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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
borneol dehydrogenase, libdh,
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BDH
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borneol dehydrogenase
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borneol dehydrogenase
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borneol dehydrogenase
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(-)-borneol + NAD+ = (-)-camphor + NADH + H+
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(-)-borneol:NAD+ oxidoreductase
NADP+ can also act, but more slowly.
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(-)-borneol + NAD+
(-)-camphor + NADH
(-)-borneol + NAD+
(-)-camphor + NADH + H+
additional information
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(-)-borneol + NAD+
(-)-camphor + NADH
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(-)-borneol + NAD+
(-)-camphor + NADH
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biosynthesis of camphor from borneol
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(-)-borneol + NAD+
(-)-camphor + NADH + H+
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ir
(-)-borneol + NAD+
(-)-camphor + NADH + H+
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(-)-borneol + NAD+
(-)-camphor + NADH + H+
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stereospecific reaction
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(-)-borneol + NAD+
(-)-camphor + NADH + H+
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(-)-borneol + NAD+
(-)-camphor + NADH + H+
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stereospecific reaction
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additional information
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no activity with other monoterpenes, e.g. alpha terpineol, 1,8-cineole, citronellol, linalool, lavandulol, nerol, geraniol, and perillyl alcohol, and sesquiterpene farnesol, or with menthol, overview
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additional information
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GC-MS analysis of borneol degradation metabolites
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additional information
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the enzyme is also active with (+)-borneol, reaction of EC 1.1.1.198
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additional information
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GC-MS analysis of borneol degradation metabolites
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additional information
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the enzyme is also active with (+)-borneol, reaction of EC 1.1.1.198
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(-)-borneol + NAD+
(-)-camphor + NADH
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biosynthesis of camphor from borneol
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(-)-borneol + NAD+
(-)-camphor + NADH + H+
additional information
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(-)-borneol + NAD+
(-)-camphor + NADH + H+
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ir
(-)-borneol + NAD+
(-)-camphor + NADH + H+
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(-)-borneol + NAD+
(-)-camphor + NADH + H+
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additional information
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GC-MS analysis of borneol degradation metabolites
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additional information
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GC-MS analysis of borneol degradation metabolites
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NADP+
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strong preference for NAD+ over NADP+ is observed. When cofactor NAD+ is replaced by NADP+, the catalytic rate of refolded BDH is reduced to below 5% compared to NAD+
additional information
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no activity with NADP+
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NAD+
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preferred cofactor
NAD+
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strong preference for NAD+ over NADP+ is observed. When cofactor NAD+ is replaced by NADP+, the catalytic rate of refolded BDH is reduced to below 5% compared to NAD+
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additional information
additional information
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Michaelis-Menten kinetics, overview
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0.053
(-)-borneol
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pH 8.0, 30°C, recombinant enzyme
0.16
(-)-borneol
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recombinant enzyme, pH 8.5, 22°C
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0.0004 - 0.53
(-)-borneol
0.0004
(-)-borneol
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pH 8.0, 30°C, recombinant enzyme
0.53
(-)-borneol
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recombinant enzyme, pH 8.5, 22°C
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0.0075
(-)-borneol
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pH 8.0, 30°C, recombinant enzyme
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22
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assay at room temperature
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gene LiBDH
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brenda
isolated from soil samples collected in Hualien County, Taiwan
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brenda
isolated from soil samples collected in Hualien County, Taiwan
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brenda
tansy
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brenda
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specifically in glandular trichomes of mature flowers
brenda
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oil glands
brenda
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brenda
additional information
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the gene exppression is regulated in a tissue-specific manner
brenda
additional information
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strain TCU-HL1 is able to use borneol as the sole carbon source
brenda
additional information
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strain TCU-HL1 is able to use borneol as the sole carbon source
brenda
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brenda
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brenda
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evolution
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the enzyme is a member of the SDR superfamily of enzymes
metabolism
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borneol is converted into camphor by BDH in borneol-degrading strain, Pseudomonas sp. strain TCU-HL1 and is further decomposed through a camphor degradation pathway
metabolism
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borneol is converted into camphor by BDH in borneol-degrading strain, Pseudomonas sp. strain TCU-HL1 and is further decomposed through a camphor degradation pathway
additional information
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molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH
additional information
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molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH
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27500
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x * 27500, about, sequence calculation
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x * 27500, about, sequence calculation
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x * 30000-40000, recombinant enzyme, SDS-PAGE
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x * 30000-40000, recombinant enzyme, SDS-PAGE
additional information
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molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH
additional information
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molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH
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stable to lyophilization
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-40°C, lyophilized, under argon, stable for several months without deterioration
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native enzyme from strain TCU-HL1 by hydrophobic interaction and anion exchange chromatography, recombinant refolded enzyme from Escherichia coli
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recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3)pLysSby nickel affinity chromatography
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gene bdh, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli in inclusion bodies
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gene LiBDH, DNA and amino acid sequence determination and analysis, phylogenetic tree, gene expression is regulated in a tissue-specific manner, expression of the His-tagged enzyme in Escherichia coli strain Rosetta (DE3)pLysS
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recombinant enzyme from Escherichia coli inclusion bodies, solubilized in 25 ml of 0.1 M potassium phosphate buffer, pH 7.0, containing 6 M urea, 10 mM DTT, and 1 mM EDTA, for 2 h at room temperature stirred. Refolding by dissolution in 8 M urea and dialysis against 10 mM potassium phosphate buffer in the presence of 10% glycerol results in an inactive enzyme
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biotechnology
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the gene encoding the borneol dhdrogenase is a target for metabolic engineering for improvement of essential oil production
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Dehal, S.S.; Croteau, R.
Metabolism of monoterpenes: Specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone
Arch. Biochem. Biophys.
258
287-291
1987
Tanacetum vulgare
brenda
Sarker, L.S.; Galata, M.; Demissie, Z.A.; Mahmoud, S.S.
Molecular cloning and functional characterization of borneol dehydrogenase from the glandular trichomes of Lavandula x intermedia
Arch. Biochem. Biophys.
528
163-170
2012
Lavandula x intermedia
brenda
Tsang, H.L.; Huang, J.L.; Lin, Y.H.; Huang, K.F.; Lu, P.L.; Lin, G.H.; Khine, A.A.; Hu, A.; Chen, H.P.
Borneol dehydrogenase from Pseudomonas sp. strain TCU-HL1 catalyzes the oxidation of (+)-borneol and its isomers to camphor
Appl. Environ. Microbiol.
82
6378-6385
2016
Pseudomonas sp., Pseudomonas sp. TCU-HL1
brenda
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1.1.1.227 (-)-borneol dehydrogenase
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