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Information on EC 6.3.2.6 - phosphoribosylaminoimidazolesuccinocarboxamide synthase and Organism(s) Escherichia coli and UniProt Accession P0A7D7

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IUBMB Comments
Forms part of the purine biosynthesis pathway.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A7D7
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
saicar synthetase, saicar synthase, phosphoribosylaminoimidazole succinocarboxamide synthetase, airc-saicars, phosphoribosylaminoimidazole-succinocarboxamide synthase, phosphoribosylaminoimidazolesuccinocarboxamide synthetase, phosphoribosylaminoimidazolesuccinocarboxamide synthase, phosphoribosylaminoimidazole-succinocarboxamide synthetase, sppurc, bapurc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoribosylaminoimidazole succinocarboxamide synthetase
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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
SAICAR synthase
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SAICAR synthetase
Succino-AICAR synthetase
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Synthetase, phosphoribosylaminoimidazolesuccinocarboxamide
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VEG286A
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-
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Vegetative protein 286A
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-
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additional information
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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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-
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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
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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
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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-
-
?
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
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 5'-(beta,gamma-imido)triphosphate
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-
IMP
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competitive with respect to 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
Maleate
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competitive with respect to L-Asp
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole
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0.036
Asp
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0.04
MgATP2-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26 - 4
adenosine 5'-(beta,gamma-imido)triphosphate
7 - 13
IMP
12 - 50
Maleate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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structure-activity molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26998
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x * 26998, calculation from nucleotide sequence
27000
76000
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ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
trimer
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3 * 27000, SDS-PAGE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
27-100°C, structure-thermostability molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in a high-copy-number plasmid
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expression in Escherichia coli
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SAICAR synthetase is cloned into a lambdaPL expression vector to give plasmid pJS408, overexpression
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Parker, J.
Identification of the purC gene product of Escherichia coli
J. Bacteriol.
157
712-717
1984
Escherichia coli
Manually annotated by BRENDA team
Tiedeman, A.A.; DeMarini, D.J.; Parker, J.; Smith, J.M.
DNA sequence of the purC gene encoding 5-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide synthetase and organization of the dapA-purC region of Escherichia coli K-12
J. Bacteriol.
172
6035-6041
1990
Escherichia coli
Manually annotated by BRENDA team
Meyer, E.; Leonard, N.J.; Bhat, B.; Stubbe, J.; Smith, J.M.
Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway
Biochemistry
31
5022-5032
1992
Escherichia coli
Manually annotated by BRENDA team
Meyer, E.; Kappock, T.J.; Osuji, C.; Stubbe, J.
Evidence for the Direct Transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase
Biochemistry
38
3012-3018
1999
Escherichia coli
Manually annotated by BRENDA team
Nelson, S.W.; Binkowski, D.J.; Honzatko, R.B.; Fromm, H.J.
Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase
Biochemistry
44
766-774
2005
Escherichia coli
Manually annotated by BRENDA team
Ginder, N.D.; Binkowski, D.J.; Fromm, H.J.; Honzatko, R.B.
Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase
J. Biol. Chem.
281
20680-20688
2006
Escherichia coli (P0A7D7), Escherichia coli
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
Manjunath, K.; Sekar, K.
Molecular dynamics perspective on the protein thermal stability: a case study using SAICAR synthetase
J. Chem. Inf. Model.
53
2448-2461
2013
Escherichia coli, Ehrlichia chaffeensis, Geobacillus kaustophilus, Pyrococcus horikoshii (O57978), Methanocaldococcus jannaschii (Q58987), Pyrococcus horikoshii DSM 12428 (O57978), Methanocaldococcus jannaschii DSM 2661 (Q58987)
Manually annotated by BRENDA team