5.4.99.18: 5-(carboxyamino)imidazole ribonucleotide mutase

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For detailed information about 5-(carboxyamino)imidazole ribonucleotide mutase, go to the full flat file.

Reaction

Synonyms

BaPurE, N5-CAIR mutase, N5-carboxy-amino-imidazole ribonucleotide mutase, N5-carboxyaminoimidazole ribonucleotide mutase, N5-carboxyaminoimidazole ribonucleotide synthetase, PurE

ECTree

     5 Isomerases

         5.4 Intramolecular transferases

             5.4.99 Transferring other groups

                5.4.99.18 5-(carboxyamino)imidazole ribonucleotide mutase

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Results	in table
36478	AA Sequence
1	Application
1	CAS Registry Number
8	Cloned(Commentary)
7	Crystallization (Commentary)
3	General Information
22	Inhibitors
9	KM Value [mM]
1	Metals/Ions
8	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
21	Organism
7	Pathway
36	PDB ID
3	pH Optimum
1	pH Stability
17	Protein Variants
5	Purification (Commentary)
3	Reaction
17	Reference
2	Specific Activity [micromol/min/mg]
9	Substrates and Products (Substrate)
3	Subunits
23	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Stability [°C]
13	Turnover Number [1/s]

Crystallization

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

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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

Acetobacter aceti

-

660590

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

Acetobacter aceti

Q2QJL3

678322

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

Acetobacter aceti

Q2QJL2

678203

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

Escherichia coli

-

663416

wild-type cocrystallized with 4-nitroaminoimidazole ribonucleotide and mutants H45N and H45Q soaked with 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate

Escherichia coli

P0AG18

678260

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

Staphylococcus aureus

A0A0H3K7Y1

726578

nanodroplet vapor diffusion method, 1.77 A resolution, unit cell parameters: a = b = 103.25 A, c = 65.45 A, alpha = beta = 90°

Thermotoga maritima

-

663353