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Literature summary extracted from

  • Kamps, J.J.; Khan, A.; Choi, H.; Lesniak, R.K.; Brem, J.; Rydzik, A.M.; McDonough, M.A.; Schofield, C.J.; Claridge, T.D.; Mecinovic, J.
    Cation-Pi interactions contribute to substrate recognition in gamma-butyrobetaine hydroxylase catalysis (2016), Chemistry, 22, 1270-1276 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.11.1 ascorbate required Pseudomonas sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.1 recombinant expression of His-tagged enzyme Pseudomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.1 (3-carboxy-2-oxopropyl)(trimethyl)arsanium
-
 Pseudomonas sp.
1.14.11.1 (3-carboxy-2-oxopropyl)(trimethyl)phosphanium
-
 Pseudomonas sp.
1.14.11.1 (3-carboxypropyl)(trimethyl)arsanium
-
 Pseudomonas sp.
1.14.11.1 (3-carboxypropyl)(trimethyl)phosphanium
-
 Pseudomonas sp.
1.14.11.1 N-(3-hydroxypyridine-2-carbonyl)-S-[(pyridin-2-yl)methyl]-L-cysteine
-
 Pseudomonas sp.
1.14.11.1 [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)arsanium
-
 Pseudomonas sp.
1.14.11.1 [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)phosphanium
-
 Pseudomonas sp.
1.14.11.1 [(2S)-3-carboxy-2-hydroxypropyl](trimethyl)arsanium
-
 Pseudomonas sp.
1.14.11.1 [(2S)-3-carboxy-2-hydroxypropyl](trimethyl)phosphanium
-
 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 kinetic analysis, overview Pseudomonas sp.
1.14.11.1 1
-
 4-Trimethylammoniobutanoate pH 7.5, 23°C Pseudomonas sp.
1.14.11.1 1.2
-
 (3-carboxypropyl)(trimethyl)phosphanium pH 7.5, 23°C Pseudomonas sp.
1.14.11.1 1.37
-
 (3-carboxypropyl)(trimethyl)arsanium pH 7.5, 23°C 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, bound to the active site 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 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 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 by nickel affinity chromatography, gel filtration, ultrafiltration, and buffer exchange via desalting gel filtration Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.1 (3-carboxypropyl)(trimethyl)arsanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)arsanium + succinate + CO2
-
 ?
1.14.11.1 (3-carboxypropyl)(trimethyl)arsanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. AK-1 [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)arsanium + succinate + CO2
-
 ?
1.14.11.1 (3-carboxypropyl)(trimethyl)phosphanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)phosphanium + succinate + CO2
-
 ?
1.14.11.1 (3-carboxypropyl)(trimethyl)phosphanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. AK-1 [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)phosphanium + 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 additional information cation-Pi interactions contribute to substrate recognition in gamma-butyrobetaine hydroxylase catalysis. BBOX contains an aromatic cage for the recognition of the positively charged trimethylammonium group of the gamma-butyrobetaine substrate. Substrate analogues (3-carboxypropyl)(trimethyl)phosphanium and (3-carboxypropyl)(trimethyl)arsanium with P and As substituting for N in the trimethylammonium group are good BBOX substrates, which follow the efficiency trend N+ >P+ >As+. An uncharged carbon analogue N-(3-hydroxypyridine-2-carbonyl)-S-[(pyridin-2-yl)methyl]-L-cysteine of gamma-butyrobetaine is not a BBOX substrate. Importance of the energetically favorable cation-Pi interactions in productive substrate recognition. Homology modeling of binding modes and structures of (3-carboxypropyl)(trimethyl)phosphanium and (3-carboxypropyl)(trimethyl)arsanium to psBBOX using an X-ray crystal structure of human BBOX in complex with ZnII, N-oxalylglycine, and gamma-butyrobetaine, PDB ID 3O2G, quantum mechanical calculations and docking simulations. Substrate specificity, overview Pseudomonas sp. ?
-
 ?
1.14.11.1 additional information cation-Pi interactions contribute to substrate recognition in gamma-butyrobetaine hydroxylase catalysis. BBOX contains an aromatic cage for the recognition of the positively charged trimethylammonium group of the gamma-butyrobetaine substrate. Substrate analogues (3-carboxypropyl)(trimethyl)phosphanium and (3-carboxypropyl)(trimethyl)arsanium with P and As substituting for N in the trimethylammonium group are good BBOX substrates, which follow the efficiency trend N+ >P+ >As+. An uncharged carbon analogue N-(3-hydroxypyridine-2-carbonyl)-S-[(pyridin-2-yl)methyl]-L-cysteine of gamma-butyrobetaine is not a BBOX substrate. Importance of the energetically favorable cation-Pi interactions in productive substrate recognition. Homology modeling of binding modes and structures of (3-carboxypropyl)(trimethyl)phosphanium and (3-carboxypropyl)(trimethyl)arsanium to psBBOX using an X-ray crystal structure of human BBOX in complex with ZnII, N-oxalylglycine, and gamma-butyrobetaine, PDB ID 3O2G, quantum mechanical calculations and docking simulations. Substrate specificity, overview Pseudomonas sp. AK-1 ?
-
 ?
1.14.11.1 [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)arsanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. (3-carboxy-2-oxopropyl)(trimethyl)arsanium + succinate + CO2
-
 ?
1.14.11.1 [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)arsanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. AK-1 (3-carboxy-2-oxopropyl)(trimethyl)arsanium + succinate + CO2
-
 ?
1.14.11.1 [(2R)-3-carboxy-2-hydroxypropyl](trimethyl)phosphanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. (3-carboxy-2-oxopropyl)(trimethyl)phosphanium + succinate + CO2
-
 ?
1.14.11.1 [(2S)-3-carboxy-2-hydroxypropyl](trimethyl)arsanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. (3-carboxy-2-oxopropyl)(trimethyl)arsanium + succinate + CO2
-
 ?
1.14.11.1 [(2S)-3-carboxy-2-hydroxypropyl](trimethyl)phosphanium + 2-oxoglutarate + O2
-
 Pseudomonas sp. (3-carboxy-2-oxopropyl)(trimethyl)phosphanium + succinate + CO2
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.11.1 23
-
 assay at 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 2.61
-
 (3-carboxypropyl)(trimethyl)arsanium pH 7.5, 23°C Pseudomonas sp.
1.14.11.1 4.13
-
 (3-carboxypropyl)(trimethyl)phosphanium pH 7.5, 23°C Pseudomonas sp.
1.14.11.1 7.02
-
 4-Trimethylammoniobutanoate pH 7.5, 23°C Pseudomonas sp.

pH Optimum

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

General Information

EC Number General Information Comment Organism
1.14.11.1 evolution the enzyme belongs to the 2-oxoglutarate/Fe(II) dependent oxygenase family Pseudomonas sp.
1.14.11.1 physiological function gamma-butyrobetaine hydroxylase (BBOX) is a nonheme Fe(II)- and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of gamma-butyrobetaine in the final step of carnitine biosynthesis Pseudomonas sp.