Enzymes
UniProtKB help_outline | 2 proteins |
Enzyme class help_outline |
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- Name help_outline (1R,2S,4R)-borneol Identifier CHEBI:15393 (Beilstein: 2038056; CAS: 464-43-7) help_outline Charge 0 Formula C10H18O InChIKeyhelp_outline DTGKSKDOIYIVQL-WEDXCCLWSA-N SMILEShelp_outline CC1(C)[C@@H]2CC[C@@]1(C)[C@@H](O)C2 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (1R,4R)-camphor Identifier CHEBI:15396 (Beilstein: 2042745; CAS: 464-49-3,76-22-2) help_outline Charge 0 Formula C10H16O InChIKeyhelp_outline DSSYKIVIOFKYAU-XCBNKYQSSA-N SMILEShelp_outline CC1(C)[C@@H]2CC[C@@]1(C)C(=O)C2 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,073 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:17329 | RHEA:17330 | RHEA:17331 | RHEA:17332 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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More general form(s) of this reaction
Publications
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Molecular cloning and functional characterization of a two highly stereoselective borneol dehydrogenases from Salvia officinalis L.
Drienovska I., Kolanovic D., Chanique A., Sieber V., Hofer M., Kourist R.
Enzymes for selective terpene functionalization are of particular importance for industrial applications. Pure enantiomers of borneol and isoborneol are fragrant constituents of several essential oils and find frequent application in cosmetics and therapy. Racemic borneol can be easily obtained fr ... >> More
Enzymes for selective terpene functionalization are of particular importance for industrial applications. Pure enantiomers of borneol and isoborneol are fragrant constituents of several essential oils and find frequent application in cosmetics and therapy. Racemic borneol can be easily obtained from racemic camphor, which in turn is readily available from industrial side-streams. Enantioselective biocatalysts for the selective conversion of borneol and isoborneol stereoisomers would be therefore highly desirable for their catalytic separation under mild reaction conditions. Although several borneol dehydrogenases from plants and bacteria have been reported, none show sufficient stereoselectivity. Despite Croteau et al. describing sage leaves to specifically oxidize one borneol enantiomer in the late 70s, no specific enzymes have been characterized. We expected that one or several alcohol dehydrogenases encoded in the recently elucidated genome of Salvia officinalis L. would, therefore, be stereoselective. This study thus reports the recombinant expression in E. coli and characterization of two enantiospecific enzymes from the Salvia officinalis L. genome, SoBDH1 and SoBDH2, and their comparison to other known ADHs. Both enzymes produce preferentially (+)-camphor from racemic borneol, but (-)-camphor from racemic isoborneol. << Less
Phytochemistry 172:112227-112227(2020) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Metabolism of monoterpenes: specificity of the dehydrogenases responsible for the biosynthesis of camphor, 3-thujone, and 3-isothujone.
Dehal S.S., Croteau R.
Sage (Salvia officinalis) is shown to contain two electrophoretically distinct dehydrogenases for the respective oxidations of (+)-borneol to (+)-camphor, and of (+)-cis-sabinol to (+)-sabinone en route to (-)-3-isothujone. Similarly, tansy (Tanacetum vulgare) is shown to contain two electrophoret ... >> More
Sage (Salvia officinalis) is shown to contain two electrophoretically distinct dehydrogenases for the respective oxidations of (+)-borneol to (+)-camphor, and of (+)-cis-sabinol to (+)-sabinone en route to (-)-3-isothujone. Similarly, tansy (Tanacetum vulgare) is shown to contain two electrophoretically distinct dehydrogenases for the respective oxidations of (-)-borneol to (-)-camphor and of (+)-cis-sabinol to (+)-sabinone en route to (+)-3-thujone. These results demonstrate that separate dehydrogenases are responsible for the biosynthesis of camphor from borneol and of the thujyl ketones via cis-sabinol, and they also indicate that the previously reported oxidations of various thujanols by the borneol dehydrogenases are only coincidental activities not relevant to the formation of 3-thujone and 3-isothujone. << Less
Arch Biochem Biophys 258:287-291(1987) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Biosynthesis of monoterpenes. Partial purfication and characterization of a bicyclic monoterpenol dehydrogenase from sage (Salvia officinalis).
Croteau R., Hooper C.L., Felton M.
Arch Biochem Biophys 188:182-193(1978) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.