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Literature summary for 1.1.1.B51 extracted from

  • Takeshita, D.; Kataoka, M.; Miyakawa, T.; Miyazono, K.; Kumashiro, S.; Nagai, T.; Urano, N.; Uzura, A.; Nagata, K.; Shimizu, S.; Tanokura, M.
    Structural basis of stereospecific reduction by quinuclidinone reductase (2014), AMB Express, 4, 0000.
    View publication on PubMed
Search for more literature for 1.1.1.B51

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor-diffusion method with a reservoir solution containing 100 mM CHES (pH 10.0), 30% PEG8000, and 3% sucrose, at 5°C Rhodotorula mucilaginosa

Protein Variants

Protein Variants Comment Organism
F212A complete loss of activity Rhodotorula mucilaginosa
F212L complete loss of activity Rhodotorula mucilaginosa
I167A complete loss of activity Rhodotorula mucilaginosa
I167V relative activity for 3-qinuclidinone is 24.5% compared to wild-type enzyme Rhodotorula mucilaginosa
K185A complete loss of activity Rhodotorula mucilaginosa
N173A relative activity for 3-qinuclidinone is 97.8% compared to wild-type enzyme Rhodotorula mucilaginosa
Q178A relative activity for 3-qinuclidinone is 164.5% compared to wild-type enzyme Rhodotorula mucilaginosa
S166A complete loss of activity Rhodotorula mucilaginosa
S168A relative activity for 3-qinuclidinone is 115.7% compared to wild-type enzyme Rhodotorula mucilaginosa
Y181A complete loss of activity Rhodotorula mucilaginosa
Y181F complete loss of activity Rhodotorula mucilaginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme N173A Rhodotorula mucilaginosa
0.103
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme Q178A Rhodotorula mucilaginosa
0.168
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme S168A Rhodotorula mucilaginosa
0.308
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme I167V Rhodotorula mucilaginosa
0.44
-
 3-quinuclidinone pH 7.0, 30°C, wild-type enzyme Rhodotorula mucilaginosa

Organism

Organism UniProt Comment Textmining
Rhodotorula mucilaginosa B9ZZZ6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-quinuclidinone + NADPH + H+
-
 Rhodotorula mucilaginosa (R)-3-quinuclidinol + NADP+
-
 ?

Subunits

Subunits Comment Organism
tetramer
-
 Rhodotorula mucilaginosa

Synonyms

Synonyms Comment Organism
RrQR
-
 Rhodotorula mucilaginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Rhodotorula mucilaginosa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.69
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme I167V Rhodotorula mucilaginosa
5.62
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme N173A Rhodotorula mucilaginosa
9.64
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme S168A Rhodotorula mucilaginosa
9.79
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme Q178A Rhodotorula mucilaginosa
15.1
-
 3-quinuclidinone pH 7.0, 30°C, wild-type enzyme Rhodotorula mucilaginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Rhodotorula mucilaginosa

Cofactor

Cofactor Comment Organism Structure
NADPH residues R60 and S61 form hydrogen bonds with the 2'-phosphate group of the NADPH. These bonds are involved in the discrimination of NADPH from NADH Rhodotorula mucilaginosa