3.5.4.10: IMP cyclohydrolase

This is an abbreviated version!
For detailed information about IMP cyclohydrolase, go to the full flat file.

Reaction

Synonyms

5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase, 5-aminoimidazole-4-carboxamide ribonucleotide tranformylase/IMP cyclohydrolase, AF1811, AICAR tranformylase/IMP cyclohydrolase, AICAR transformylase/IMP cyclohydrolase, AICAR transformylase/inosine 5'-monophosphate cyclohydrolase, AICAR-FT/IMP-CHase, AICAR-transformylase/IMP cyclohydrolase, ATIC, atic-1, IMP synthetase, IMPCH, IMPCHase, inosinate cyclohydrolase, inosine 5'-monophosphate cyclohydrolase, inosine monophosphate cyclohydrolase, inosinicase, ITGA2, MjPurO, MthPurO, PurH, PurH2, PurH2-type IMP cyclohydrolase, PurO, PurO-type IMP cyclohydrolase, TK0430

ECTree

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.4 In cyclic amidines

                3.5.4.10 IMP cyclohydrolase

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Results	in table
2	Activating Compound
37909	AA Sequence
3	Application
1	CAS Registry Number
17	Cloned(Commentary)
6	Crystallization (Commentary)
397	Disease/ Diagnostics
1	Expression
12	General Information
4	IC50 Value
26	Inhibitors
2	kcat/KM [mM/s]
3	Ki Value [mM]
26	KM Value [mM]
1	Metals/Ions
13	Molecular Weight [Da]
24	Natural Substrates/ Products (Substrates)
40	Organism
8	Pathway
58	PDB ID
12	pH Optimum
2	pH Range
3	pH Stability
1	pI Value
1	Posttranslational Modification
30	Protein Variants
16	Purification (Commentary)
6	Reaction
1	Reaction Type
39	Reference
19	Source Tissue
10	Specific Activity [micromol/min/mg]
2	Storage Stability
45	Substrates and Products (Substrate)
19	Subunits
44	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
1	Temperature Range [°C]
8	Temperature Stability [°C]
23	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.5.4.10 - IMP cyclohydrolase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

enzyme in complex with inhibitors, sitting drop vapor diffusion method, 22°C, 10 mg/ml protein, mixing of equal volumes of protein and reservoir solutions, the latter containing 20% w/v PEG 8000, 0.2 M imidazole, pH 7.2, 5 mM dithiothreitol, X-ray diffraction structure determination and analysis at 2.0-2.7 A resolution

Gallus gallus

P31335

687546

-

Homo sapiens

P31939

650235

in complex with transformylase inhibitors BW1540 and BW2315

Homo sapiens

P31939

652530

MthPurO in complex with either IMP or 5-aminoimidazole-4-carboxamide ribonucleotide, crystals from 30 mg/ml protein in 25-30% MPD, 0.2 M ammonium acetate, and 0.1 M sodium citrate buffer, pH 5.6, 0.001 ml protein solution is mixed with 0.001 ml of reservoir solution, equilibration against 0.5 mL reservoir solution, 24°C, od-shaped crystals, 3-4 weeks, X-ray diffraction structure determination and analysis at 2.0 A and 2.6 A resolution, respectively, method optimization, molecular replacement and modelling

Methanothermobacter thermautotrophicus

O27089

685152

MthPurO in complex with either IMP or 5-aminoimidazole-4-carboxamide ribonucleotide, X-ray diffraction structure determination and analysis at 2.0 A and 2.6 A resolution, respectively

Methanothermobacter thermautotrophicus

O27089

685152

20 mg/ml purified recombinant enzyme in 20 mM Tris, pH 7.9, 150 mM NaCl, 0.25 mM TCEP, nanodroplet vapor diffusion method, the crystallization solution contains 20% w/v PEG 6000 and 0.1 M citrate pH 5.0, 10% v/v PEG 200 as a cryoprotectant, X-ray diffraction structure determination and anaylsis at 1.88 A resolution, modelling

Thermotoga maritima

Q9X0X6

689976