mg2+ Mg2+ or Mn2+ are required Thermosynechococcus vestitus
Mn2+ Mg2+ or Mn2+ are required Thermosynechococcus vestitus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
4 * 100000, SDS-PAGE Thermosynechococcus vestitus
400000
-
the molecular mass of cyanophycin increases with increasing reaction temperature Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [L-Asp(4-L-Arg)]n + L-Asp Thermosynechococcus vestitus
-
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
?
additional information Thermosynechococcus vestitus CphA requires L-Asp, L-Arg, ATP, Mg2+, and low-molecular mass cyanophycin as a primer for cyanophycin synthesis and catalyzes the elongation of a low-molecular mass cyanophycin, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus
-
gene cphA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration Thermosynechococcus vestitus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [L-Asp(4-L-Arg)]n + L-Asp
-
Thermosynechococcus vestitus ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp primer and product analysis using recombinantly expressed Tlr2170 protein, overview Thermosynechococcus vestitus ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
?
additional information CphA requires L-Asp, L-Arg, ATP, Mg2+, and low-molecular mass cyanophycin as a primer for cyanophycin synthesis and catalyzes the elongation of a low-molecular mass cyanophycin, overview Thermosynechococcus vestitus ?
-
?
additional information the enzyme catalyzes the two-step reaction performing reactions of EC 6.3.2.30 and EC 6.3.2.29. Recombinant Tlr2170 protein catalyzes in vitro cyanophycin synthesis in the absence of a primer. The Tlr2170 protein shows strict substrate specificity toward L-Asp and L-Arg Thermosynechococcus vestitus ?
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 100000, SDS-PAGE Thermosynechococcus vestitus

Synonyms

Synonyms Comment Organism
CphA
-
Thermosynechococcus vestitus
cyanophycin synthetase
-
Thermosynechococcus vestitus
More cf. EC 6.3.2.30 Thermosynechococcus vestitus
Tlr2170 protein
-
Thermosynechococcus vestitus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Thermosynechococcus vestitus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 70
-
Thermosynechococcus vestitus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
purified recombinant Tlr2170 protein retains 80% activity after a 60 min incubation at 50°C Thermosynechococcus vestitus
70
-
purified recombinant Tlr2170, inactivation Thermosynechococcus vestitus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Thermosynechococcus vestitus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Thermosynechococcus vestitus