BRENDA - Enzyme Database show
show all sequences of 1.1.1.B51

Structural basis of stereospecific reduction by quinuclidinone reductase

Takeshita, D.; Kataoka, M.; Miyakawa, T.; Miyazono, K.; Kumashiro, S.; Nagai, T.; Urano, N.; Uzura, A.; Nagata, K.; Shimizu, S.; Tanokura, M.; AMB Express 4, 0000 (2014)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
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
Engineering
Amino acid exchange
Commentary
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
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodotorula mucilaginosa
B9ZZZ6
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-quinuclidinone + NADPH + H+
-
728943
Rhodotorula mucilaginosa
(R)-3-quinuclidinol + NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
-
Rhodotorula mucilaginosa
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rhodotorula mucilaginosa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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
Commentary
Organism
7
-
assay at
Rhodotorula mucilaginosa
Cofactor
Cofactor
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
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
Crystallization (Commentary) (protein specific)
Crystallization
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
Engineering (protein specific)
Amino acid exchange
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-quinuclidinone + NADPH + H+
-
728943
Rhodotorula mucilaginosa
(R)-3-quinuclidinol + NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
-
Rhodotorula mucilaginosa
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rhodotorula mucilaginosa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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 (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Rhodotorula mucilaginosa
Other publictions for EC 1.1.1.B51
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
728943
Takeshita
Structural basis of stereospec ...
Rhodotorula mucilaginosa
AMB Express
4
0000
2014
-
-
-
1
11
-
-
5
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
1
-
-
5
1
-
-
1
-
-
-
-
-
-
1
1
11
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
-
-
5
1
-
-
-
-
-
-
-
-
-
728883
Takeshita
Crystallization and preliminar ...
Rhodotorula mucilaginosa
Acta Crystallogr. Sect. F
65
645-647
2009
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
729053
Uzura
Stereoselective synthesis of ( ...
Rhodotorula mucilaginosa, Rhodotorula mucilaginosa JCM3782
Appl. Microbiol. Biotechnol.
83
617-626
2009
-
2
1
-
-
-
3
2
-
-
2
-
-
2
-
-
1
-
-
-
1
-
8
1
1
-
-
-
2
-
-
1
-
-
-
-
2
1
1
-
-
-
-
3
-
2
-
-
2
-
-
-
-
1
-
-
1
-
8
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-