Information on EC 6.3.2.6 - phosphoribosylaminoimidazolesuccinocarboxamide synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
6.3.2.6
-
RECOMMENDED NAME
GeneOntology No.
phosphoribosylaminoimidazolesuccinocarboxamide synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxamide formation
-
-
-
-
carboxylic acid amide formation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
inosine-5'-phosphate biosynthesis I
-
-
inosine-5'-phosphate biosynthesis II
-
-
inosine-5'-phosphate biosynthesis III
-
-
Metabolic pathways
-
-
Purine metabolism
-
-
purine metabolism
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
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
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-67-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme with phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase activities
-
-
Manually annotated by BRENDA team
gene purC
-
-
Manually annotated by BRENDA team
gene purCE
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii DSM 12428
-
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
-
SwissProt
Manually annotated by BRENDA team
gene purC
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
Zygotic paics mutants have pigmentation defects in which xanthophore and iridophore pigmentation is almost completely absent, and melanin-derived pigmentation is significantly decreased, even though pigment cells are present in normal amounts and distributions. Zygotic paics mutants are also microphthalmic, resulting from defects in cell cycle exit of proliferative retinoblasts within the developing eye. Maternal-zygotic and maternal-effect mutants demonstrate a crucial requirement for maternally derived paics, these mutants show more severe developmental defects than their zygotic counterparts
physiological function
-
the enzyme is involved in the de novo purine biosynthesis pathway
physiological function
Pyrococcus horikoshii OT-3
-
the enzyme is involved in the de novo purine biosynthesis pathway
-
additional information
-
bifunctional enzyme complex, termed PAICS, harboring 5-aminoimidazole ribonucleotide carboxylase and 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase activities, the SAICAR active sites is located in the N-terminal domain of PAICS, structure modeling, overview. In addition to the basic loop responsible for phosphate-binding, the adenine-ribose moiety of the nucleotide sits in a largely hydrophobic pocket sandwiched between beta1-strands of the SAICAR domain
additional information
-
structure-activity molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
-
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
-
-
-
-
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
-
-
-
-
-
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
-
-
-
-
-
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
-
-
-
-
-
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
Pigeon
-
-
-
-
-
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
-
r, in the reverse reaction phosphate can be replaced by arsenate, in the reverse reaction ADP cannot be replaced by any of the other nucleoside diphosphates
-
-
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
-
rapid equilibrium random ter-ter mechanism
-
-
?
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
?
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
?
show the reaction diagram
-
catalyzes the aspartate addition at the alpha-amino group to the growing purine backbone
-
-
-
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
P0A7D7
-
-
-
?
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-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-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-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
Q58987
-
-
-
?
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
-
-
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
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
P27616
-
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
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
-
-
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
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
Q9I7S8
bifunctional enzyme having also 5-aminoimidazole ribonucleotide carboxylase, i.e. AIRc, activity
-
?
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
-
phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) is an important bifunctional enzyme in de novo purine biosynthesis in vertebrate with both 5-aminoimidazole ribonucleotide carboxylase (AIRc) and 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase (SAICARs) activities
-
-
?
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
-
PurCE performs the sixth and seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
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, ligation of the carboxylate group of CAIR to the amino group of aspartate, pathway overview
-
-
?
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
P27616
seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
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
-
-
?
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
-
ligation of the carboxylate group of CAIR to the amino group of aspartate
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
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
Pyrococcus horikoshii DSM 12428
O57978
-
-
-
?
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
Q9I7S8
-
-
?
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
-
-
-
?
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
-
-
-
?
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
P27616
-
-
?
additional information
?
-
-
in higher organisms PurC and PurE are fused to form a bifunctional enzyme, overview, active site structure, overview
-
-
-
additional information
?
-
-
in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview
-
-
-
additional information
?
-
P27616
in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview
-
-
-
additional information
?
-
-
in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
?
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
?
show the reaction diagram
-
catalyzes the aspartate addition at the alpha-amino group to the growing purine backbone
-
-
-
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-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-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-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
Q58987
-
-
-
?
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
-
phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) is an important bifunctional enzyme in de novo purine biosynthesis in vertebrate with both 5-aminoimidazole ribonucleotide carboxylase (AIRc) and 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase (SAICARs) activities
-
-
?
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
-
PurCE performs the sixth and seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
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, ligation of the carboxylate group of CAIR to the amino group of aspartate, pathway overview
-
-
?
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
P27616
seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
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
-
-
?
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
Q9I7S8
-
-
?
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
-
-
-
?
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
-
-
-
?
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
P27616
-
-
?
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
Pyrococcus horikoshii DSM 12428
O57978
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
Mg2+
-
required
Mn2+
-
can replace Mg2+, maximal activation at 0.06 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-(beta,gamma-imido)triphosphate
-
-
IMP
-
competitive with respect to 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
Maleate
-
competitive with respect to L-Asp
PCMB
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
-
-
0.036
Asp
-
-
0.04
MgATP2-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
adenosine 5'-(beta,gamma-imido)triphosphate
-
37C, Kis, competitive versus ATP
0.6
adenosine 5'-(beta,gamma-imido)triphosphate
-
37C, Kii, noncompetitive versus L-Asp; 37C, Kis, noncompetitive versus 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
0.7
adenosine 5'-(beta,gamma-imido)triphosphate
-
37C, Kis, noncompetitive versus L-Asp
4
adenosine 5'-(beta,gamma-imido)triphosphate
-
37C, Kii, noncompetitive versus 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
7
IMP
-
37C, Kis, noncompetitive versus ATP; 37C, Kis, noncompetitive versus L-Asp
9
IMP
-
37C, Kii, noncompetitive versus ATP
9.1
IMP
-
37C, Kis, competitive versus 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
13
IMP
-
37C, Kii, noncompetitive versus L-Asp
12
Maleate
-
37C, Kis, noncompetitive versus ATP
15
Maleate
-
37C, Kis, competitive versus 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
16
Maleate
-
37C, Kis, competitive versus L-Asp
40
Maleate
-
37C, Kii, competitive versus 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
50
Maleate
-
37C, Kii, noncompetitive versus ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11.06
-
-
additional information
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Pigeon
-
-
Manually annotated by BRENDA team
additional information
-
enzyme is expressed in rapidly dividing tissues
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A)
Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Geobacillus kaustophilus (strain HTA426)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
76000
-
ultracentrifugation
1268
96000
-
gradient gel electrophoresis of the native protein
1266
350000
-
gel filtration
1263
360000
-
gel filtration
728777
420000
-
gel filtration
1266
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 27000, SDS-PAGE
?
-
x * 27431, calculation from nucleotide sequence
?
-
x * 26998, calculation from nucleotide sequence
?
-
x * 35500, calculation from crystallographic data and X-ray diffraction
?
-
x * 52000, SDS-PAGE
?
-
x * 26600, calculated
dimer
-
structure overview
dimer
-
structure overview, PDB ID 2GQS
dimer
Pyrococcus horikoshii DSM 12428
-
-
-
octamer
-
the 2.8 A resolution structure reveals that eight PAICS subunits, each composed of distinct AIRc and SAICARs domains, assemble a compact homo-octamer with an octameric-carboxylase core and four symmetric periphery dimers formed by synthetase domains
octamer
-
4 dimers of PurC around a core of octameric PurE, the PurC dimers do not contact each other, structure overview, PDB ID 2H31
oligomer
-
x * 50000, SDS-PAGE
trimer
-
3 * 27000, SDS-PAGE
monomer
P27616
structure overview
additional information
-
structure modeling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion, crystal structures of the ADP and the ADP/4-carboxy-5-aminoimidazole ribonucleotide complexes of SAICAR synthetase. ADP and 4-carboxy-5-aminoimidazole ribonucleotide bind to the active site in association with three Mg2+, two of which coordinate the same oxygen atom of the 4-carboxyl group of CAIR, whereas, the third coordinates the alpha- and beta-phosphoryl groups of ADP. The polypeptide fold for residues 204-221 of the Escherichia coli structure differs significantly from those of the ligand-free SAICAR synthetase from Thermatoga maritima and the adenine nucleotide complexes of the synthetase from Saccharomyces cerevisiae
P0A7D7
the 2.8 A resolution structure reveals that eight PAICS subunits, each composed of distinct AIRc and SAICARs domains, assemble a compact homo-octamer with an octameric-carboxylase core and four symmetric periphery dimers formed by synthetase domains
-
space group P31, presence of a hexamer in the asymmetric unit
O57978
at 2.5 A resolution
-
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
-
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
-
to 2.8 A resolution, space group P2
-
hanging-drop vapor-diffusion conditions, 2.2 A resolution crystal structure. Protein structure is described and compared with that of the ATP-SAICAR synthase complex from yeast
-
purified enzyme in 150 mM NaCl, 1 mM DTT, 10 mM HEPES-KOH, pH 7.5, is mixed with 50 mM Tris pH 8.0, 2M ammonium sulfate and 1% PEG400, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 8
-
narrow stability profile with maximal stability at pH 7.6
1266
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
27-100C, structure-thermostability molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
728030
additional information
Q58987
delineation of the mesophilic (Escherichia coli, Ehrlichia chaffeensis), thermophilic (Geobacillus kaustophilus), and hyperthermophilic (Methanocaldococcus jannaschii, Pyrococcus horikoshii) proteins on the basis of their thermal stability by studying their dynamic aspects at 27C and 60C using molecular dynamics
728030
additional information
-
delineation of the mesophilic (Escherichia coli, Ehrlichia chaffeensis), thermophilic (Geobacillus kaustophilus), and hyperthermophilic (Methanocaldococcus jannaschii, Pyrococcus horikoshii) proteins on the basis of their thermal stability by studying their dynamic aspects at 27C and 60C using molecular dynamics
728030
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT is essential in maintaining the stability, in absence of DTT the activity is completely lost within two hours of extraction
-
the ionic strength required to maintain enzyme activity is 0.1 M Tris HCl, at pH 7.8
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, concentrated enzyme, above 1 mg/ml, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurification of EC 4.1.1.21/EC 6.3.2.6
-
copurification of the bifunctional protein complex possessing phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (EC 6.3.2.6)
-
partial
Pigeon
-
ammonium sulfate, DEAE-Sephadex, Butyl-Toyopearl
-
recombinant protein
-
recombinant His-tagged enzyme from insect HighFive cells by nickel affinity and anion exchange chromatography, followed by gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of a 12-gene cluster encoding 9 enzymes for de novo purine nucleotide synthesis
-
functional complementation of Escherichia coli purC purine auxotroph
Q9I7S8
cloned in a high-copy-number plasmid
-
expression in Escherichia coli
-
SAICAR synthetase is cloned into a lambdaPL expression vector to give plasmid pJS408, overexpression
-
bifunctional enzyme 5-aminoimidazole ribonucleotide carboxylase/5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
-
expression in Escherichia coli
O57978
expression in Escherichia coli
-
recombinant expression of His-tagged enzyme in insect HighFive cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) is an important bifunctional enzyme in de novo purine biosynthesis in vertebrate with both 5-aminoimidazole ribonucleotide carboxylase (AIRc) and 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase (SAICARs) activities. It is an attractive target for rational anticancer drug design, since rapidly dividing cancer cells rely heavily on the purine de novo pathway for synthesis of adenine and guanine, whereas normal cells favor the salvage pathway