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Literature summary extracted from

  • Rydzik, A.M.; Leung, I.K.; Kochan, G.T.; Loik, N.D.; Henry, L.; McDonough, M.A.; Claridge, T.D.; Schofield, C.J.
    Comparison of the substrate selectivity and biochemical properties of human and bacterial gamma-butyrobetaine hydroxylase (2014), Org. Biomol. Chem., 12, 6354-6358 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.11.1 ascorbate required Homo sapiens

Application

EC Number Application Comment Organism
1.14.11.1 medicine BBOX is a therapeutic target in humans, the BBOX inhibitor mildronate is used to decrease fatty acid oxidation in patients after myocardial infarction Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.1 gene BBOX1, recombinant expression of His-tagged codon-optimized enzyme in Escherichia coli strain BL21(DE3) Homo sapiens
1.14.11.1 recombinant expression of N-terminally His-tagged codon-optimized enzyme in Escherichia coli strain BL21(DE3) Pseudomonas sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.1 crystal structure analysis, PDB ID 3O2G Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.1 (3R)-3-fluoro-4-(trimethylammonio)butanoate
-
 Homo sapiens
1.14.11.1 3-carboxy-N-(fluoromethyl)-N,N-dimethylpropan-1-aminium
-
 Homo sapiens
1.14.11.1 4-Trimethylammoniobutanoate substrate inhibition Homo sapiens
1.14.11.1 4-Trimethylammoniobutanoate substrate inhibition at high concentrations Pseudomonas sp.
1.14.11.1 mildronate
-
 Homo sapiens
1.14.11.1 N-oxalylglycine
-
 Homo sapiens
1.14.11.1 N-oxalylglycine binding structure modeling Pseudomonas sp.
1.14.11.1 Ni2+ binding structure modeling Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.1 additional information
-
 additional information Michaelis-Menten kinetics Homo sapiens
1.14.11.1 additional information
-
 additional information Michaelis-Menten kinetics Pseudomonas sp.
1.14.11.1 0.0042
-
 4-Trimethylammoniobutanoate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.02
-
 (3R)-3-fluoro-4-(trimethylammonio)butanoate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.02
-
 (2S)-3-carboxy-N-(fluoromethyl)-2-hydroxy-N,N-dimethylpropan-1-aminium pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.153
-
 2-oxoglutarate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.163
-
 4-Trimethylammoniobutanoate pH 7.5, temperature not specified in the publication, only the Michaelis-Menten range is fitted Pseudomonas sp.
1.14.11.1 0.412
-
 (2S)-3-carboxy-N-(fluoromethyl)-2-hydroxy-N,N-dimethylpropan-1-aminium pH 7.5, temperature not specified in the publication Pseudomonas sp.
1.14.11.1 0.532
-
 2-oxoglutarate pH 7.5, temperature not specified in the publication Pseudomonas sp.
1.14.11.1 0.623
-
 (3R)-3-fluoro-4-(trimethylammonio)butanoate pH 7.5, temperature not specified in the publication Pseudomonas sp.
1.14.11.1 2.474
-
 4-Trimethylammoniobutanoate pH 7.5, temperature not specified in the publication, the whole range is fitted Pseudomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.1 Fe2+ nonheme Fe2+-dependent oxygenase, dependent on, required for catalysis Homo sapiens
1.14.11.1 Fe2+ nonheme Fe2+-dependent oxygenase, dependent on, required for catalysis Pseudomonas sp.
1.14.11.1 additional information Ni2+ cannot substitute for Fe2+ Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.1 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 Homo sapiens
-
 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
 ?
1.14.11.1 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 Pseudomonas sp.
-
 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
 ?
1.14.11.1 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 Pseudomonas sp. AK-1
-
 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.1 Homo sapiens O75936
-
-
1.14.11.1 Pseudomonas sp. P80193
-
-
1.14.11.1 Pseudomonas sp. AK-1 P80193
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.11.1 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography Homo sapiens
1.14.11.1 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography, to over 90% purity Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.1 (3R)-3-fluoro-4-(trimethylammonio)butanoate + 2-oxoglutarate + O2
-
 Homo sapiens 3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + formylfluoride
-
 ?
1.14.11.1 (3R)-3-fluoro-4-(trimethylammonio)butanoate + 2-oxoglutarate + O2
-
 Pseudomonas sp. 3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + formylfluoride
-
 ?
1.14.11.1 (3R)-3-fluoro-4-(trimethylammonio)butanoate + 2-oxoglutarate + O2
-
 Pseudomonas sp. AK-1 3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + formylfluoride
-
 ?
1.14.11.1 (R)-2-amino-3-carboxy-N,N,N-trimethylpropan-1-aminium + 2-oxoglutarate + O2
-
 Pseudomonas sp. N-[(3R)-3-amino-3-carboxy-2-hydroxypropyl]-N,N-dimethylmethanaminium + succinate + CO2
-
 ?
1.14.11.1 (R)-2-amino-3-carboxy-N,N,N-trimethylpropan-1-aminium + 2-oxoglutarate + O2
-
 Pseudomonas sp. AK-1 N-[(3R)-3-amino-3-carboxy-2-hydroxypropyl]-N,N-dimethylmethanaminium + succinate + CO2
-
 ?
1.14.11.1 (S)-2-amino-3-carboxy-N,N,N-trimethylpropan-1-aminium + 2-oxoglutarate + O2
-
 Pseudomonas sp. N-[(3S)-3-amino-3-carboxy-2-hydroxypropyl]-N,N-dimethylmethanaminium + succinate + CO2
-
 ?
1.14.11.1 (S)-2-amino-3-carboxy-N,N,N-trimethylpropan-1-aminium + 2-oxoglutarate + O2
-
 Pseudomonas sp. AK-1 N-[(3S)-3-amino-3-carboxy-2-hydroxypropyl]-N,N-dimethylmethanaminium + succinate + CO2
-
 ?
1.14.11.1 (S)-3-carboxy-2-hydroxy-N,N,N-trimethylpropan-1-aminium + 2-oxoglutarate + O2
-
 Pseudomonas sp. (3S)-3-carboxy-2,3-dihydroxy-N,N,N-trimethylpropan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 2-carboxy-N,N,N-trimethylethan-1-aminium + 2-oxoglutarate + O2
-
 Homo sapiens 4-carboxy-3-hydroxy-N,N,N-trimethylbutan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 2-carboxy-N,N,N-trimethylethan-1-aminium + 2-oxoglutarate + O2
-
 Pseudomonas sp. 4-carboxy-3-hydroxy-N,N,N-trimethylbutan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 3-carboxy-N-(fluoromethyl)-N,N-dimethylpropan-1-aminium + 2-oxoglutarate + O2
-
 Homo sapiens (2S)-3-carboxy-N-(fluoromethyl)-2-hydroxy-N,N-dimethylpropan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 3-carboxy-N-(fluoromethyl)-N,N-dimethylpropan-1-aminium + 2-oxoglutarate + O2
-
 Pseudomonas sp. (2S)-3-carboxy-N-(fluoromethyl)-2-hydroxy-N,N-dimethylpropan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 4-trimethylammoniobutanoate + 2-oxoglutarate + O2
-
 Homo sapiens 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
 ?
1.14.11.1 4-trimethylammoniobutanoate + 2-oxoglutarate + O2
-
 Pseudomonas sp. 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
 ?
1.14.11.1 4-trimethylammoniobutanoate + 2-oxoglutarate + O2
-
 Pseudomonas sp. AK-1 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
-
 ?
1.14.11.1 4-trimethylammoniopropanoate + 2-oxoglutarate + O2
-
 Homo sapiens 2-carboxy-2-hydroxy-N,N,N-trimethylethan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 D-carnitine + 2-oxoglutarate + O2
-
 Homo sapiens 3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 D-carnitine + 2-oxoglutarate + O2
-
 Pseudomonas sp. 3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 L-carnitine + 2-oxoglutarate + O2
-
 Homo sapiens 3-carboxy-N,N,N-trimethyl-2-oxopropan-1-aminium + succinate + CO2
-
 ?
1.14.11.1 additional information no activity with trimethyllysine, acetylcholine, phosphocholine, thioacetylcholine, carbachol, and gamma-butyrobetaine analogues carboxy-N,N,N-trimethylmethanaminium, 5-carboxy-N,N,N-trimethylpentan-1-aminium, N,N,N-trimethyl-4-oxopentan-1-aminium, and 4-methoxy-N,N,N-trimethyl-4-oxobutan-1-aminium, substrate specificity, overview Homo sapiens ?
-
 ?
1.14.11.1 additional information no activity with trimethyllysine, acetylcholine, phosphocholine, thioacetylcholine, carbachol, and gamma-butyrobetaine analogues carboxy-N,N,N-trimethylmethanaminium, 5-carboxy-N,N,N-trimethylpentan-1-aminium, N,N,N-trimethyl-4-oxopentan-1-aminium, and 4-methoxy-N,N,N-trimethyl-4-oxobutan-1-aminium, substrate specificity, overview Pseudomonas sp. ?
-
 ?
1.14.11.1 additional information no activity with trimethyllysine, acetylcholine, phosphocholine, thioacetylcholine, carbachol, and gamma-butyrobetaine analogues carboxy-N,N,N-trimethylmethanaminium, 5-carboxy-N,N,N-trimethylpentan-1-aminium, N,N,N-trimethyl-4-oxopentan-1-aminium, and 4-methoxy-N,N,N-trimethyl-4-oxobutan-1-aminium, substrate specificity, overview Pseudomonas sp. AK-1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.11.1 More homology structure modelling Homo sapiens
1.14.11.1 More homology structure modelling Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
1.14.11.1 BBOX
-
 Homo sapiens
1.14.11.1 BBOX
-
 Pseudomonas sp.
1.14.11.1 gamma-butyrobetaine hydroxylase
-
 Homo sapiens
1.14.11.1 gamma-butyrobetaine hydroxylase
-
 Pseudomonas sp.
1.14.11.1 hBBOX
-
 Homo sapiens
1.14.11.1 psBBOX
-
 Pseudomonas sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.11.1 0.059
-
 (3R)-3-fluoro-4-(trimethylammonio)butanoate pH 7.5, temperature not specified in the publication Pseudomonas sp.
1.14.11.1 0.14
-
 (3R)-3-fluoro-4-(trimethylammonio)butanoate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.3
-
 (2S)-3-carboxy-N-(fluoromethyl)-2-hydroxy-N,N-dimethylpropan-1-aminium pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.83
-
 4-Trimethylammoniobutanoate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 1.6
-
 2-oxoglutarate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 3.5
-
 2-oxoglutarate pH 7.5, temperature not specified in the publication Pseudomonas sp.
1.14.11.1 5
-
 (2S)-3-carboxy-N-(fluoromethyl)-2-hydroxy-N,N-dimethylpropan-1-aminium pH 7.5, temperature not specified in the publication Pseudomonas sp.
1.14.11.1 21.3
-
 4-Trimethylammoniobutanoate pH 7.5, temperature not specified in the publication Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.11.1 7.5
-
 assay at Homo sapiens
1.14.11.1 7.5
-
 assay at Pseudomonas sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.11.1 0.024
-
 4-Trimethylammoniobutanoate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.125
-
 4-Trimethylammoniobutanoate pH 7.5, temperature not specified in the publication Pseudomonas sp.
1.14.11.1 0.136
-
 (3R)-3-fluoro-4-(trimethylammonio)butanoate pH 7.5, temperature not specified in the publication Homo sapiens
1.14.11.1 0.226
-
 3-carboxy-N-(fluoromethyl)-N,N-dimethylpropan-1-aminium pH 7.5, temperature not specified in the publication Homo sapiens

General Information

EC Number General Information Comment Organism
1.14.11.1 evolution comparison of properties, substrate specificities, and structures of the human enzyme (PDB ID 3O2G) and the enzyme from Pseudomonas sp. AK1, detailed overview Homo sapiens
1.14.11.1 evolution comparison of properties, substrate specificities, and structures of the human enzyme (PDB ID 3O2G) and the enzyme from Pseudomonas sp. AK1, detailed overview Pseudomonas sp.
1.14.11.1 metabolism gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step in the biosynthesis of carnitine i.e. the stereoselective hydroxylation of gamma-butyrobetaine (GBB) Homo sapiens
1.14.11.1 metabolism gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step in the biosynthesis of carnitine i.e. the stereoselective hydroxylation of gamma-butyrobetaine (GBB) Pseudomonas sp.
1.14.11.1 additional information homology structure modeling with bound Ni2+ and N-oxalglycine, modeled based on human BBOX structure, DB ID 2O2G Pseudomonas sp.