Literature summary for 1.14.11.1 extracted from

Tars, K.; Rumnieks, J.; Zeltins, A.; Kazaks, A.; Kotelovica, S.; Leonciks, A.; Sharipo, J.; Viksna, A.; Kuka, J.; Liepinsh, E.; Dambrova, M.
Crystal structure of human gamma-butyrobetaine hydroxylase (2010), Biochem. Biophys. Res. Commun., 398, 634-639.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged GBBH in Escherichia coli strain WK6	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
3-(2,2,2-trimethylhydrazinium propionate dihydrate)	i.e. mildronate, a synthetic inhibitor of GBBH, is a non-hydroxylatable analog of gamma-butyrobetaine	Homo sapiens
4-Trimethylammoniobutanoate	substrate inhibition at concentrations above 0.2 mM	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0275	-	4-Trimethylammoniobutanoate	pH 7.0, 37°C, recombinant enzyme	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	Fe(II)-binding residues form a conserved His-X-Asp-Xn-His triad	Homo sapiens
Zn2+	quantitative determination of Zn2+ by atomic absorption spectrometry, zinc-binding site structure in the N-terminal domain of GBBH, overview	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
4-trimethylammoniobutanoate + 2-oxoglutarate + O2	Homo sapiens	-	3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O75936	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged GBBH from Escherichia coli strain WK6 by nickel affinity chromatography	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-trimethylammoniobutanoate + 2-oxoglutarate + O2	-	Homo sapiens	3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2	-	?
4-trimethylammoniobutanoate + 2-oxoglutarate + O2	catalytic domain and active site structure, overview	Homo sapiens	3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	the GBBH monomer consists of a catalytic double-stranded beta-helix domain, and a smaller N-terminal domain, the N-terminal domain of GBBH has a similar fold to the DUF971 superfamily. GBBH is dimeric in its biological state. the dimerization interface of GBBH is very different from that of related enzymes, three-dimensional structure, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
gamma-butyrobetaine hydroxylase	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Homo sapiens

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.062	-	pH 7.0, 37°C, recombinant enzyme	Homo sapiens	3-(2,2,2-trimethylhydrazinium propionate dihydrate)

General Information

General Information	Comment	Organism
evolution	the GBBH residues involved in zinc binding are evolutionary conserved in all sequenced eukaryotes more complex than Caenorhabditis elegans	Homo sapiens
physiological function	GBBH is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine. L-Carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy	Homo sapiens