EC 1.1.1.275: (+)-trans-carveol dehydrogenase
This is an abbreviated version!
For detailed information about (+)-trans-carveol dehydrogenase, go to the full flat file.
Reaction
Synonyms
carveol dehydrogenase, MAP_4146, MAV_0896, MAV_1393, MAV_1810, MAV_2598, MAV_2983
ECTree
1.1.1.275 (+)-trans-carveol dehydrogenaseAdvanced search results
results (
results (| Results | in table |
|---|---|
| 6 | AA Sequence |
| 2 | Application |
| 2 | Cofactor |
| 6 | Crystallization (Commentary) |
| 1 | Localization |
| 1 | Natural Substrates/ Products (Substrates) |
| 15 | Organism |
| 6 | Pathway |
| 20 | PDB ID |
| 1 | pH Optimum |
| 1 | Reaction |
| 3 | Reaction Type |
| 15 | Reference |
| 2 | Source Tissue |
| 9 | Substrates and Products (Substrate) |
| 13 | Synonyms |
| 1 | Systematic Name |
| 1 | Temperature Optimum [°C] |
Crystallization
Crystallization on EC 1.1.1.275 - (+)-trans-carveol dehydrogenase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
to 1.55 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 2.0 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 2.15 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 1.85 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
