Literature summary for 6.3.2.30 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.

Search for more literature for 6.3.2.30

Activating Compound

Activating Compound	Comment	Organism	Structure
K+	-	Trichormus variabilis
Mg2+	-	Trichormus variabilis
sulfhydryl reagents	-	Trichormus variabilis

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli DH5alpha	Trichormus variabilis

General Stability

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	as Mg-ATP	Trichormus variabilis

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Trichormus variabilis	O86109	-	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Subunits	Comment	Organism
dimer	2 * 100000, SDS-PAGE	Trichormus variabilis

Synonyms

Synonyms	Comment	Organism
cyanophycin synthetase	-	Trichormus variabilis

Temperature Stability [°C]

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)