We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments 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 . 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
paics, phosphoribosylaminoimidazole carboxylase, air carboxylase, class ii pure, aminoimidazole ribonucleotide carboxylase, phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-Amino-1-ribosylimidazole 5-phosphate carboxylase
-
-
-
-
5-Phosphoribosyl-5-aminoimidazole carboxylase
-
-
-
-
aminoimidazole ribonucleotide carboxylase
-
-
Carboxylyase, phosphoribosylaminoimidazole
-
-
-
-
phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
-
AIR carboxylase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
4-carboxy-5-aminoimidazole ribonucleotide + H+
5-aminoimidazole ribonucleotide + CO2
-
-
-
r
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + carbon dioxide
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
5-aminoimidazole ribonucleotide + CO2
4-carboxy-5-aminoimidazole ribonucleotide + H+
-
-
-
r
additional information
?
-
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
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
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate is formed directly from 1-(5-phosphoribosyl)-5-aminoimidazole + CO2
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
1-(5-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
Pigeon
-
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
-
enzyme of the de novo purine biosynthesis
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
-
sixth step in the purine biosynthetic pathway
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
-
enzyme in the biosynthetic pathway to AMP
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
Pigeon
-
enzyme of the de novo purine biosynthesis
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
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
?
-
the enzyme does not bind N5-carboxy-4-carboxy-5-aminoimidazole ribonucleotide
-
-
?
additional information
?
-
-
the enzyme does not bind N5-carboxy-4-carboxy-5-aminoimidazole ribonucleotide
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + carbon dioxide
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
-
enzyme of the de novo purine biosynthesis
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
-
sixth step in the purine biosynthetic pathway
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
-
enzyme in the biosynthetic pathway to AMP
-
-
?
1-(5-Phosphoribosyl)-5-aminoimidazole + CO2
?
Pigeon
-
enzyme of the de novo purine biosynthesis
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abortion, Spontaneous
PAICS deficiency, a new defect of de novo purine synthesis resulting in multiple congenital anomalies and fatal outcome.
Adenocarcinoma of Lung
Role and regulation of coordinately expressed de novo purine biosynthetic enzymes PPAT and PAICS in lung cancer.
Adenocarcinoma of Lung
Roles of highly expressed PAICS in lung adenocarcinoma.
Breast Neoplasms
Knockdown of PAICS inhibits malignant proliferation of human breast cancer cell lines.
Breast Neoplasms
Roles of highly expressed PAICS in lung adenocarcinoma.
Breast Neoplasms
Systematic functional perturbations uncover a prognostic genetic network driving human breast cancer.
Carcinogenesis
Knockdown of PAICS inhibits malignant proliferation of human breast cancer cell lines.
Carcinogenesis
PAICS contributes to gastric carcinogenesis and participates in DNA damage response by interacting with histone deacetylase 1/2.
Carcinoma, Non-Small-Cell Lung
Regulating COX10-AS1 / miR-142-5p / PAICS axis inhibits the proliferation of non-small cell lung cancer.
Colorectal Neoplasms
Downregulation of PAICS due to loss of chromosome 4q is associated with poor survival in stage III colorectal cancer.
Colorectal Neoplasms
PAICS, a Purine Nucleotide Metabolic Enzyme, is Involved in Tumor Growth and the Metastasis of Colorectal Cancer.
Glioma
PAICS is related to glioma grade and can promote glioma growth and migration.
Lung Neoplasms
Regulating COX10-AS1 / miR-142-5p / PAICS axis inhibits the proliferation of non-small cell lung cancer.
Lung Neoplasms
Role and regulation of coordinately expressed de novo purine biosynthetic enzymes PPAT and PAICS in lung cancer.
Lung Neoplasms
Roles of highly expressed PAICS in lung adenocarcinoma.
Melanoma
Comprehensive genomic characterization of cutaneous malignant melanoma cell lines derived from metastatic lesions by whole-exome sequencing and SNP array profiling.
Microphthalmos
Zebrafish mutations in gart and paics identify crucial roles for de novo purine synthesis in vertebrate pigmentation and ocular development.
Neoplasm Metastasis
Downregulation of PAICS due to loss of chromosome 4q is associated with poor survival in stage III colorectal cancer.
Neoplasm Metastasis
PAICS, a Purine Nucleotide Metabolic Enzyme, is Involved in Tumor Growth and the Metastasis of Colorectal Cancer.
Neoplasms
A functional yeast survival screen of tumor-derived cDNA libraries designed to identify anti-apoptotic mammalian oncogenes.
Neoplasms
A Role for De Novo Purine Metabolic Enzyme PAICS in Bladder Cancer Progression.
Neoplasms
Combinatorial targeting of MTHFD2 and PAICS in purine synthesis as a novel therapeutic strategy.
Neoplasms
Crystal structures of human PAICS reveal substrate and product binding of an emerging cancer target.
Neoplasms
Downregulation of PAICS due to loss of chromosome 4q is associated with poor survival in stage III colorectal cancer.
Neoplasms
Genetic and metabolomic analysis of AdeD and AdeI mutants of de novo purine biosynthesis: cellular models of de novo purine biosynthesis deficiency disorders.
Neoplasms
Knockdown of PAICS inhibits malignant proliferation of human breast cancer cell lines.
Neoplasms
PAICS contributes to gastric carcinogenesis and participates in DNA damage response by interacting with histone deacetylase 1/2.
Neoplasms
PAICS, a De Novo Purine Biosynthetic Enzyme, Is Overexpressed in Pancreatic Cancer and Is Involved in Its Progression.
Neoplasms
PAICS, a Purine Nucleotide Metabolic Enzyme, is Involved in Tumor Growth and the Metastasis of Colorectal Cancer.
Neoplasms
Roles of highly expressed PAICS in lung adenocarcinoma.
Neuroblastoma
Combinatorial targeting of MTHFD2 and PAICS in purine synthesis as a novel therapeutic strategy.
Pancreatic Neoplasms
PAICS, a De Novo Purine Biosynthetic Enzyme, Is Overexpressed in Pancreatic Cancer and Is Involved in Its Progression.
Perinatal Death
PAICS deficiency, a new defect of de novo purine synthesis resulting in multiple congenital anomalies and fatal outcome.
phosphoribosylaminoimidazole carboxylase deficiency
PAICS contributes to gastric carcinogenesis and participates in DNA damage response by interacting with histone deacetylase 1/2.
phosphoribosylaminoimidazole carboxylase deficiency
PAICS deficiency, a new defect of de novo purine synthesis resulting in multiple congenital anomalies and fatal outcome.
Prostatic Neoplasms
Crystal structures of human PAICS reveal substrate and product binding of an emerging cancer target.
Prostatic Neoplasms
Expression and Role of PAICS, a De Novo Purine Biosynthetic Gene in Prostate Cancer.
Prostatic Neoplasms
Expression and role of PAICS, a de novo purine biosynthetic gene in prostate cancer.
Prostatic Neoplasms
Roles of highly expressed PAICS in lung adenocarcinoma.
Stomach Neoplasms
PAICS contributes to gastric carcinogenesis and participates in DNA damage response by interacting with histone deacetylase 1/2.
Urinary Bladder Neoplasms
A Role for De Novo Purine Metabolic Enzyme PAICS in Bladder Cancer Progression.
Uterine Cervical Neoplasms
Potential suppressive functions of microRNA-504 in cervical cancer cells malignant process were achieved by targeting PAICS and regulating EMT.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 10°C
13
CO2
50 mM Tris-HCl (pH 8.0), at 10°C
0.0038
4-carboxy-5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 10°C
0.009
4-carboxy-5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40
1-(5-phosphoribosyl)-5-aminoimidazole
-
-
16 - 65
4-carboxy-5-aminoimidazole ribonucleotide
77
CO2
50 mM Tris-HCl (pH 8.0), at 30°C
16
4-carboxy-5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 10°C
65
4-carboxy-5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
33
4-carboxy-5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 30°C
6.4
5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 10°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.1
3-nitro-1-(beta-D-ribofuranosyl)pyrrole 5'-phosphate
Gallus gallus
-
IC50 above 0.1 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6.9
determination from amino acid sequence
7.7
calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
SwissProt
brenda
-
UniProt
brenda
-
SwissProt
brenda
-
-
-
brenda
Pigeon
-
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
two enzymes PurK and PurE are required for the reaction
-
-
brenda
-
-
-
brenda
bifunctional enzyme: phosphoribosylaminoimidazole carboxylase/4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide synthetase, with two independent folding domains, each containing a different catalytic site
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
accumulates 5-aminoimidazole ribotide
brenda
-
brenda
-
-
brenda
-
-
brenda
Pigeon
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
17000
-
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
17176
-
x * 17176, subunit I, + x * 42150, subunit II, calculation from nucleotide sequence
17189
8 * 17189, calculated from amino acid sequence
39000
-
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
40500
-
1 * 40500 + 1 * 56000, SDS-PAGE, two subunits associate in a 1:1 ratio
42150
-
x * 17176, subunit I, + x * 42150, subunit II, calculation from nucleotide sequence
50000
-
8 * 50000, SDS-PAGE
56000
-
1 * 40500 + 1 * 56000, SDS-PAGE, two subunits associate in a 1:1 ratio
62200
determination from amino acid sequence, 570 amino acid residues in length
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
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
8 * 17189, calculated from amino acid sequence
homooctamer
8 * 17195, ESI-MS
octamer
-
crystallization data
octamer
-
8 * 50000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
22
-
stable for several days
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
prolonged dialysis of more than 12 h, results in 50% loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4°C, stable for at least 6 months
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ebbole, D.J.; Zalkin, H.
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis
J. Biol. Chem.
262
8274-8287
1987
Bacillus subtilis
brenda
Hilton Patey, C.A.; Shaw, G.
Purification and properties of an enzyme duet, phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase, involved in the biosynthesis of purine nucleotides de novo
Biochem. J.
135
543-545
1973
Gallus gallus
brenda
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
brenda
Saxild, H.H.; Nygaard, P.
Gene-enzyme relationships of the purine biosynthetic pathway in Bacillus subtilis
Mol. Gen. Genet.
211
160-167
1988
Bacillus subtilis
brenda
Rowe, P.B.; McCairns, E.; Madsen, G.; Sauer, D.; Elliott, H.
De novo purine synthesis in avian liver. Co-purification of the enzymes and properties of the pathway
J. Biol. Chem.
253
7711-7721
1978
Pigeon
brenda
Firestine, S.M.; Davisson, V.J.
Carboxylase in de novo purine biosynthesis. Characterization of the Gallus gallus bifunctional enzyme
Biochemistry
33
11917-11926
1994
Gallus gallus
brenda
Firestine, S.M.; Poon, S.W.; Mueller, E.J.; Stubbe, J.; Davisson, V.J.
Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms ?
Biochemistry
33
11927-11934
1994
Gallus gallus, Escherichia coli
brenda
Firestine, S.M.; Davisson, V.J.
A tight binding-inhibitor of 5-aminoimidazole ribonucleotide carboxylase
J. Med. Chem.
36
3484-3486
1993
Gallus gallus
brenda
Humble, R.W.; Mackenzie, G.; Shaw, G.
Rapid purification of a bifunctional protein complex possessing phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (EC 6.3.2.6) activities
Adv. Exp. Med. Biol.
7
223-227
1991
Ovis aries
brenda
Sychrova, H.; Braun, V.; Souciet, J.L.
Molecular cloning and sequence analysis of Zygosaccharomyces rouxii ADE2 gene encoding a phosphoribosyl-aminoimidazole carboxylase
Yeast
15
1399-1402
1999
Schizosaccharomyces pombe (P15567), Saccharomyces cerevisiae (P21264), Ogataea methanolica (Q01930), Candida albicans (Q92210), Zygosaccharomyces rouxii (Q9UVE6)
brenda
Boyle, M.P.; Kalliomaa, A.K.; Levdikov, V.; Blagova, E.; Fogg, M.J.; Brannigan, J.A.; Wilson, K.S.; Wilkinson, A.J.
Crystal structure of PurE (BA0288) from Bacillus anthracis at 1.8 A resolution
Proteins
61
674-676
2005
Bacillus anthracis
brenda
Firestine, S.; Wu, W.; Youn, H.; Jo Davisson, V.
Interrogating the mechanism of a tight binding inhibitor of AIR carboxylase
Bioorg. Med. Chem.
17
794-803
2009
Gallus gallus
brenda
Tranchimand, S.; Starks, C.M.; Mathews, I.I.; Hockings, S.C.; Kappock, T.J.
Treponema denticola PurE is a bacterial AIR carboxylase
Biochemistry
50
4623-4637
2011
Treponema denticola (Q73PV9), Treponema denticola
brenda
Duval, N.; Luhrs, K.; Wilkinson, T.G.; Baresova, V.; Skopova, V.; Kmoch, S.; Vacano, G.N.; Zikanova, M.; Patterson, D.
Genetic and metabolomic analysis of AdeD and AdeI mutants of de novo purine biosynthesis: cellular models of de novo purine biosynthesis deficiency disorders
Mol. Genet. Metab.
108
178-189
2013
Cricetulus griseus (M1R995), Cricetulus griseus
brenda
Taschner, M.; Basquin, J.; Benda, C.; Lorentzen, E.
Crystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 A resolution
Proteins
81
1473-1478
2013
Trichoplusia ni, Bombyx mori (Q1HQ66)
brenda
Select items on the left to see more content.
html completed