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Literature summary for 1.1.1.B52 extracted from

  • Hou, F.; Miyakawa, T.; Kataoka, M.; Takeshita, D.; Kumashiro, S.; Uzura, A.; Urano, N.; Nagata, K.; Shimizu, S.; Tanokura, M.
    Structural basis for high substrate-binding affinity and enantioselectivity of 3-quinuclidinone reductase AtQR (2014), Biochem. Biophys. Res. Commun., 446, 911-915.
    View publication on PubMed

Application

Application Comment Organism
pharmacology stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals Agrobacterium tumefaciens
synthesis stereospecific production of (R)-3-quinuclidinol, an important chiral building block for the synthesis of various pharmaceuticals Agrobacterium tumefaciens

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed as a fusion protein with an N-terminal His6 tag in Eschrichia coli Rosetta(DE3) Agrobacterium tumefaciens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized under a reservoir solution condition of 0.2 M ammonium acetate, 0.1 M HEPES pH 8.5 and 24% (w/v) PEG3350 Agrobacterium tumefaciens

Protein Variants

Protein Variants Comment Organism
D40A no activity Agrobacterium tumefaciens
E197A no activity Agrobacterium tumefaciens
R196A activity is 76% compared to activity of wild-type enzyme Agrobacterium tumefaciens
Y216V activity is 31% compared to activity of wild-type enzyme Agrobacterium tumefaciens

General Stability

General Stability Organism
NADH contributes to the stability of the alpha7 helix of the enzyme Agrobacterium tumefaciens

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens G1K3P5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Agrobacterium tumefaciens

Synonyms

Synonyms Comment Organism
AtQR
-
Agrobacterium tumefaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Agrobacterium tumefaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Agrobacterium tumefaciens

Cofactor

Cofactor Comment Organism Structure
NADH
-
Agrobacterium tumefaciens