Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+)-borneol + (-)-isoborneol + NAD+
(+)-camphor + (-)-isoborneol + NADH + H+
-
the reaction is catalyzed by isoform BDH1
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH
(+)-borneol + NAD+
(+)-camphor + NADH + H+
(+)-borneol + NADP+
(+)-camphor + NADPH + H+
(+)-camphor + NADH + H+
(+)-borneol + NAD+
(+)-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
-
?
(+)-endo-norborneol + NAD+
(-)-exonorcamphor + NADH + H+
(+)-fenchol + NAD+
(-)-fenchone + NADH + H+
(+)-isoborneol + NAD+
(+)-isocamphor + NADH
-
nearly the same activity compared to (+)-borneol
-
?
(+)-isoborneol + NAD+
(+)-isocamphor + NADH + H+
(+)-isoborneol + NAD+
(-)-camphor + NADH + H+
(+/-)-borneol + NAD+
(+/-)-camphor + NADH + H+
(+/-)-isoborneol + NAD+
(-)-camphor + NADH + H+
(+/-)-isoborneol + NADH + H+
?
-
-
-
-
?
(-)-artemisia alcohol + NAD+
artemisia ketone + NADH + H+
-
-
-
?
(-)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
(-)-cis-carveol + NAD+
(-)-carvone + NADH + H+
(-)-endo-fenchol + NAD+
1,3,3-trimethyl-bicyclo[2.2.1]heptan-2-one + NADH
-
poor substrate
-
?
(-)-exo-norborneol + NAD+
(+)-exonorcamphor + NADH + H+
(-)-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
-
?
(-)-trans-carveol + NAD+
(-)-carvone + NADH + H+
-
-
-
?
(-)-trans-pinocarveol + NAD+
(-)-pinocarvone + NADH + H+
-
-
-
?
(1R)-(+)-camphor + (1S)-(-)-camphor + NADH + H+
(+)-borneol + (1S)-(-)-camphor + NAD+
-
-
-
-
?
(1R)-menthol + NAD+
(1R)-trans-p-menthan-3-one + NADH
-
poor substrate
-
?
2-hydroxyheptanol + NAD+
2-oxoheptanol + NADH + H+
-
-
-
-
?
2-methyl cyclohexanol + NAD+
?
2-methylcyclohexanol + NAD+
2-methylcyclohexanone + NADH + H+
-
-
-
-
?
3-hydroxyoctanol + NAD+
3-oxooctanol + NADH + H+
-
-
-
-
?
3-methyl cyclohexanol + NAD+
3-methycyclohexanone + NADH + H+
-
-
-
-
?
3-methyl cyclohexanol + NAD+
?
4-methyl cyclohexanol + NAD+
?
geraniol + NAD+
geranial + NADH + H+
-
poor substrate
-
?
nerol + NAD+
neryl aldehyde + NADH
-
poor substrate
-
?
additional information
?
-
(+)-borneol + NAD+
(+)-camphor + NADH
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH
-
B-site stereospecific, partially reversible
-
r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
camphor is the only product
-
ir
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
(+)-borneol is the preferred substrate
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
(+)-borneol is the preferred substrate
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
stereospecific reaction
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
r
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
the enzyme prefers to degrade (+)-borneol, rather than (-)-borneol
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
the reaction is catalyzed by isoform BDH2
-
-
?
(+)-borneol + NAD+
(+)-camphor + NADH + H+
-
-
-
-
?
(+)-borneol + NADP+
(+)-camphor + NADPH + H+
-
-
-
r
(+)-borneol + NADP+
(+)-camphor + NADPH + H+
-
-
-
r
(+)-camphor + NADH + H+
(+)-borneol + NAD+
-
-
-
-
r
(+)-camphor + NADH + H+
(+)-borneol + NAD+
-
-
-
-
r
(+)-camphor + NADH + H+
(+)-borneol + NAD+
-
-
-
-
r
(+)-endo-norborneol + NAD+
(-)-exonorcamphor + NADH + H+
-
-
-
-
?
(+)-endo-norborneol + NAD+
(-)-exonorcamphor + NADH + H+
-
-
-
-
?
(+)-fenchol + NAD+
(-)-fenchone + NADH + H+
-
-
-
-
?
(+)-fenchol + NAD+
(-)-fenchone + NADH + H+
-
-
-
-
?
(+)-isoborneol + NAD+
(+)-isocamphor + NADH + H+
-
-
-
-
?
(+)-isoborneol + NAD+
(+)-isocamphor + NADH + H+
-
-
-
-
?
(+)-isoborneol + NAD+
(-)-camphor + NADH + H+
-
-
-
-
?
(+)-isoborneol + NAD+
(-)-camphor + NADH + H+
-
-
-
-
?
(+/-)-borneol + NAD+
(+/-)-camphor + NADH + H+
-
-
-
-
?
(+/-)-borneol + NAD+
(+/-)-camphor + NADH + H+
-
-
-
-
?
(+/-)-isoborneol + NAD+
(-)-camphor + NADH + H+
-
-
-
-
?
(+/-)-isoborneol + NAD+
(-)-camphor + NADH + H+
-
the reaction is catalyzed by isoform BDH2
-
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
-
-
-
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
-
-
-
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
-
-
-
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
-
-
-
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
-
-
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
-
36% of the activity compared to (+)-borneol
-
?
(-)-borneol + NAD+
(-)-camphor + NADH + H+
-
the reaction is catalyzed by isoform BDH2
-
-
?
(-)-carveol + NAD+
?
-
-
-
-
?
(-)-carveol + NAD+
?
-
-
-
-
?
(-)-cis-carveol + NAD+
(-)-carvone + NADH + H+
-
-
-
?
(-)-cis-carveol + NAD+
(-)-carvone + NADH + H+
-
-
-
-
?
(-)-exo-norborneol + NAD+
(+)-exonorcamphor + NADH + H+
-
-
-
-
?
(-)-exo-norborneol + NAD+
(+)-exonorcamphor + NADH + H+
-
-
-
-
?
2-methyl cyclohexanol + NAD+
?
-
-
-
-
?
2-methyl cyclohexanol + NAD+
?
-
-
-
-
?
3-methyl cyclohexanol + NAD+
?
-
-
-
-
?
3-methyl cyclohexanol + NAD+
?
-
-
-
-
?
4-methyl cyclohexanol + NAD+
?
-
-
-
-
?
4-methyl cyclohexanol + NAD+
?
-
-
-
-
?
cyclohexanol + NAD+
?
-
-
-
-
?
cyclohexanol + NAD+
?
-
-
-
-
?
heptan-2-ol + NAD+
?
-
-
-
-
?
heptan-2-ol + NAD+
?
-
-
-
-
?
octan-3-ol + NAD+
?
-
-
-
-
?
octan-3-ol + NAD+
?
-
-
-
-
?
propan-1-ol + NAD+
?
-
-
-
-
?
propan-1-ol + NAD+
?
-
-
-
-
?
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
?
-
-
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
?
-
-
(-)-borneol is an additional substrate, reaction of EC 1.1.1.227. (+)-Borneol is the preferred substrate
-
-
-
additional information
?
-
-
the recombinant enzyme does not use isopropanol, cyclohexanol, cyclopentanol, or(+/-)-2-butanol as alternative substrates, and NADP+ as a cofactor
-
-
-
additional information
?
-
-
(-)-borneol is an additional substrate, reaction of EC 1.1.1.227. (+)-Borneol is the preferred substrate
-
-
-
additional information
?
-
-
the recombinant enzyme does not use isopropanol, cyclohexanol, cyclopentanol, or(+/-)-2-butanol as alternative substrates, and NADP+ as a cofactor
-
-
-
additional information
?
-
-
enzyme also catalyzes the reaction of (-)-borneol and (-)-camphor, reaction of EC 1.1.1.227. No substrates: isopropanol, cyclopentanol, cyclohexanol, 1,2-butandiol, 2-butanol, L-carveol, and DL-menthol
-
-
-
additional information
?
-
-
enzyme also catalyzes the reaction of (-)-borneol and (-)-camphor, reaction of EC 1.1.1.227. No substrates: isopropanol, cyclopentanol, cyclohexanol, 1,2-butandiol, 2-butanol, L-carveol, and DL-menthol
-
-
-
additional information
?
-
GC-MS analysis of borneol degradation metabolites
-
-
?
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
?
-
-
the enzyme is also active with (-)-borneol, reaction of EC 1.1.1.227
-
-
?
additional information
?
-
-
isopropanol, cyclopentanol, cyclohexanol, 1,2-butandiol, (+/-)-2-butanol, L-carveol, and DL-menthol are not accepted as substrates
-
-
-
additional information
?
-
-
enzyme additionally catalyzes the reaction with (-)-borneol, reaction of EC 1.1.1.227. (+)-Borneol is the preferred substrate
-
-
-
additional information
?
-
enzyme additionally catalyzes the reaction with (-)-borneol, reaction of EC 1.1.1.227. (+)-Borneol is the preferred substrate
-
-
-
additional information
?
-
-
no activity with menthol
-
-
-
additional information
?
-
-
isoforms BDH1 and BDH2 also accept monocyclic and linear substrates, clearly favoring secondary alcohols over primary alcohols. No substrate: menthol
-
-
-
additional information
?
-
-
no activity with menthol
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0251 - 0.46
(+)-borneol
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
-
0.0251
(+)-borneol
-
isoform BDH3, at pH 8.5 and 30°C
0.0483
(+)-borneol
pH 9.0, 33°C, recombinant enzyme
0.053
(+)-borneol
pH 8.0, 32°C
0.07
(+)-borneol
isoform BDH2, at pH 7.0, temperature not specified in the publication
0.09
(+)-borneol
soluble isoform BDH1, at pH 7.0, temperature not specified in the publication
0.09
(+)-borneol
soluble recombinant protein, pH 7, 25°C
0.095
(+)-borneol
-
wild-type, pH 7.5, 30°C
0.095
(+)-borneol
-
wild type enzyme, at pH 7.5 and 30°C
0.12
(+)-borneol
refolded isoform BDH1, at pH 7.0, temperature not specified in the publication
0.12
(+)-borneol
refolded recombinant protein, pH 7, 25°C
0.13
(+)-borneol
-
at pH 11.0 and 25°C
0.13
(+)-borneol
-
pH 11, 25°C
0.14
(+)-borneol
-
pH 7, 25°C
0.14
(+)-borneol
-
at pH 7.0 and 25°C
0.16
(+)-borneol
-
isoform BDH2, at pH 8.0 and 20°C
0.2
(+)-borneol
recombinant enzyme, pH 8.5, 22°C
0.28
(+)-borneol
-
mutant enzyme S146A/Y188A, at pH 7.5 and 30°C
0.28
(+)-borneol
-
mutant Y188A, pH 7.5, 30°C
0.46
(+)-borneol
-
mutant enzyme S146A/Y188T, at pH 7.5 and 30°C
0.46
(+)-borneol
-
mutant Y188T, pH 7.5, 30°C
0.0369
(-)-borneol
-
isoform BDH3, at pH 9.0 and 32°C
0.115
(-)-borneol
-
wild type enzyme, at pH 7.5 and 30°C
0.12
(-)-borneol
refolded isoform BDH1, at pH 7.0, temperature not specified in the publication
0.21
(-)-borneol
soluble isoform BDH1, at pH 7.0, temperature not specified in the publication
0.34
(-)-borneol
-
mutant enzyme S146A/Y188A, at pH 7.5 and 30°C
0.64
(-)-borneol
-
at pH 7.0 and 25°C
0.73
(-)-borneol
-
mutant enzyme S146A/Y188T, at pH 7.5 and 30°C
0.85
(-)-borneol
-
at pH 11.0 and 25°C
1.5
(-)-borneol
isoform BDH2, at pH 7.0, temperature not specified in the publication
0.006
NAD+
-
wild type enzyme, at pH 7.5 and 30°C
0.048
NAD+
-
isoform BDH2, at pH 8.0 and 20°C
0.06
NAD+
-
wild-type, pH 7.5, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0021 - 29.4
(-)-borneol
0.0004
(+)-borneol
pH 8.0, 32°C
0.005
(+)-borneol
-
isoform BDH2, at pH 8.0 and 20°C
0.0054
(+)-borneol
-
isoform BDH3, at pH 8.5 and 30°C
0.0058
(+)-borneol
pH 9.0, 33°C, recombinant enzyme
0.5
(+)-borneol
refolded isoform BDH1, at pH 7.0, temperature not specified in the publication
0.5
(+)-borneol
refolded recombinant protein, pH 7, 25°C
0.75
(+)-borneol
recombinant enzyme, pH 8.5, 22°C
0.89
(+)-borneol
-
wild-type, pH 7.5, 30°C
0.89
(+)-borneol
-
at pH 7.5 and 30°C
1.51
(+)-borneol
-
mutant enzyme S146A/Y188A, at pH 7.5 and 30°C
1.51
(+)-borneol
-
mutant Y188A, pH 7.5, 30°C
3.32
(+)-borneol
-
mutant enzyme S146A/Y188T, at pH 7.5 and 30°C
3.32
(+)-borneol
-
mutant Y188T, pH 7.5, 30°C
17
(+)-borneol
soluble isoform BDH1, at pH 7.0, temperature not specified in the publication
17
(+)-borneol
soluble recombinant protein, pH 7, 25°C
27.8
(+)-borneol
isoform BDH2, at pH 7.0, temperature not specified in the publication
75
(+)-borneol
-
pH 7, 25°C
75
(+)-borneol
-
at pH 7.0 and 25°C
209
(+)-borneol
-
at pH 11.0 and 25°C
209
(+)-borneol
-
pH 11, 25°C
0.0021
(-)-borneol
-
isoform BDH3, at pH 9.0 and 32°C
0.07
(-)-borneol
-
mutant enzyme S146A/Y188A, at pH 7.5 and 30°C
0.13
(-)-borneol
-
mutant enzyme S146A/Y188T, at pH 7.5 and 30°C
0.38
(-)-borneol
refolded isoform BDH1, at pH 7.0, temperature not specified in the publication
0.97
(-)-borneol
-
at pH 7.5 and 30°C
11.3
(-)-borneol
-
at pH 7.0 and 25°C
12.4
(-)-borneol
soluble isoform BDH1, at pH 7.0, temperature not specified in the publication
18.5
(-)-borneol
isoform BDH2, at pH 7.0, temperature not specified in the publication
29.4
(-)-borneol
-
at pH 11.0 and 25°C
0.0049
NAD+
-
isoform BDH2, at pH 8.0 and 20°C
0.006
NAD+
-
at pH 7.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0029
-
with (-)-carveol as substrate, at pH 7.5 and 25°C
0.0032
-
with propan-1-ol as substrate, at pH 7.5 and 25°C
0.0039
-
with (+)-endo-norborneol as substrate, at pH 7.5 and 25°C
0.0044
-
with 3-methyl cyclohexanol as substrate, at pH 7.5 and 25°C
0.0046
-
with (+)-fenchol as substrate, at pH 7.5 and 25°C
0.0048
-
with (-)-exo-norborneol as substrate, at pH 7.5 and 25°C
0.005
-
with (-)-carveol as substrate, at pH 7.5 and 25°C
0.0062
-
with heptan-2-ol as substrate, at pH 7.5 and 25°C
0.0083
-
with 4-methyl cyclohexanol as substrate, at pH 7.5 and 25°C
0.0098
-
with heptan-2-ol as substrate, at pH 7.5 and 25°C
0.01
-
with 2-methyl cyclohexanol as substrate, at pH 7.5 and 25°C
0.011
-
with 4-methyl cyclohexanol as substrate, at pH 7.5 and 25°C
0.013
-
with octan-3-ol as substrate, at pH 7.5 and 25°C
0.018
-
with 3-methyl cyclohexanol as substrate, at pH 7.5 and 25°C
0.023
-
with 2-methyl cyclohexanol as substrate, at pH 7.5 and 25°C
0.024
-
with (+)-isoborneol as substrate, at pH 7.5 and 25°C
0.043
-
with octan-3-ol as substrate, at pH 7.5 and 25°C
0.069
-
with (-)-exo-norborneol as substrate, at pH 7.5 and 25°C
0.115
-
with (+)-isoborneol as substrate, at pH 7.5 and 25°C
0.122
-
with (+/-)-borneol as substrate, at pH 7.5 and 25°C
10.33
substrate (-)-trans-pinocarveol, pH 9.5, 30°C
13
-
isoform BDH1, substrate 6-hydroxyoctanol, pH 9, temperature not specified in the publication
13.5
substrate (-)-trans-carveol, pH 9.5, 30°C
147.4
substrate (-)-cis-carveol, pH 9.5, 30°C
16
-
isoform BDH2, substrate (-)-carveol, pH 9, temperature not specified in the publication
2.17
substrate (-)-borneol, pH 9.5, 30°C
24
-
isoform BDH1, substrate isoborneol, pH 9, temperature not specified in the publication
30
-
isoform BDH1, substrate rac-borneol, pH 9, temperature not specified in the publication
35.7
substrate (-)-artemisia alcohol, pH 9.5, 30°C
5.33
substrate (+)-borneol, pH 9.5, 30°C
9.8
-
isoform BDH1, substrate 2-hydroxyheptanol, pH 9, temperature not specified in the publication
0.0033
-
with cyclohexanol as substrate, at pH 7.5 and 25°C
0.0033
-
with propan-1-ol as substrate, at pH 7.5 and 25°C
0.028
-
with (+)-endo-norborneol as substrate, at pH 7.5 and 25°C
0.028
-
with cyclohexanol as substrate, at pH 7.5 and 25°C
0.03
-
with (+)-fenchol as substrate, at pH 7.5 and 25°C
0.03
-
with (+/-)-borneol as substrate, at pH 7.5 and 25°C
10
-
isoform BDH1, substrate 2-methylcyclohexanol, pH 9, temperature not specified in the publication
10
-
isoform BDH2, substrate rac-borneol, pH 9, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
1 * 30000-40000, SDS-PAGE, 1 * 27600, about, sequence calculation, x * 30000-40000, recombinant enzyme, SDS-PAGE
?
x * 31040, sequence calculation
?
-
x * 27400, calculated from amino acid sequence
?
-
x * 30000, SDS-PAGE, x * 27400, calculated from sequence
?
-
x * 30000, SDS-PAGE
-
?
-
x * 27400, calculated from amino acid sequence
-
?
-
x * 30000, SDS-PAGE, x * 27400, calculated from sequence
-
?
-
x * 27500, calculated from sequence, x * 31000, SDS-PAGE
?
-
x * 27500, calculated from sequence, x * 31000, SDS-PAGE
-
?
-
x * 27500, calculated from amino acid sequence
?
x * about 30000, isoform BDH1, SDS-PAGE
?
x * about 35000, isoform BDH2, SDS-PAGE
additional information
enzyme three-dimensional structural molecular modeling and docking
additional information
-
enzyme three-dimensional structural molecular modeling and docking
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Y188A
-
mutant catalyzes stereoselective reduction of racemic camphor with 23% conversion and 99% enantiomeric excess
Y188T
-
mutant catalyzes stereoselective reduction of racemic camphor with 22% conversion and 99% enantiomeric excess
Y188A
-
mutant catalyzes stereoselective reduction of racemic camphor with 23% conversion and 99% enantiomeric excess
-
Y188T
-
mutant catalyzes stereoselective reduction of racemic camphor with 22% conversion and 99% enantiomeric excess
-
E145G
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
E145L/Y188A
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
E145M/Y188A
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
E145M/Y188T
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
E145S/Y188A
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
E145S/Y188T
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
S145H
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
S145L
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
S145M
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
S145S
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
S146A
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
S146A/Y188A
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
S146A/Y188T
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
Y188A
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
Y188I
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
Y188L
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
Y188T
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
Y188V
-
the mutant shows a significant increase in (+)-camphor selectivity compared to the wild type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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), Lavandula x intermedia
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.
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
Khine, A.; Chen, H.; Huang, K.; Ko, T.
Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1
Acta Crystallogr. Sect. F
76
309-313
2020
Pseudomonas sp. TCU-HL1 (A0A1B3EB36)
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 sp. ATCC 17453, Pseudomonas putida ATCC 17453
brenda
Chanique, A.; Dimos, N.; Drienovska, I.; Calderini, E.; Pantin, M.; Helmer, C.; Hofer, M.; Sieber, V.; Parra, L.; Loll, B.; Kourist, R.
A structural view on the stereospecificity of plant borneol-type dehydrogenases
ChemCatChem
13
2262-2277
2021
Salvia officinalis, Salvia rosmarinus, Pseudomonas sp. TCU-HL1
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
Drienovska, I.; Kolanovic, D.; Chanique, A.; Sieber, V.; Hofer, M.; Kourist, R.
Molecular cloning and functional characterization of a two highly stereoselective borneol dehydrogenases from Salvia officinalis L
Phytochemistry
172
112227
2020
Salvia officinalis
-
brenda
Ma, R.; Su, P.; Jin, B.; Guo, J.; Tian, M.; Mao, L.; Tang, J.; Chen, T.; Lai, C.; Zeng, W.; Cui, G.; Huang, L.
Molecular cloning and functional identification of a high-efficiency (+)-borneol dehydrogenase from Cinnamomum camphora (L.) Presl
Plant Physiol. Biochem.
158
363-371
2021
Cinnamomum camphora
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, Pseudomonas sp. TCU-HL1 (A0A1B3EB36)
brenda