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

Reaction

(R)-3-quinuclidinol
+
NAD+
=
3-quinuclidinone
+
NADH
+
H+

Synonyms

3-quinuclidinone reductase, alcohol dehydrogenase, ArQR, AtQR, BacC, NADHdependent 3-quinuclidionone reductase, QNR

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.B52 3-quinuclidinone reductase (NADH)

Crystallization

Crystallization on EC 1.1.1.B52 - 3-quinuclidinone reductase (NADH)

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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystallized under a reservoir solution condition of 0.2 M ammonium acetate, 0.1 M HEPES pH 8.5 and 24% (w/v) PEG3350
-
purified recombinant His-tagged enzyme, enzyme AtQR and 2 mM NADH are crystallized from a reservoir solution containing of 0.2 M ammonium acetate, 0.1 M HEPES, pH 8.5, and 24% w/v PEG 3350, X-ray diffraction structure determination and analysis at 1.72 A resolution. 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. Molecular replacement using structure of meso-2,3-butanediol dehydrogenase, PDB ID 1GEG, from Klebsiella pneumoniae as template
-
sitting-drop vapour-diffusion method at 20C. Crystals are obtained using a reservoir solution containing PEG 3350 as a precipitant. X-ray diffraction data are collected to 1.72 A resolution. The crystal belongs to space group P2(1), with unit-cell parameters a = 62.0, b = 126.4, c = 62.0 A, beta = 110.5, and is suggested to contain four molecules in the asymmetric unit
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