3.5.4.16: GTP cyclohydrolase I

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

Reaction

Synonyms

dihydroneopterin triphosphate synthase, FelE, folE, GCH, GCH-1, GCH1, GCHI, GCYH-IA, GCYH-IB, GTP 8-formylhydrolase, GTP CHase I, GTP cyclohydrolase, GTP cyclohydrolase 1, GTP cyclohydrolase I, GTP cyclohydrolase IA, GTP cyclohydrolase IB, GTP cyclohydrolase-1, GTP-CH, GTP-CH-I, GTP-CH1, GTP-cyclohydrolase 1, GTP-cyclohydrolase I, GTPCH, GTPCH I, GTPCH-1, GTPCH1, GTPCHI, guanosine 5'-triphosphate-cyclohydrolase I, guanosine triphosphate 8-deformylase, guanosine triphosphate cyclohydrolase, guanosine triphosphate cyclohydrolase 1, guanosine triphosphate cyclohydrolase I, guanosine-5'-triphosphate cyclohydrolase 1, hydrolase, guanosine triphosphate cyclo-, MptA, Punch, Punch protein

ECTree

     3 Hydrolases

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

             3.5.4 In cyclic amidines

                3.5.4.16 GTP cyclohydrolase I

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Results	in table
17	Activating Compound
48611	AA Sequence
9	Application
1	CAS Registry Number
30	Cloned(Commentary)
10	Crystallization (Commentary)
1199	Disease/ Diagnostics
5	Expression
34	General Information
1	General Stability
170	Inhibitors
10	Ki Value [mM]
39	KM Value [mM]
14	Localization
24	Metals/Ions
41	Molecular Weight [Da]
58	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
273	Organism
15	Pathway
286	PDB ID
39	pH Optimum
1	pH Range
2	pH Stability
3	Posttranslational Modification
68	Protein Variants
31	Purification (Commentary)
11	Reaction
2	Reaction Type
118	Reference
2	Renatured (Commentary)
86	Source Tissue
29	Specific Activity [micromol/min/mg]
5	Storage Stability
161	Substrates and Products (Substrate)
30	Subunits
120	Synonyms
1	Systematic Name
24	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.5.4.16 - GTP cyclohydrolase I

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

selenomethionine-labeled isozyme GCYH-IB, sitting drop vapor diffusion method, using polyethylene glycol 6000 (10-16% (w/v)), LiCl (1-1.4 M), Tris (50 mM, pH 9.0), and Tris-HCl (50 mM, pH 7.0)

Bacillus subtilis

-

712290

-

Escherichia coli

-

209563

crystallization of purified recombinant enzyme mutants H112S, H113S, and C181S, free, mutant H112S in 0.1 M MES, pH 6.0, 0.2 M sodium acetate, 3 mM sodium azide, or complexed with substrate GTP, mutants H112S and C181S in 0.1 M MOPS, pH 7.0, 10% w/v PEG 6000, 0.1 M ammonium sulfate, or mutant H113S in 0.1 M Tris-HCl, pH 8.5, 0.2 M (NH4)H2PO4, 50% v/v 2-methyl-2,4-pentanediol, addition of GTP for the complex formation, hanging drop vapour diffusion method at room temperature, X-ray diffraction structure determination and analysis at about 2.1-3.2 A resolution, modeling

Escherichia coli

P0A6T5

656511

4.6 mg/ml purified recombinant DELTA42-hGTP-CH-I in 0.1 M potassium phosphate, pH 7.0, 0.02% NaN3, mixed with precipitation solution containing 6% PEG 6000, 150 mM KCl, 100 mM MOPS, pH 7.0, equilibration against precipitant solution, X-ray diffraction strcuture determination and analysis at 3.1 A resolution, modeling

Homo sapiens

P30793

657176

sitting-drop vapor-diffusion method at 20°C. Crystallized from 1.3 M sodium citrate pH 7.3. The crystal structure is solved at a resolution of 2.4 A

Listeria monocytogenes serotype 1/2a

Q8Y5X1

755735

crystals are grown at 20°C by vapor diffusion in sitting drops. High-resolution crystal structures of the enzyme: one in complex with the reaction intermediate analog and competitive inhibitor 8-oxo-GTP, and one with a TRIS molecule bound in the active site and mimicking another reaction intermediate

Neisseria gonorrhoeae

Q5F9K6

756001

5 mg/ml enzyme subunit GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP, free and complexed with the human catalytic subunit of the enzyme, batch procedure, at 4°C overnight, total reflection X-ray fluorescence spectrometry, structure determination and analysis at 2.6 A resolution, modeling

Rattus norvegicus

-

656492

crystallization of purified recombinant enzyme and protein GFRP forming a BH2-induced inhibitory complex, involving dGTP, in 14% isopropanol, 0.2 M ammonium sulfate, 10% PEG 300, 10% ethylene glycol, 0.1 M MES-Na, pH 6.0, rapid freezing of crystals in liquid nitrogen, X-ray diffraction structure determination and analysis at 2.8 A resolution

Rattus norvegicus

-

656261

purified recombinant enzyme complexed with recombinant wild-type and selenomethionine derivatized GFRP, the complex with the latter being used as CH3HGCl derivative, 5 mg/ml protein complex in 24% v/v 2-methyl-2,4-pentanediol, 75 mM Tris-HCl, pH 7.5, 50 mM KCl, 5 mM phenylalanine, X-ray diffraction structure determination and analysis at 2.7-2.8 A resolution, model building

Rattus norvegicus

-

657188

purified enzyme complexed with 8-oxo-GTP or 8-oxo-dGTP, and as free enzyme, hanging drop vapour diffusion method, 20°C, 0.002 ml of 13.7 mg/ml protein is mixed with 0.002 ml reservoir solution containing 0.1 M HEPES, pH 6.8, 2.0 M ammonium sulfate, 3.4% PEG 400, and 15% glycerol, X-ray diffraction structure determination and analysis at 2.0 and 1.8 A or at 2.2. A resolution, respectively

Thermus thermophilus

Q5SH52

669149