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Information on EC 1.1.1.198 - (+)-borneol dehydrogenase for references in articles please use BRENDA:EC1.1.1.198
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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
AaBDH, ADH2,
BDH , bicyclic monoterpenol dehydrogenase,
THL1_4180 ,
more
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bicyclic monoterpenol dehydrogenase
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ADH2
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BDH
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THL1_4180
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(+)-borneol + NAD+ = (+)-camphor + NADH + H+
NADP+ can also act, but more slowly
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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+
(+)-borneol + NADP+
(+)-camphor + NADPH + H+
(+)-dihydrocarveol + NAD+
(-)-dihydrocarvone + NADH
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poor substrate
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?
(+)-endo-fenchol + NAD+
1,3,3-trimethyl-bicyclo[2.2.1]heptan-2-one + NADH
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26% of the activity compared to (+)-borneol
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?
(+)-isoborneol + NAD+
(+)-isocamphor + NADH
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nearly the same activity compared to (+)-borneol
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?
(-)-artemisia alcohol + NAD+
artemisia ketone + NADH + H+
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?
(-)-borneol + NAD+
(+)-camphor + NADH + H+
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?
(-)-borneol + NAD+
(-)-camphor + NADH
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36% of the activity compared to (+)-borneol
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?
(-)-cis-carveol + NAD+
(-)-carvone + NADH + H+
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-
?
(-)-endo-fenchol + NAD+
1,3,3-trimethyl-bicyclo[2.2.1]heptan-2-one + NADH
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poor substrate
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?
(-)-isoborneol + NAD+
(-)-isocamphor + NADH
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30% of the activity compared to (+)-borneol
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?
(-)-neothujol + NAD+
(-)-neothujone + NADH
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65% of the activity compared to (+)-borneol
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?
(-)-thujol + NAD+
(-)-thujone + NADH
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2fold higher activity than for (+)-borneol
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?
(-)-trans-carveol + NAD+
(-)-carvone + NADH + H+
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-
-
?
(-)-trans-pinocarveol + NAD+
(-)-pinocarvone + NADH + H+
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-
-
?
(1R)-menthol + NAD+
(1R)-trans-p-menthan-3-one + NADH
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poor substrate
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?
geraniol + NAD+
geranial + NADH
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poor substrate
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?
nerol + NAD+
neryl aldehyde + NADH
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poor substrate
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?
additional information
?
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(+)-borneol + NAD+
(+)-camphor + NADH
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?
(+)-borneol + NAD+
(+)-camphor + NADH
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B-site stereospecific, partially reversible
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r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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-
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?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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camphor is the only product
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ir
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
stereospecific reaction
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?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
stereospecific reaction
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?
(+)-borneol + NADP+
(+)-camphor + NADPH + H+
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r
(+)-borneol + NADP+
(+)-camphor + NADPH + H+
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r
(+)-borneol + NADP+
(+)-camphor + NADPH + H+
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r
additional information
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no substrates: citronellol, lavandulol, myrtenol, and (S)-(-)-perillyl alcohol, artemisinic alcohol, farnesol, khusinol, and santalol, secoisolariciresinol, larixol, phytol, retinol, benzyl alcohol, cinnamyl alcohol, 2-cyclohexen-1-ol, and 3-methyl-2-buten-1-ol
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additional information
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substrate specificity, overview. No activity with other monoterpene alcohol, several kinds of monoterpene alcohols including (-)-artemisia alcohol, cis-carveol, trans-carveol, and trans-pinocarveol. The enzyme is specific for (+)-borneol
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additional information
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no substrate: 1,8-cineole, citronellol, linalool, lavandulol, nerol, geraniol, perillyl alcohol, and farnesol. The reverse reduction assay in which camphor is used as a substrate and NADH as a cofactor, does not produce detectable amounts of borneol or other products
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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 1.1.1.227
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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 1.1.1.227
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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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B-site stereospecific, partially reversible
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r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
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r
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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NAD+
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NAD+
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+. NAD+ docking into the active site of the BDH homology model for binding domain and mode analysis
NADP+
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65-85% as efficient as NAD+
NADP+
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25% as efficient as NAD+
NADP+
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
no cofactor: NADP+
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additional information
no cofactor: NADP+
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additional information
an N-terminal conserved Gly13-X-X-X-Gly17-X-Gly19 sequence motif is present in the NAD(H)-binding region
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additional information
enzyme AaBDH is active in the presence of cofactor NADP+ or NAD+, NAD+ is the preferred cofactor
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(+)-Camphor
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27% inhibition at 0.5 mM
(-)-Thujol
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competitive inhibition of (+)-borneol oxidation
8-hydroxyquinoline
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57% inhibition at 1 mM
Borate
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inhibition of borneol oxidation
Cu2+
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85% inhibition at 2 mM
ethylenediaminetetraacetate
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slight inhibition at 1 mM
Hg2+
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nearly complete inhibition at 2 mM
iodoacetamide
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41% inhibition at 1 mM
N-ethylmaleimide
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53% inhibition at 1 mM
NaCN
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slight inhibition at 1 mM
NADH
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46% inhibition at 1 mM
NaN3
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slight inhibition at 1 mM
o-phenanthroline
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slight inhibition at 1 mM
p-hydroxymercuribenzoate
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50% inhibition at 0.05 mM
Pb2+
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26% inhibition at 2 mM
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0.086
(-)-artemisia alcohol
pH 9.5, 30°C
0.027
(-)-cis-carveol
pH 9.5, 30°C
additional information
additional information
Michaelis-Menten kinetics
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0.03
(+)-borneol
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0.0483
(+)-borneol
pH 9.0, 33°C, recombinant enzyme
0.053
(+)-borneol
pH 8.0, 32°C
0.2
(+)-borneol
recombinant enzyme, pH 8.5, 22°C
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0.0004 - 0.75
(+)-borneol
0.0004
(+)-borneol
pH 8.0, 32°C
0.0058
(+)-borneol
pH 9.0, 33°C, recombinant enzyme
0.75
(+)-borneol
recombinant enzyme, pH 8.5, 22°C
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10.33
substrate (-)-trans-pinocarveol, pH 9.5, 30°C
13.5
substrate (-)-trans-carveol, pH 9.5, 30°C
147.4
substrate (-)-cis-carveol, pH 9.5, 30°C
2.17
substrate (-)-borneol, pH 9.5, 30°C
35.7
substrate (-)-artemisia alcohol, pH 9.5, 30°C
5.33
substrate (+)-borneol, pH 9.5, 30°C
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22
assay at room temperature
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5.66
sequence calculation
6.16
sequence calculation
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UniProt
brenda
a borneol-degrading strain, isolated from soil samples collected in Hualien County, Taiwan
UniProt
brenda
a borneol-degrading strain, isolated from soil samples collected in Hualien County, Taiwan
UniProt
brenda
sage
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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transcripts are specifically expressed in glandular trichomes of mature flowers
brenda
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brenda
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ADH2 gene is highly expressed in old leaves, whereas the artemisinin biosynthetic genes are mainly expressed in bud and young leaves. The expression of ADH2 gene increases quickly during leaf development. ADH2 expression is exclusively located to T-shaped trichome, not glandular secretory trichome
brenda
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brenda
high expression in glandular trichome
brenda
transcripts are specifically expressed in glandular trichomes of mature flowers
brenda
additional information
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
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brenda
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evolution
BDH is a member of the NAD+-dependent dehydrogenases
evolution
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BDH is a member of the NAD+-dependent dehydrogenases
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metabolism
the enzyme from the soil microorganism is involved in degradation of borneol through a camphor degradation pathway, pathway overview. 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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the enzyme from the soil microorganism is involved in degradation of borneol through a camphor degradation pathway, pathway overview. 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
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additional information
enzyme three-dimensional structural modelling, and docking analysis, overview
additional information
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enzyme three-dimensional structural modelling, and docking analysis, overview
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I3SBG4_MEDTR
271
0
28617
TrEMBL
A0A2P6QKU7_ROSCH
95
0
9656
TrEMBL
A0A2P6QE87_ROSCH
233
0
24606
TrEMBL
A0A396I496_MEDTR
271
0
28695
TrEMBL
A0A191ZDL6_ARTAN
294
0
31043
TrEMBL
A0A1B3EB36_9PSED
260
0
27607
TrEMBL
E5DD06_ARTAN
265
0
28128
TrEMBL
K4N0V2_9LAMI
259
0
27270
TrEMBL
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27500
x * 27500, calculated
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?
x * 31040, sequence calculation
monomer
1 * 30000-40000, SDS-PAGE, 1 * 27600, about, sequence calculation, x * 30000-40000, recombinant enzyme, SDS-PAGE
monomer
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1 * 30000-40000, SDS-PAGE, 1 * 27600, about, sequence calculation, x * 30000-40000, recombinant enzyme, SDS-PAGE
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additional information
enzyme three-dimensional structural molecular modeling and docking
additional information
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enzyme three-dimensional structural molecular modeling and docking
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8
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most stable around
286163
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0°C, 0.1 M sodium phosphate, pH 8.0, 15% glycerol, 20 mM 2-mercaptoethanol, 3 days, 25% loss of activity
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near homogeneity, chromatography techniques, affinity chromatography
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recombinant enzyme refolded from inclusion bodies after expression in Escherichia coli strain BL21 by anion exchange chromatography and dialysis for refolding, native enzyme from strain TCU-HL1 by hydrophobic interaction and anion exchange chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and desalting gel filtration
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expression in Escherichia coli
gene bdh, DNA and amino acid sequence determination and analysis, library construction of genes involved in camphor biosynthesis from different cultivars, sequence comparisons, phylogenetic tree of plant alcohol dehydrogenase, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), semi-quantitative RT-PCR enzyme expression analysis
gene bdh, DNA and amino acid sequence determination and analysis, recombinnat expression in inclusion bodies in Escherichia coli strain BL21
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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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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
Salvia officinalis
brenda
Croteau, R.; Hooper, C.L.; Felton, M.
Biosynthesis of monoterpenes. Partial purification and characterization of a bicyclic monoterpenol dehydrogenase from sage (Salvia officinalis)
Arch. Biochem. Biophys.
188
182-193
1978
Salvia officinalis
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 (K4N0V2)
brenda
Polichuk, D.R.; Zhang, Y.; Reed, D.W.; Schmidt, J.F.; Covello, P.S.
A glandular trichome-specific monoterpene alcohol dehydrogenase from Artemisia annua
Phytochemistry
71
1264-1269
2010
Artemisia annua (E5DD06)
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. (A0A1B3EB36), Pseudomonas sp. TCU-HL1 (A0A1B3EB36)
brenda
Fu, X.; Shi, P.; Shen, Q.; Jiang, W.; Tang, Y.; Lv, Z.; Yan, T.; Li, L.; Wang, G.; Sun, X.; Tang, K.
T-shaped trichome-specific expression of monoterpene synthase ADH2 using promoter-beta-GUS fusion in transgenic Artemisia annua L
Biotechnol. Appl. Biochem.
63
834-840
2016
Artemisia annua
brenda
Tian, N.; Tang, Y.; Xiong, S.; Tian, D.; Chen, Y.; Wu, D.; Liu, Z.; Liu, S.
Molecular cloning and functional identification of a novel borneol dehydrogenase from Artemisia annua L.
Ind. Crops Prod.
77
190-195
2015
Artemisia annua (A0A191ZDL6)
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brenda
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