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]

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

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

drug development

Bacillus anthracis

A0A1S0QXP6

the enzyme in the de novo purine biosynthesis pathway is an attractive target for antibacterial drug design. Zenobia fragment library screening by saturation transfer difference nucleus magnetic resonance (STD-NMR), water-ligand observed via gradient spectroscopy (WaterLOGSY) NMR, and surface plasmon resonance (SPR) methods, method optimization, overview. The selected compouds are categorized into five different basic scaffolds, and at least two fragments from two different scaffolds exhibit inhibitory activity against the BaPurE enzyme

747257