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
inosine-5'-phosphate biosynthesis II
-
Purine metabolism
-
Metabolic pathways
-
Biosynthesis of secondary metabolites
-
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
-
-
-
-
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
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
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]
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
M1R995
accumulates 5-aminoimidazole ribotide
Manually annotated by BRENDA team
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)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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
360000
-
-
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
octamer
-
8 * 50000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
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
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 ACCESSION NO.
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