Information on EC 4.1.1.21 - phosphoribosylaminoimidazole carboxylase

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

EC NUMBER
COMMENTARY
4.1.1.21
-
RECOMMENDED NAME
GeneOntology No.
phosphoribosylaminoimidazole carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
inosine-5'-phosphate biosynthesis II
-
Metabolic pathways
-
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase [5-amino-1-(5-phospho-D-ribosyl)imidazole-forming]
While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase [3]. 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5-Amino-1-ribosylimidazole 5-phosphate carboxylase
-
-
-
-
5-Phosphoribosyl-5-aminoimidazole carboxylase
-
-
-
-
AIR carboxylase
-
-
-
-
AIR carboxylase
-
-
AIR carboxylase
Q73PV9
-
AIRC
-
-
-
-
aminoimidazole ribonucleotide carboxylase
-
-
Carboxylyase, phosphoribosylaminoimidazole
-
-
-
-
class II PurE
Q73PV9
-
PurE
Q73PV9
-
CAS REGISTRY NUMBER
COMMENTARY
9032-04-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
two enzymes PurK and PurE are required for the reaction
-
-
Manually annotated by BRENDA team
bifunctional enzyme: phosphoribosylaminoimidazole carboxylase/4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide synthetase, with two independent folding domains, each containing a different catalytic site
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
Pigeon
-
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
PurK accelerates the growth of the organism by coupling ATP hydrolysis to HCO3-activation and subsequent N-carboxylation of 1-(5-phosphoribosyl)-5-aminoimidazole
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
show the reaction diagram
-
1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate is formed directly from 1-(5-phosphoribosyl)-5-aminoimidazole + CO2
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
-
sixth step in the purine biosynthetic pathway
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
-
enzyme of the de novo purine biosynthesis
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
Pigeon
-
enzyme of the de novo purine biosynthesis
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
-
enzyme in the biosynthetic pathway to AMP
-
-
-
4-carboxy-5-aminoimidazole ribonucleotide + H+
5-aminoimidazole ribonucleotide + CO2
show the reaction diagram
Q73PV9, -
-
-
-
r
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
Q92210
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
Q01930
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
P21264
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
P15567
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + carbon dioxide
show the reaction diagram
Q9UVE6
-
-
?
5-aminoimidazole ribonucleotide + CO2
4-carboxy-5-aminoimidazole ribonucleotide + H+
show the reaction diagram
Q73PV9, -
-
-
-
r
additional information
?
-
-
AIR carboxylase cannot use N5-carboxyaminoimidazole ribonucleotide, 5-amino-1-(beta-D-ribofuranosyl)pyrazole-4-carboxylate 5'-phosphate, and 5-amino-1-(beta-D-ribofuranosyl)-1,2,3-triazole-4-carboxylate 5'-phosphate as substrates
-
-
-
additional information
?
-
Q73PV9, -
the enzyme does not bind N5-carboxy-4-carboxy-5-aminoimidazole ribonucleotide
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
-
sixth step in the purine biosynthetic pathway
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
-
enzyme of the de novo purine biosynthesis
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
Pigeon
-
enzyme of the de novo purine biosynthesis
-
-
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
-
enzyme in the biosynthetic pathway to AMP
-
-
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
Q92210
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
Q01930
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
P21264
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
P15567
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + carbon dioxide
show the reaction diagram
Q9UVE6
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-nitro-1-(beta-D-ribofuranosyl)pyrrole 5'-phosphate
-
-
4-nitro-1-(-beta-D-ribofuranosyl)pyrazole 5'-phosphate
-
-
4-nitro-1-(beta-D-ribofuranosyl)imidazole 5'-phosphate
-
-
4-Nitro-5-aminoimidazole ribonucleotide
-
steady-state inhibitor
4-Nitro-5-aminoimidazole ribonucleotide
-
tight-binding inhibitor
4-Nitro-5-aminoimidazole ribonucleotide
-
slow, tight binding inhibitor
5-Amino-1(5'-phospho-beta-D-ribofuranosyl)-4-nitroimidazole
-
-
5-amino-1-(beta-D-ribofuranosyl)-1,2,3-triazole-4-carboxylate 5'-phosphate
-
-
5-amino-1-(beta-D-ribofuranosyl)-4-nitropyrazole 5'-phosphate
-
-
5-amino-1-(beta-D-ribofuranosyl)imidazole-4-carboxaldehyde 5'-phosphate
-
-
5-amino-1-(beta-D-ribofuranosyl)pyrazole-4-carboxylate 5'-phosphate
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.076
-
1-(5-phosphoribosyl)-5-aminoimidazole
-
-
0.0038
-
4-carboxy-5-aminoimidazole ribonucleotide
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 10C
-
0.009
-
4-carboxy-5-aminoimidazole ribonucleotide
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 30C
-
0.06
-
5-aminoimidazole ribonucleotide
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 10C
-
13
-
CO2
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 10C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
40
-
1-(5-phosphoribosyl)-5-aminoimidazole
-
-
16
-
4-carboxy-5-aminoimidazole ribonucleotide
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 10C
-
65
-
4-carboxy-5-aminoimidazole ribonucleotide
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 30C
-
77
-
CO2
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
33
-
4-carboxy-5-aminoimidazole ribonucleotide
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 30C
0
6.4
-
5-aminoimidazole ribonucleotide
Q73PV9, -
50 mM Tris-HCl (pH 8.0), at 10C
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.022
-
4-nitro-1-(-beta-D-ribofuranosyl)pyrazole 5'-phosphate
-
in 50 mM Tris-HCl, 0.5 mM EDTA, pH 8.0
0.0013
-
4-nitro-1-(beta-D-ribofuranosyl)imidazole 5'-phosphate
-
in 50 mM Tris-HCl, 0.5 mM EDTA, pH 8.0
3.4e-07
-
4-Nitro-5-aminoimidazole ribonucleotide
-
in 50 mM Tris-HCl, 0.5 mM EDTA, pH 8.0
0.0028
-
5-amino-1-(beta-D-ribofuranosyl)-1,2,3-triazole-4-carboxylate 5'-phosphate
-
in 50 mM Tris-HCl, 0.5 mM EDTA, pH 8.0
0.00039
-
5-amino-1-(beta-D-ribofuranosyl)-4-nitropyrazole 5'-phosphate
-
in 50 mM Tris-HCl, 0.5 mM EDTA, pH 8.0
0.062
-
5-amino-1-(beta-D-ribofuranosyl)imidazole-4-carboxaldehyde 5'-phosphate
-
in 50 mM Tris-HCl, 0.5 mM EDTA, pH 8.0
0.006
-
5-amino-1-(beta-D-ribofuranosyl)pyrazole-4-carboxylate 5'-phosphate
-
in 50 mM Tris-HCl, 0.5 mM EDTA, pH 8.0
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
3-nitro-1-(beta-D-ribofuranosyl)pyrrole 5'-phosphate
-
IC50 above 0.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42.75
-
-
-
additional information
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
-
Q9UVE6
determination from amino acid sequence
7.7
-
Q73PV9, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Pigeon
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Bacillus anthracis (strain A0248)
Bacillus anthracis (strain A0248)
Bacillus anthracis (strain A0248)
Bacillus anthracis (strain A0248)
Bacillus anthracis (strain A0248)
Burkholderia ambifaria (strain MC40-6)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
62200
-
Q9UVE6
determination from amino acid sequence, 570 amino acid residues in length
184000
-
Q73PV9, -
gel filtration
420000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 17176, subunit I, + x * 42150, subunit II, calculation from nucleotide sequence
?
-
x * 17000, purE encoded protein, + x * 39000, purK encoded protein, SDS-PAGE. PurE has an octameric MW of 126000 by gel filtration. PurK has a dimeric MW of 79000 by gel filtration
?
-
1 * 40500 + 1 * 56000, SDS-PAGE, two subunits associate in a 1:1 ratio
homooctamer
Q73PV9, -
8 * 17189, calculated from amino acid sequence; 8 * 17195, ESI-MS
octamer
-
crystallization data
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein expressed in Escherichia coli
-
hanging drop vapor diffusion method, using 14-16% (w/v) PEG 1000, 100 mM MgCl2, and 100 mM imidazole (pH 8.0)
Q73PV9, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
stable for several days
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
prolonged dialysis of more than 12 h, results in 50% loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bifunctional protein complex possessing phosphoribosylaminoimidazole carboxylase, EC 4.1.1.21, and phosphoribosylaminoimidazolesuccinocarboxamide synthetase, EC 6.3.2.6, activities
-
copurification of the enzymes of the de novo purine biosynthetic pathway
Pigeon
-
streptomycin precipitation, ammonium sulfate precipitation, phenyl Sepharose 6 column chromatography, hydroxyapatite column chromatography, and Superdex 200 gel filtration
Q73PV9, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
Q73PV9, -
expression in Escherichia coli
Q9UVE6
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
T40N
Q73PV9, -
the specific actzivity of the mutant is 20000fold lower than that of wild type enzyme