Information on EC 5.4.99.18 - 5-(carboxyamino)imidazole ribonucleotide mutase

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

EC NUMBER
COMMENTARY hide
5.4.99.18
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RECOMMENDED NAME
GeneOntology No.
5-(carboxyamino)imidazole ribonucleotide mutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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inosine-5'-phosphate biosynthesis I
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inosine-5'-phosphate biosynthesis III
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Metabolic pathways
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Purine metabolism
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purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole carboxymutase
In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates [6]. In the absence of EC 6.3.2.6, phosphoribosylaminoimidazolesuccinocarboxamide synthase, the reaction is reversible [3]. The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation [3].
CAS REGISTRY NUMBER
COMMENTARY hide
255379-40-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 6872
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Manually annotated by BRENDA team
NK6051
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Manually annotated by BRENDA team
gene purE
A6QFS3
UniProt
Manually annotated by BRENDA team
DSM1617
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
A6QFS3
His38 is essential for function, role of His38 as a general acid/base catalyst, structure analysis, comparison to Homo sapiens class II PurE enzyme, active site structure, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
show the reaction diagram
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
show the reaction diagram
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
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
show the reaction diagram
A6QFS3
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
A6QFS3
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007 - 0.2
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 15.6
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
0.0021 - 15.5
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36
pH 8.0, 37C, direction of decarboxylation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
A6QFS3
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
A6QFS3
assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Staphylococcus aureus (strain Newman)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
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8 * 17000, SDS-PAGE
18864
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
18900
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
21000
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
126000
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gel filtration
136000
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sucrose density gradient ultracentrifugation
197000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop method, crystals grow best at 295 K with the optimized mother-liquor conditions of 21-23% PEG 4K, 0.19 M ammonium acetate and 90 mM citrate, pH 5.25-5.5. Crystals belong to space group I422, with unit-cell parameters a = 99.25, c = 164.81 A
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multiple REDOR NMR studies of a 151000 Da complex of uniformly 15N-labeled enzyme and the active site ligand [6-13C]-citrate show a single ionization equilibrium associated with the key histidine H59. H59 exists in approximately equimolar amounts of an Ndelta-unprotonated pyridine-like form and an Ndelta-protonated pyrrole-like form. Proton transfer mechanism involves H59 Ndelta
mutant H59N soaked in 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, protonation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate C4 may occur in absence of H59
hanging-drop vapor-diffusion method, crystals grown in the presence of 4-carboxaminoimidazole ribonucleotide belong to space group P2(1)2(1)2(1), with unit cell parameters a = 86.92, b = 94.55 and c = 149.96 A. The 1.5 A crystal structure reveals an octameric structure with 422 symmetry
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wild-type cocrystallized with 4-nitroaminoimidazole ribonucleotide and mutants H45N and H45Q soaked with 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
purified recombinant detagged enzyme, crystallization at room temperature, 10 mg/ml protein is mixed with a reservoir solution consisting of 0.1 M sodium acetate trihydrate, pH 4.5, and 2 M ammonium sulfate, 24 h, X-ray diffraction structure determination and analysis at 1.45 Aresolution, molecular replacement using the structure of Bacillus anthracis PurE, PDB ID 1xmp, as template
A6QFS3
nanodroplet vapor diffusion method, 1.77 A resolution, unit cell parameters: a = b = 103.25 A, c = 65.45 A, alpha = beta = 90
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
maximum of enzyme stability near pH 7.0
678203
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
melting temperature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
A6QFS3
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme is active in Escherichia coli
expression in Escherichia coli
gene purE, expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3)
A6QFS3
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H59D
0.16% of wild-type activity
H59N
inactive, crystallization data
H59Q
almost inactive
H89D
4.4% of wild-type activity
H89F
14% of wild-type activity
H89G
91% of wild-type activity
H89N
2.9% of wild-type activity
H89V
17% of wild-type activity
H45N
very low catalytic activity
H45Q
very low catalytic activity
H45W
very low catalytic activity
H38F
A6QFS3
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
H38N
A6QFS3
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
H38W
A6QFS3
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
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