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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC 1.1.1.182
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formerly, part transferred
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BDH
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cf. EC1.1.1.198
borneol dehydrogenase
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borneol dehydrogenase
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TCK1_3449
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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 + H+
(-)-camphor + NADH + H+
(-)-borneol + NAD+
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r
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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r
(-)-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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?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
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biosynthesis of camphor from borneol
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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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(+)-borneol is the preferred substrate, reaction of EC 1.1.1.198
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additional information
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additional substrates are (+)-borneol, (+)-camphor and (+)-isoborneol, reaction of EC 1.1.1.198. No substrates: isopropanol, cyclopentanol, cyclohexanol, 1,2-butandiol, 2-butanol, L-carveol, and DL-menthol
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additional information
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additional substrates are (+)-borneol, (+)-camphor and (+)-isoborneol, reaction of EC 1.1.1.198. No substrates: isopropanol, cyclopentanol, cyclohexanol, 1,2-butandiol, 2-butanol, L-carveol, and DL-menthol
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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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(+)-borneol is the preferred substrate, reaction of EC 1.1.1.198
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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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?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
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biosynthesis of camphor from borneol
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?
additional information
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(+)-borneol is the preferred substrate, 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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?
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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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(-)-Camphor
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0.06
NAD+
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wild-type, pH 7.5, 30°C
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
0.11
(-)-borneol
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wild-type, pH 7.5, 30°C
0.16
(-)-borneol
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recombinant enzyme, pH 8.5, 22°C
0.21
(-)-borneol
soluble recombinant protein, pH 7, 25°C
0.34
(-)-borneol
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mutant Y188A, pH 7.5, 30°C
0.64
(-)-borneol
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pH 7, 25°C
0.73
(-)-borneol
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mutant Y188T, pH 7.5, 30°C
0.85
(-)-borneol
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pH 11, 25°C
1.5
(-)-borneol
refolded recombinant protein, pH 7, 25°C
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0.0004 - 29.4
(-)-borneol
0.0004
(-)-borneol
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pH 8.0, 30°C, recombinant enzyme
0.07
(-)-borneol
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mutant Y188A, pH 7.5, 30°C
0.13
(-)-borneol
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mutant Y188T, pH 7.5, 30°C
0.38
(-)-borneol
refolded recombinant protein, pH 7, 25°C
0.53
(-)-borneol
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recombinant enzyme, pH 8.5, 22°C
0.97
(-)-borneol
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wild-type, pH 7.5, 30°C
11.3
(-)-borneol
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pH 7, 25°C
12.4
(-)-borneol
soluble recombinant protein, pH 7, 25°C
29.4
(-)-borneol
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pH 11, 25°C
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0.0075
(-)-borneol
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pH 8.0, 30°C, recombinant enzyme
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0.08
(-)-Camphor
soluble recombinant protein, pH 7, 25°C
0.52
(-)-Camphor
refolded recombinant protein, pH 7, 25°C
1.03
(-)-Camphor
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pH 7, 25°C
1.07
(-)-Camphor
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pH 11, 25°C
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4.5
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reduction of camphor
7.5
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oxidation of borneol
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22
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assay at room temperature
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4.8
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calculated fromn sequence
5.4
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calculated from sequence
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gene LiBDH
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brenda
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brenda
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brenda
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brenda
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brenda
isolated from soil samples collected in Hualien County, Taiwan
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brenda
isoform BDH1, cf. EC 1.1.1.198
UniProt
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
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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
additional information
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molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH
physiological function
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neither wild-tpe nor a gene deletion mutant is able to grow on (-)-borneol or (-)-camphor as sole carbon source. Both strains grow similarly on (+)-borneol or (+)-camphor
physiological function
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neither wild-tpe nor a gene deletion mutant is able to grow on (-)-borneol or (-)-camphor as sole carbon source. Both strains grow similarly on (+)-borneol or (+)-camphor
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A0A1B3EB36_9PSED
260
0
27607
TrEMBL
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27500
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x * 27500, about, sequence calculation
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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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x * 27500, about, sequence calculation
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x * 30000, SDS-PAGE, x * 27400, calculated from sequence
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x * 30000, SDS-PAGE, x * 27400, calculated from sequence
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x * 27500, calculated from sequence, x * 31000, SDS-PAGE
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x * 27500, calculated from sequence, x * 31000, SDS-PAGE
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x * 30000-40000, recombinant enzyme, SDS-PAGE
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Y188A
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mutant catalyzes stereoselective reduction of racemic camphor with 23% conversion and 99% enantiomeric excess
Y188T
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mutant catalyzes stereoselective reduction of racemic camphor with 22% conversion and 99% enantiomeric excess
Y188A
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mutant catalyzes stereoselective reduction of racemic camphor with 23% conversion and 99% enantiomeric excess
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Y188T
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mutant catalyzes stereoselective reduction of racemic camphor with 22% conversion and 99% enantiomeric excess
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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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partial, using Phenyl-Sepharose hydrophobic interaction, Q-Sepharose Fast Flow and Mono-Q anion-exchange columns
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production of enzyme in the form of inclusion body in Escherichia coli. The refolded BDH1 tends to precipitate. Insoluble recombinant BDH1 is converted into a soluble form by adding glycerol in LB medium
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3)pLysSby nickel affinity chromatography
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expression in Escherichia coli
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
synthesis
production of enzyme in the form of inclusion body in Escherichia coli. The refolded BDH1 tends to precipitate. Insoluble recombinant BDH1 is converted into a soluble form by adding glycerol in LB medium
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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.
brenda
Hofer, M.; Diener, J.; Begander, B.; Kourist, R.; Sieber, V.
Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor
Appl. Microbiol. Biotechnol.
105
3159-3167
2021
Pseudomonas putida, Pseudomonas putida ATCC 17453
brenda
Khine, A.; Yang, M.; Hu, A.; Lin, G.; Toh, Y.; Chen, H.
Production of optically pure (-)-borneol by Pseudomonas monteilii TCU-CK1 and characterization of borneol dehydrogenase involved
Enzyme Microb. Technol.
139
109586
2020
Pseudomonas monteilii, Pseudomonas monteilii TCU-CK1
brenda
Khine, A.A.; Lu, P.C.; Ko, T.P.; Huang, K.F.; Chen, H.P.
Cloning, expression, identification and characterization of borneol dehydrogenase isozymes in Pseudomonas sp. TCU-HL1
Protein Expr. Purif.
175
105715
2020
Pseudomonas sp. TCU-HL1 (A0A1B3EB36)
brenda
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