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
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phosphate-dependent
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protomer
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nadh-dependent
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vapour-diffusion
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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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General Information
General Information on EC 1.1.1.B52 - 3-quinuclidinone reductase (NADH)
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evolution
additional information
AtQR has all three catalytic residues of the short-chain dehydrogenases/reductases family and the hydrophobic wall for the enantioselective reduction of 3-quinuclidinone
evolution
the enzyme belongs to the short-chain alcohol dehydrogenase/reductase (SDR) family
evolution
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the enzyme belongs to the short-chain alcohol dehydrogenase/reductase (SDR) family
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the alpha7 helix is a unique and functionally significant part of AtQR and is related to form a deep catalytic cavity, it is stabilized by NADH. An additional residue on the a7 helix, Glu197, exists near the active site of AtQR. This acidic residue is considered to form a direct interaction with the amine part of 3-quinuclidinone, which contributes to substrate orientation and enhancement of substrate-binding affinity. Glu197 is an indispensable residue for the enzyme activity. Asp40 plays an important role in binding to NADH. Glu197 may be the key residue for enhancing the substrate-binding affinity. Structure-function anaysis and enantioselectivity, overview.
additional information
-
the alpha7 helix is a unique and functionally significant part of AtQR and is related to form a deep catalytic cavity, it is stabilized by NADH. An additional residue on the a7 helix, Glu197, exists near the active site of AtQR. This acidic residue is considered to form a direct interaction with the amine part of 3-quinuclidinone, which contributes to substrate orientation and enhancement of substrate-binding affinity. Glu197 is an indispensable residue for the enzyme activity. Asp40 plays an important role in binding to NADH. Glu197 may be the key residue for enhancing the substrate-binding affinity. Structure-function anaysis and enantioselectivity, overview.