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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.2.6 - phosphoribosylaminoimidazolesuccinocarboxamide synthase and Organism(s) Gallus gallus

for references in articles please use BRENDA:EC6.3.2.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Forms part of the purine biosynthesis pathway.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Gallus gallus
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Gallus gallus
The enzyme appears in selected viruses and cellular organisms
Synonyms
saicar synthetase, saicar synthase, phosphoribosylaminoimidazole succinocarboxamide synthetase, airc-saicars, phosphoribosylaminoimidazole-succinocarboxamide synthase, phosphoribosylaminoimidazolesuccinocarboxamide synthetase, phosphoribosylaminoimidazole-succinocarboxamide synthetase, sppurc, bapurc, phosphoribosylaminoimidazolesuccinocarboxamide synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-Aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
-
-
-
-
N-(5-Amino-1-ribosyl-4-imidazolylcarbonyl)-L-aspartic acid 5´-phosphate synthetase
-
-
-
-
Phosphoribosylaminoimidazolesuccinocarboxamide synthetase
-
-
-
-
SAICAR synthetase
-
-
-
-
Succino-AICAR synthetase
-
-
-
-
Synthetase, phosphoribosylaminoimidazolesuccinocarboxamide
-
-
-
-
VEG286A
-
-
-
-
Vegetative protein 286A
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxamide formation
-
-
-
-
carboxylic acid amide formation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate:L-aspartate ligase (ADP-forming)
Forms part of the purine biosynthesis pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-67-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
show the reaction diagram
-
one of the enzymes of the series involved in the biosynthesis of the purine nucleotides de novo
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
show the reaction diagram
-
one of the enzymes of the series involved in the biosynthesis of the purine nucleotides de novo
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
can replace Mg2+, maximal activation at 0.04 mM
Mg2+
-
at 0.05 mM ADP, Mg2+ saturation is reached at 2-3 mM
Mn2+
-
can replace Mg2+, maximal activation at 0.06 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PCMB
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PUR6_CHICK
426
0
47240
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
350000
-
gel filtration
52000
-
x * 52000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, concentrated enzyme, above 1 mg/ml, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of EC 4.1.1.21/EC 6.3.2.6
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme 5-aminoimidazole ribonucleotide carboxylase/5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buchanan, J.M.; Lukens, L.N.; Miller, R.W.
N-(5-Amino-1-ribosyl-4-imidazolylcarbonyl)-L-aspartic acid 5-phosphate synthetase
Methods Enzymol.
51
186-193
1978
Gallus gallus
Manually annotated by BRENDA team
Hilton Patey, C.A.; Shaw, G.
Purification and properties of an enzyme duet, phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase, involved in the biosynthesis of purine nucleotides de novo
Biochem. J.
135
543-545
1973
Gallus gallus
Manually annotated by BRENDA team
Chen, Z.D.; Dixon, J.E.; Zalkin, H.
Cloning of a chicken liver cDNA encoding 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase by functional complementation of Escherichia coli pur mutants
Proc. Natl. Acad. Sci. USA
87
3097-3101
1990
Gallus gallus
Manually annotated by BRENDA team