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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.B51 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

EC Number Protein Variants Comment Organism
1.1.1.B51 F212A complete loss of activity Rhodotorula mucilaginosa
1.1.1.B51 F212L complete loss of activity Rhodotorula mucilaginosa
1.1.1.B51 I167A complete loss of activity Rhodotorula mucilaginosa
1.1.1.B51 I167V relative activity for 3-qinuclidinone is 24.5% compared to wild-type enzyme Rhodotorula mucilaginosa
1.1.1.B51 K185A complete loss of activity Rhodotorula mucilaginosa
1.1.1.B51 N173A relative activity for 3-qinuclidinone is 97.8% compared to wild-type enzyme Rhodotorula mucilaginosa
1.1.1.B51 Q178A relative activity for 3-qinuclidinone is 164.5% compared to wild-type enzyme Rhodotorula mucilaginosa
1.1.1.B51 S166A complete loss of activity Rhodotorula mucilaginosa
1.1.1.B51 S168A relative activity for 3-qinuclidinone is 115.7% compared to wild-type enzyme Rhodotorula mucilaginosa
1.1.1.B51 Y181A complete loss of activity Rhodotorula mucilaginosa
1.1.1.B51 Y181F complete loss of activity Rhodotorula mucilaginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.B51 0.1
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme N173A Rhodotorula mucilaginosa
1.1.1.B51 0.103
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme Q178A Rhodotorula mucilaginosa
1.1.1.B51 0.168
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme S168A Rhodotorula mucilaginosa
1.1.1.B51 0.308
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme I167V Rhodotorula mucilaginosa
1.1.1.B51 0.44
-
 3-quinuclidinone pH 7.0, 30°C, wild-type enzyme Rhodotorula mucilaginosa

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.B51 Rhodotorula mucilaginosa B9ZZZ6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.B51 3-quinuclidinone + NADPH + H+
-
 Rhodotorula mucilaginosa (R)-3-quinuclidinol + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.B51 tetramer
-
 Rhodotorula mucilaginosa

Synonyms

EC Number Synonyms Comment Organism
1.1.1.B51 RrQR
-
 Rhodotorula mucilaginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.B51 30
-
 assay at Rhodotorula mucilaginosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.B51 2.69
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme I167V Rhodotorula mucilaginosa
1.1.1.B51 5.62
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme N173A Rhodotorula mucilaginosa
1.1.1.B51 9.64
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme S168A Rhodotorula mucilaginosa
1.1.1.B51 9.79
-
 3-quinuclidinone pH 7.0, 30°C, mutant enzyme Q178A Rhodotorula mucilaginosa
1.1.1.B51 15.1
-
 3-quinuclidinone pH 7.0, 30°C, wild-type enzyme Rhodotorula mucilaginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.B51 7
-
 assay at Rhodotorula mucilaginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.B51 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