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
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
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
inosine-5'-phosphate biosynthesis II
-
-
Metabolic pathways
-
-
Purine metabolism
-
-
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
COMMENTARY
LITERATURE
5-Amino-1-ribosylimidazole 5-phosphate carboxylase
-
-
-
-
5-Phosphoribosyl-5-aminoimidazole carboxylase
-
-
-
-
AdeD
M1R995
-
AIR carboxylase
-
-
-
-
AIR carboxylase
-
-
AIR carboxylase
Q73PV9
-
AIRC
-
-
-
-
aminoimidazole ribonucleotide carboxylase
-
-
Carboxylyase, phosphoribosylaminoimidazole
-
-
-
-
class II PurE
Q73PV9
-
PAICS
M1R995
-
phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
M1R995
-
PurE
Q73PV9
-
CAS REGISTRY NUMBER
COMMENTARY
9032-04-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
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
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
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]
SUBSTRATE
ORGANISM
UNIPROT
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]
SUBSTRATE
ORGANISM
UNIPROT
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33
4-carboxy-5-aminoimidazole ribonucleotide
Q73PV9
50 mM Tris-HCl (pH 8.0), at 30C
15198
6.4
5-aminoimidazole ribonucleotide
Q73PV9
50 mM Tris-HCl (pH 8.0), at 10C
41712
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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
0.00000034
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]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
3-nitro-1-(beta-D-ribofuranosyl)pyrrole 5'-phosphate
-
IC50 above 0.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42.75
-
-
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
Q9UVE6
determination from amino acid sequence
7.7
Q73PV9
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
M1R995
accumulates 5-aminoimidazole ribotide
Manually annotated by BRENDA team
Pigeon
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
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)
Burkholderia ambifaria (strain MC40-6)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62200
Q9UVE6
determination from amino acid sequence, 570 amino acid residues in length
654019
184000
Q73PV9
gel filtration
714253
360000
-
gel filtration
728777
420000
-
gel filtration
4137
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
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
?
-
x * 17176, subunit I, + x * 42150, subunit II, calculation from nucleotide sequence
?
-
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
homooctamer
-
8 * 17195, ESI-MS
octamer
-
crystallization data
octamer
-
8 * 50000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein expressed in Escherichia coli
-
protein sequence is used in model building on Trchoderma ni enzyme crystals providing an excellent fit to the electron density. Comparison to the structure of human enzyme
Q1HQ66
hanging drop vapor diffusion method, using 14-16% (w/v) PEG 1000, 100 mM MgCl2, and 100 mM imidazole (pH 8.0)
Q73PV9
to 2.8 A resolution, space-group P22121 with one homo-tetramer in the asymmetric unit. Comparison to the structure of human enzyme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
stable
4137
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
stable for several days
4137
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
prolonged dialysis of more than 12 h, results in 50% loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
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
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
Q73PV9
expression in Escherichia coli
Q9UVE6
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E177K
M1R995
mutation identified in PAICS gene of AdeD cell, located in alpha4. Mutation impacts protein structure and completely abolishes its biosynthesis
I237V
M1R995
mutation identified in PAICS gene of AdeD cell, located in the loop between beta14 and alpha5
W363?
M1R995
mutation identified in PAICS gene of AdeD cell, located in alpha9. Mutation impacts protein structure and completely abolishes its biosynthesis
T40N
Q73PV9
the specific actzivity of the mutant is 20000fold lower than that of wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
M1R995
sensitive and rapid analytical method for detection of purine de novo biosynthesis intermediates based on high performance liquid chromatography with electrochemical detection. Method is applied to accumulation of 5-aminoimidazole ribotide in AdeD cells