6.3.2.29: cyanophycin synthase (L-aspartate-adding)
This is an abbreviated version!
For detailed information about cyanophycin synthase (L-aspartate-adding), go to the full flat file.
Reaction
Synonyms
CGP synthetase, CphA, CphA1, CphA2, CphA49, CphANE1, cyanophycin synthetase, More, Tlr2170 protein
ECTree
6.3.2.29 cyanophycin synthase (L-aspartate-adding)Advanced search results
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results (Substrates Products
Substrates Products on EC 6.3.2.29 - cyanophycin synthase (L-aspartate-adding)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + cyanophycin granule polypeptide-L-Asp + L-arginine
?
-
-
-
-
?
ATP + [L-Asp(4-L-Arg)]3-L-Asp + L-Arg
ADP + phosphate + [L-Asp(4-L-Arg)]4 + L-Asp
-
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
[L-Asp(4-L-Arg)]n-L-Asp + ADP + phosphate
-
-
-
?
L-aspartic acid + ATP
poly-L-aspartic acid + ADP + phosphate
-
-
-
-
?
[L-Asp(4-L-Arg)]n + L-Asp + ATP
[L-Asp(4-L-Arg)]n-Asp + ADP + phosphate
-
a small amount of cyanophycin is required as a primer
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
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
study of expression profiles of the genes cphA1 and cphA2 and their dependence on the type of nitrogen supply in the medium
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
normal assay conditions
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [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
no formation of AMP
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
role of the C-terminal region of CphANE1, Glu856 is critical for CphANE1 catalytic activity, overview
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
study determined the effect of different light and nutrition conditions on cyanophycin granule formation
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
Thermosynechococcus vestitus
-
-
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
Thermosynechococcus vestitus
-
primer and product analysis using recombinantly expressed Tlr2170 protein, overview
-
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [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
no formation of AMP
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [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
no formation of AMP
-
?
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
-
-
-
?
additional information
?
-
-
without L-arginine 1.1% activity compared to the reaction mixture containing both substrates, no activity using L-lysine instead of L-arginine, no activity without addition of small amounts of cyanophycin as a primer for synthesis
-
-
?
additional information
?
-
cyanophycin accumulation is studied, comparison of nitrogen-fixing and non-nitrogen-fixing cyanobacteria
-
-
?
additional information
?
-
-
no activity without L-arginine, with L-lysine instead of L-arginine there is 15% activity compared to the normal conditions
-
-
?
additional information
?
-
-
the enzyme catalyzes the two-step reaction performing reactions of EC 6.3.2.30 and EC 6.3.2.29
-
-
?
additional information
?
-
-
the enzyme catalyzes the two-step reaction performing reactions of EC 6.3.2.30 and EC 6.3.2.29
-
-
?
additional information
?
-
negligible activities when L-arginine is omitted, no activity when L-arginine is replaced by L-glutamic acid, citrulline, ornithine, arginine amide, agmatine, or norvaline
-
-
?
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
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
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
-
-
?
additional information
?
-
-
no product is formed if the peptide primer is blocked at the C-terminus or if L-arginine is solely supplied as substrate
-
-
?
additional information
?
-
cyanophycin synthetase catalyzes the synthesis of cyanophycin by ATP-dependent polymerization of L-Asp and L-Arg. In vitro, the activity of CphA generally depends on the presence of L-Asp, L-Arg, ATP, Mg2+, K+, sulfhydryl compound, and cyanophycin as primers
-
-
?
additional information
?
-
the recombinant CphA49 exhibits strict primer dependency and broad substrate specificities. L-Lys and L-Glu can substitute for L-Asp, but with very low catalytic activity. No activity with L-Arg and L-citrulline, L-Arg and L-ornithine, L-Asp and L-citrulline, and L-Asp and L-ornithine
-
-
?
