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Enzyme Nomenclature
Information on EC 1.1.1.198 - (+)-borneol dehydrogenase
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1.1.1.198 (+)-borneol dehydrogenaseIUBMB Comments
NADP+ can also act, but more slowly.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH2
BDH
THL1_4180
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
(+)-borneol:NAD+ oxidoreductase
NADP+ can also act, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
67185-75-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-dihydrocarveol + NAD+
(-)-dihydrocarvone + NADH
-
poor substrate
-
?
(+)-endo-fenchol + NAD+
1,3,3-trimethyl-bicyclo[2.2.1]heptan-2-one + NADH
-
26% of the activity compared to (+)-borneol
-
?
(+)-isoborneol + NAD+
(+)-isocamphor + NADH
-
nearly the same activity compared to (+)-borneol
-
?
(-)-borneol + NAD+
(-)-camphor + NADH
-
36% of the activity compared to (+)-borneol
-
?
(-)-endo-fenchol + NAD+
1,3,3-trimethyl-bicyclo[2.2.1]heptan-2-one + NADH
-
poor substrate
-
?
(-)-isoborneol + NAD+
(-)-isocamphor + NADH
-
30% of the activity compared to (+)-borneol
-
?
(-)-neothujol + NAD+
(-)-neothujone + NADH
-
65% of the activity compared to (+)-borneol
-
?
(-)-thujol + NAD+
(-)-thujone + NADH
-
2fold higher activity than for (+)-borneol
-
?
(1R)-menthol + NAD+
(1R)-trans-p-menthan-3-one + NADH
-
poor substrate
-
?
(+)-borneol + NAD+
(+)-camphor + NADH
-
B-site stereospecific, partially reversible
-
r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
camphor is the only product
ir
(+)-borneol + NAD+
(+)-camphor + NADH + H+
stereospecific reaction
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
stereospecific reaction
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
GC-MS analysis of borneol degradation metabolites
-
?
additional information
?
-
the enzyme is also active with (-)-borneol, reaction of EC 1.1.1.227
-
?
additional information
?
-
GC-MS analysis of borneol degradation metabolites
-
?
additional information
?
-
the enzyme is also active with (-)-borneol, reaction of EC 1.1.1.227
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-borneol + NAD+
(+)-camphor + NADH
-
B-site stereospecific, partially reversible
-
r
additional information
?
-
GC-MS analysis of borneol degradation metabolites
-
-
?
additional information
?
-
GC-MS analysis of borneol degradation metabolites
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
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
an N-terminal conserved Gly13-X-X-X-Gly17-X-Gly19 sequence motif is present in the NAD(H)-binding region
-
additional information
enzyme AaBDH is active in the presence of cofactor NADP+ or NAD+, NAD+ is the preferred cofactor
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
transcripts are specifically expressed in glandular trichomes of mature flowers
brenda
additional information
-
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
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
-
strain TCU-HL1 is able to use borneol as the sole carbon source
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
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
-
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
additional information
enzyme three-dimensional structural modelling, and docking analysis, overview
additional information
-
enzyme three-dimensional structural modelling, and docking analysis, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). I3SBG4_MEDTR
271
0
28617
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6QKU7_ROSCH
95
0
9656
TrEMBL
other Location (Reliability: 5)
A0A2P6QE87_ROSCH
233
0
24606
TrEMBL
other Location (Reliability: 4)
A0A396I496_MEDTR
271
0
28695
TrEMBL
Mitochondrion (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
1 * 30000-40000, SDS-PAGE, 1 * 27600, about, sequence calculation, x * 30000-40000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 30000-40000, SDS-PAGE, 1 * 27600, about, sequence calculation, x * 30000-40000, recombinant enzyme, SDS-PAGE
additional information
enzyme three-dimensional structural molecular modeling and docking
additional information
-
enzyme three-dimensional structural molecular modeling and docking
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
-
brenda
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