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1.14.11.1: gamma-butyrobetaine dioxygenase

This is an abbreviated version!
For detailed information about gamma-butyrobetaine dioxygenase, go to the full flat file.

Word Map on EC 1.14.11.1

Reaction

4-Trimethylammoniobutanoate
+
2-oxoglutarate
+
O2
=
3-hydroxy-4-trimethylammoniobutanoate
+
succinate
+
CO2

Synonyms

4-trimethylaminobutyric acid dioxygenase, alpha-butyrobetaine hydroxylase, BBD, BBH, BBOX, BBOX1, Bu hydroxylase, butyrobetaine hydroxylase, gamma butyrobetaine hydroxylase, gamma-BBD, gamma-BBH, gamma-buryrobetaine dioxygenase, gamma-butyrobetaine dioxygenase, gamma-butyrobetaine hydroxylase, gamma-butyrobetaine hydroxylase 1, GBB hydroxylase, GBBH, hBBOX, oxygenase, gamma-butyrobetaine di-, psBBOX

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.1 gamma-butyrobetaine dioxygenase

Crystallization

Crystallization on EC 1.14.11.1 - gamma-butyrobetaine dioxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of a crystal structure of human BBOX in complex with inhibitor AR692B and Ni2+ (an Fe2+ surrogate), P212121 space group, 2.8 A resolution
crystal structure analysis, PDB ID 3O2G
purified recombinant enzyme in complex with inhibitors 4-(ethyldimethylammonio)butanoate, 3-carboxy-N-(2-fluoroethyl)-N,N-dimethylpropan-1-aminium, 1-(3-carboxypropyl)-1-methylpyrrolidin-1-ium, 4-(trimethylammonio)pentanoate, [3-(trimethylammonio)propyl]phosphinate, and 3-(1,1,1,2-tetramethylhydrazin-1-ium-2-yl)propanoate, sitting drop vapor technique, mixing of 0.001 ml of 7 mg/ml protein, 8 mM N-oxalylglycine and 4 mM inhibitor, with 0.001 ml of well solution containing 0.2 M ammonium citrate, 20% PEG 3350, 3% hexanediamine, and 10 mM ZnSO4, pH 7.0, X-ray diffraction structure determination and analysis at 1.70-2.40 A resolution
purified recombinant His-tagged GBBH, and SeMet-labeled variant, by sitting drop vapor diffusion technique, mixing 0.001 ml of 7 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.2 M ammonium sulfate and 100 mM sodium acetate, pH 4.5. In co-crystallization trials with ligands, each ligand is added to the reservoir solution to a final concentration of 5 mM, X-ray diffraction structure determination and analysis at 2.0 A and 3.5 A resolution, respectively