1.1.1.B52: 3-quinuclidinone reductase (NADH)
This is an abbreviated version!
For detailed information about 3-quinuclidinone reductase (NADH), go to the full flat file.
Word Map on EC 1.1.1.B52
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1.1.1.B52
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rhodotorula
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synthesis
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rubra
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pharmacology
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tumefaciens
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agrobacterium
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peg
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nicotinamide
-
phosphate-dependent
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protomer
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nadh-dependent
-
vapour-diffusion
-
sitting-drop
- 1.1.1.B52
-
rhodotorula
- synthesis
- rubra
- pharmacology
- tumefaciens
-
agrobacterium
- peg
- nicotinamide
-
phosphate-dependent
-
protomer
-
nadh-dependent
-
vapour-diffusion
-
sitting-drop
Reaction
Synonyms
3-quinuclidinone reductase, alcohol dehydrogenase, ArQR, AtQR, BacC, NADHdependent 3-quinuclidionone reductase, QNR
ECTree
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Cofactor
Cofactor on EC 1.1.1.B52 - 3-quinuclidinone reductase (NADH)
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NADH
three NADH-bound protomers and one NADH-free protomer form a tetrameric structure in an asymmetric unit of crystals. NADH not only acts as a proton donor, but also contributes to the stability of the alpha7 helix. NADH is located in a deep cleft of the large domain and bound at the C-terminal end of the beta-sheet. The adenosine moiety of NADH is bound to a pocket formed by Gly16, Leu41, Val62, Asp63, Val64, Thr65, Ala91, Val93, and Val113. Residue Asp40 plays an important role in binding to NADH