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Information on EC 6.3.2.29 - cyanophycin synthase (L-aspartate-adding) and Organism(s) Synechococcus sp. MA19 and UniProt Accession Q8VTA5

for references in articles please use BRENDA:EC6.3.2.29
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EC Tree
IUBMB Comments
Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.30, cyanophycin synthase (L-arginine-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store . Both enzymes are found in the same protein but have different active sites [2,4]. Both L-Asp and L-Arg must be present before either enzyme will display significant activity .
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This record set is specific for:
Synechococcus sp. MA19
UNIPROT: Q8VTA5
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The taxonomic range for the selected organisms is: Synechococcus sp. MA19
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
CGP synthetase, CphA, CphA1, CphA2, CphA49, CphANE1, cyanophycin synthetase, More, Tlr2170 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyanophycin synthetase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [L-Asp(4-L-Arg)]n + L-Asp = ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
show the reaction diagram
i.e. the second reaction of cyanophycin synthesis catalysed by cyanophycin synthase, the first reaction is catalysed by the enzyme's other active centre
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
cyanophycin:L-aspartate ligase (ADP-forming)
Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.30, cyanophycin synthase (L-arginine-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store [2]. Both enzymes are found in the same protein but have different active sites [2,4]. Both L-Asp and L-Arg must be present before either enzyme will display significant activity [2].
CAS REGISTRY NUMBER
COMMENTARY hide
131554-17-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + [L-Asp(4-L-Arg)]n + L-Asp
ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
show the reaction diagram
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-
-
?
additional information
?
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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
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.113
30°C, pH 8.2, 123fold purification
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8VTA5_9SYNE
903
0
98516
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
monomer, SDS-PAGE
100600
monomer, calculated from the amino acid sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
preincubation for 30 min in this temperature range resulted in 84% to 72% activity compared to preincubation at 30°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli TOP10 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hai, T.; Oppermann-Sanio, F.B.; Steinbchel, A.
Molecular characterization of a thermostable cyanophycin synthetase from the thermophilic cyanobacterium Synechococcus sp. strain MA19 and in vitro synthesis of cyanophycin and related polyamides
Appl. Environ. Microbiol.
68
93-101
2002
Synechococcus sp. MA19 (Q8VTA5)
Manually annotated by BRENDA team