Information on EC 4.1.1.21 - phosphoribosylaminoimidazole carboxylase

New: Word Map on EC 4.1.1.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
4.1.1.21
-
RECOMMENDED NAME
GeneOntology No.
phosphoribosylaminoimidazole carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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 hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-04-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
?
show the reaction diagram
4-carboxy-5-aminoimidazole ribonucleotide + H+
5-aminoimidazole ribonucleotide + CO2
show the reaction diagram
-
-
-
r
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + carbon dioxide
show the reaction diagram
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
5-aminoimidazole ribonucleotide + CO2
4-carboxy-5-aminoimidazole ribonucleotide + H+
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
show the reaction diagram
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-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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 hide
LITERATURE
IMAGE
0.076
1-(5-phosphoribosyl)-5-aminoimidazole
-
-
0.0038 - 0.009
4-carboxy-5-aminoimidazole ribonucleotide
0.06
5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 10C
13
CO2
50 mM Tris-HCl (pH 8.0), at 10C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40
1-(5-phosphoribosyl)-5-aminoimidazole
Gallus gallus
-
-
16 - 65
4-carboxy-5-aminoimidazole ribonucleotide
77
CO2
Treponema denticola
Q73PV9
50 mM Tris-HCl (pH 8.0), at 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33
4-carboxy-5-aminoimidazole ribonucleotide
Treponema denticola
Q73PV9
50 mM Tris-HCl (pH 8.0), at 30C
15198
6.4
5-aminoimidazole ribonucleotide
Treponema denticola
Q73PV9
50 mM Tris-HCl (pH 8.0), at 10C
41712
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.1
3-nitro-1-(beta-D-ribofuranosyl)pyrrole 5'-phosphate
Gallus gallus
-
IC50 above 0.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42.75
-
-
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
determination from amino acid sequence
7.7
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
accumulates 5-aminoimidazole ribotide
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62200
determination from amino acid sequence, 570 amino acid residues in length
184000
gel filtration
360000
-
gel filtration
420000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
8 * 17189, calculated from amino acid sequence; 8 * 17195, ESI-MS
octamer
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
hanging drop vapor diffusion method, using 14-16% (w/v) PEG 1000, 100 mM MgCl2, and 100 mM imidazole (pH 8.0)
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 hide
LITERATURE
6 - 8
-
stable
4137
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
stable for several days
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E177K
mutation identified in PAICS gene of AdeD cell, located in alpha4. Mutation impacts protein structure and completely abolishes its biosynthesis
I237V
mutation identified in PAICS gene of AdeD cell, located in the loop between beta14 and alpha5
W363?
mutation identified in PAICS gene of AdeD cell, located in alpha9. Mutation impacts protein structure and completely abolishes its biosynthesis
T40N
the specific actzivity of the mutant is 20000fold lower than that of wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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
Show AA Sequence (448 entries)
Please use the Sequence Search for a certain query.