Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ziegler, K.; Diener, A.; Herpin, C.; Richter, R.; Deutzmann, R.; Lockau, W.
    Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-poly-L-aspartate (cyanophycin) (1998), Eur. J. Biochem., 254, 154-159.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.2.29 K+
-
Trichormus variabilis
6.3.2.29 Mg2+
-
Trichormus variabilis
6.3.2.29 sulfhydryl reagents
-
Trichormus variabilis
6.3.2.30 K+
-
Trichormus variabilis
6.3.2.30 Mg2+
-
Trichormus variabilis
6.3.2.30 sulfhydryl reagents
-
Trichormus variabilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.29 expression in Escherichia coli DH5alpha Trichormus variabilis
6.3.2.30 expression in Escherichia coli DH5alpha Trichormus variabilis

General Stability

EC Number General Stability Organism
6.3.2.29 purified enzyme is unstable at both 0°C and -70°C Trichormus variabilis
6.3.2.30 purified enzyme is unstable at both 0°C and -70°C Trichormus variabilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.29 Mg2+ as Mg-ATP Trichormus variabilis
6.3.2.30 Mg2+ as Mg-ATP Trichormus variabilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.2.29 100000
-
2 * 100000, SDS-PAGE Trichormus variabilis
6.3.2.29 230000
-
gel filtration Trichormus variabilis
6.3.2.30 100000
-
2 * 100000, SDS-PAGE Trichormus variabilis
6.3.2.30 230000
-
gel filtration Trichormus variabilis

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.29 Trichormus variabilis O86109
-
-
6.3.2.30 Trichormus variabilis O86109
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.29 dye-ligand, gel filtration and ion-exchange chromatography, enriched about 4500fold Trichormus variabilis
6.3.2.30 dye-ligand, gel filtration and ion-exchange chromatography, enriched about 4500fold Trichormus variabilis

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.2.29 ATP + [L-Asp(4-L-Arg)]n + L-Asp = ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp i.e. the second reaction of cyanophycin synthesis catalysed by cyanophycin synthase, the first reaction is catalysed by the enzyme's other active centre Trichormus variabilis
6.3.2.30 ATP + [L-Asp(4-L-Arg)]n-L-Asp + L-Arg = ADP + phosphate + [L-Asp(4-L-Arg)]n+1 i.e. the first reaction of cyanophycin synthesis, the second reaction is catalysed by the enzyme's other active centre Trichormus variabilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.2.29 0.00221
-
at 28°C, pH 8.2 Trichormus variabilis
6.3.2.30 0.00221
-
at pH 8.2 and 28°C Trichormus variabilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.29 ATP + [L-Asp(4-L-Arg)]n + L-Asp [L-Asp(4-L-Arg)]n-Asp is a cyanophycin molecule with a C-terminal L-Asp residue that is not linked to an L-Arg residue via its beta-carboxy group, this intermediate is produced in the first reaction catalysed by cyanophycin synthase Trichormus variabilis ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp no formation of AMP ?
6.3.2.30 ATP + [L-Asp(4-L-Arg)]n-L-Asp + L-Arg a small amount of cyanophycin is required as a primer Trichormus variabilis ADP + phosphate + [L-Asp(4-L-Arg)]n+1 no formation of AMP, [L-Asp(4-L-Arg)]n-Asp is the substrate for the second reaction catalysed by cyanophycin synthase, EC 6.3.2.30 ?

Subunits

EC Number Subunits Comment Organism
6.3.2.29 dimer 2 * 100000, SDS-PAGE Trichormus variabilis
6.3.2.30 dimer 2 * 100000, SDS-PAGE Trichormus variabilis

Synonyms

EC Number Synonyms Comment Organism
6.3.2.29 cyanophycin synthetase
-
Trichormus variabilis
6.3.2.30 cyanophycin synthetase
-
Trichormus variabilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.3.2.30 additional information
-
purified enzyme is unstable at both 0°C and -70°C Trichormus variabilis