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Information on EC 6.3.2.6 - phosphoribosylaminoimidazolesuccinocarboxamide synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P27616

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IUBMB Comments
Forms part of the purine biosynthesis pathway.
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Saccharomyces cerevisiae
UNIPROT: P27616
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
saicar synthetase, saicar synthase, phosphoribosylaminoimidazole succinocarboxamide synthetase, airc-saicars, phosphoribosylaminoimidazole-succinocarboxamide synthase, phosphoribosylaminoimidazolesuccinocarboxamide synthetase, sppurc, bapurc, phosphoribosylaminoimidazolesuccinocarboxamide synthase, phosphoribosylaminoimidazole-succinocarboxamide synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-Aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
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N-(5-Amino-1-ribosyl-4-imidazolylcarbonyl)-L-aspartic acid 5´-phosphate synthetase
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Phosphoribosylaminoimidazolesuccinocarboxamide synthetase
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SAICAR synthase
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SAICAR synthetase
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Succino-AICAR synthetase
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Synthetase, phosphoribosylaminoimidazolesuccinocarboxamide
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VEG286A
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Vegetative protein 286A
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additional information
the enzyme is a member of the ATP-grasp superfamily
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
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carboxamide formation
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PATHWAY SOURCE
PATHWAYS
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-, -, -
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
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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 + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
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?
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
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?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
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?
additional information
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in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview
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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 + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
seventh of ten steps in the purine biosynthesis, pathway overview
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ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
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-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35500
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x * 35500, calculation from crystallographic data and X-ray diffraction
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
structure overview
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x * 35500, calculation from crystallographic data and X-ray diffraction
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion, drops contain protein at a concentration of 8-15 mg/ml in 50 mM Tris-HCl, pH 7.0, 40 mM aspartic acid and 1.0-1.25 M ammonium sulfate, crystals diffract to 1.9 A resolution
hanging-drop vapor-diffusion method. Crystals of the complex of the enzyme SAICAR synthase with the reaction product belong to space group P2(1)2(1)2(1) containing one molecule per asymmetric unit
at 2.5 A resolution
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crystals of SAICAR complexed with 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide and succinic acid are grown by hanging drop vapor diffusion at room temperature, mother liquor consists of 24 mg/ml SAICAR, 1 M ammonium sulfate, 100 mM 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide, 100 mM succinic acid and 50 mM Tris-HCl, pH 7.5, crystals diffract to 1.3 A
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sephadex, Butyl-Toyopearl
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grebenko, A.I.; Levdikov, V.M.; Barynin, V.V.; Melik-Adamyan, W.R.
Crystallization and preliminary X-ray investigation of phosphoribosylaminoimidazolesuccinocarboxamide synthase from the yeast Saccharomyces cerevisiae
J. Mol. Biol.
228
298-299
1992
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Urusova, D.V.; Antonyuk, S.V.; Grebenko, A.I.; Lamzin, V.S.; Melik-Adamyan, V.R.
X-ray diffraction study of the complex of the enzyme SAICAR synthase with substrate analogs
Crystallogr. Rep.
48
763-767
2003
Saccharomyces cerevisiae
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Manually annotated by BRENDA team
Levdikov, V.M.; Barynin, V.V.; Grebenko, A.I.; Melik-Adamyan, W.R.; Lamzin, V.S.; Wilson, K.S.
The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis
Structure
6
363-376
1998
Saccharomyces cerevisiae (P27616), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Urusova, D.V.; Levdikov, V.M.; Antonyuk, S.V.; Grebenko, A.I.; Lamzin, V.S.; Melik-Adamyan, V.R.
X-ray diffraction study of the complex of the enzyme SAICAR synthase with the reaction product
Crystallogr. Rep.
51
824-827
2006
Saccharomyces cerevisiae (P27616)
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Manually annotated by BRENDA team
Zhang, Y.; Morar, M.; Ealick, S.E.
Structural biology of the purine biosynthetic pathway
Cell. Mol. Life Sci.
65
3699-3724
2008
Escherichia coli, Homo sapiens, Thermotoga maritima, Saccharomyces cerevisiae (P27616)
Manually annotated by BRENDA team