BRENDA - Enzyme Database
show all sequences of 1.1.99.31

Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and substrate binding

Xu, Y.; Dewanti, A.R.; Mitra, B.; Biochemistry 41, 12313-12319 (2002)

Data extracted from this reference:

Engineering
Protein Variants
Commentary
Organism
R165E
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 81.8fold decrease in kcat for (S)-mandelate, 199fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165G
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 27.3fold decrease in kcat for (S)-mandelate, 48.3fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165G/R277G
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
Pseudomonas putida
R165G/R277K
double mutant is less stable than single Arg165 mutant in term of long-term storage. 9000fold decrease in kcat for (S)-mandelate, 261.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165K
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 3fold decrease in kcat for (S)-mandelate, 12.5fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165K/R277G
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
Pseudomonas putida
R165K/R277K
double mutant is less stable than single Arg165 mutant in term of long-term storage. 327fold decrease in kcat for (S)-mandelate, 126.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165M
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 19.6fold decrease in kcat for (S)-mandelate, 36.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R277G
1565fold decrease in kcat for (S)-mandelate, 141fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R277K
5.5 fold decrease in kcat for (S)-mandelate, 46.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
Inhibitors
Inhibitors
Commentary
Organism
Structure
(R)-mandelate
-
Pseudomonas putida
2-phenylethanoate
-
Pseudomonas putida
phenylethanediol
poor competitive inhibitor of wild-type enzyme
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.12
-
(S)-Mandelate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
1.5
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
4.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165M
Pseudomonas putida
5.6
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
5.8
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
12
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165E
Pseudomonas putida
15.2
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K/R277K
Pseudomonas putida
17
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
31.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas putida
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Pseudomonas putida
Storage Stability
Storage Stability
Organism
-70C, wild-type enzyme retains activity for more than 1 year. The single Arg165 mutant lose activity after 2-3 months, double mutants R165K/R277K and R165G/R277K are inactivated after 2-3 weeks in storage
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(S)-mandelate + acceptor
reduction of 2,6-dichloroindophenol in presence of N-methylphenazonium methosulfate
667572
Pseudomonas putida
2-oxo-2-phenylacetate + reduced acceptor
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.04
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
0.23
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
1.1
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K/R277K
Pseudomonas putida
4.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165E
Pseudomonas putida
13.2
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
18.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165M
Pseudomonas putida
66
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
120
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
360
-
(S)-Mandelate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
-
Pseudomonas putida
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.9
-
(R)-mandelate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
3.1
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
7.2
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
11
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
11
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165K/R277K
Pseudomonas putida
12
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
12
-
2-phenylethanoate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
19.5
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
20.3
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
22.5
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
67
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
73
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
700
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
-
Pseudomonas putida
Engineering (protein specific)
Protein Variants
Commentary
Organism
R165E
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 81.8fold decrease in kcat for (S)-mandelate, 199fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165G
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 27.3fold decrease in kcat for (S)-mandelate, 48.3fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165G/R277G
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
Pseudomonas putida
R165G/R277K
double mutant is less stable than single Arg165 mutant in term of long-term storage. 9000fold decrease in kcat for (S)-mandelate, 261.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165K
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 3fold decrease in kcat for (S)-mandelate, 12.5fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165K/R277G
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
Pseudomonas putida
R165K/R277K
double mutant is less stable than single Arg165 mutant in term of long-term storage. 327fold decrease in kcat for (S)-mandelate, 126.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R165M
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 19.6fold decrease in kcat for (S)-mandelate, 36.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R277G
1565fold decrease in kcat for (S)-mandelate, 141fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
R277K
5.5 fold decrease in kcat for (S)-mandelate, 46.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
Pseudomonas putida
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(R)-mandelate
-
Pseudomonas putida
2-phenylethanoate
-
Pseudomonas putida
phenylethanediol
poor competitive inhibitor of wild-type enzyme
Pseudomonas putida
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.9
-
(R)-mandelate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
3.1
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
7.2
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
11
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
11
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165K/R277K
Pseudomonas putida
12
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
12
-
2-phenylethanoate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
19.5
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
20.3
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
22.5
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
67
-
2-phenylethanoate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
73
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
700
-
(R)-mandelate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.12
-
(S)-Mandelate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
1.5
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
4.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165M
Pseudomonas putida
5.6
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
5.8
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
12
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165E
Pseudomonas putida
15.2
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K/R277K
Pseudomonas putida
17
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
31.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas putida
Storage Stability (protein specific)
Storage Stability
Organism
-70C, wild-type enzyme retains activity for more than 1 year. The single Arg165 mutant lose activity after 2-3 months, double mutants R165K/R277K and R165G/R277K are inactivated after 2-3 weeks in storage
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(S)-mandelate + acceptor
reduction of 2,6-dichloroindophenol in presence of N-methylphenazonium methosulfate
667572
Pseudomonas putida
2-oxo-2-phenylacetate + reduced acceptor
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.04
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G/R277K
Pseudomonas putida
0.23
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277G
Pseudomonas putida
1.1
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K/R277K
Pseudomonas putida
4.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165E
Pseudomonas putida
13.2
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165G
Pseudomonas putida
18.4
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165M
Pseudomonas putida
66
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R277K
Pseudomonas putida
120
-
(S)-Mandelate
pH 7.5, 20C, mutant enzyme R165K
Pseudomonas putida
360
-
(S)-Mandelate
pH 7.5, 20C, wild-type enzyme
Pseudomonas putida
Other publictions for EC 1.1.99.31
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
Synonyms
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)
740174
Chen
Stereoselective biotransformat ...
Escherichia coli
Bioresour. Bioproc.
4
2-2
2017
-
-
-
-
-
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-
1
-
-
-
1
-
1
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1
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1
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1
1
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1
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1
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1
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1
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1
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1
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-
-
-
-
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-
740119
Mazurenko
Immobilization of membrane-bou ...
Pseudomonas putida, Pseudomonas putida DSM 291
Bioelectrochemistry
104
65-70
2015
-
-
-
-
-
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-
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2
-
4
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2
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1
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2
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725744
Wang
-
A bi-enzymatic system for effi ...
Pseudomonas aeruginosa
J. Mol. Catal. B
94
47-50
2013
-
-
1
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-
-
2
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1
-
1
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1
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2
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1
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1
1
1
1
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1
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1
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1
1
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2
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1
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1
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2
-
1
-
1
1
1
-
1
-
-
-
-
-
-
-
-
-
695329
Sukumar
Structures of the G81A mutant ...
Pseudomonas putida
Acta Crystallogr. Sect. D
65
543-552
2009
-
-
1
1
2
-
-
12
-
-
-
-
-
4
-
-
1
-
-
-
-
-
4
-
1
-
-
-
12
-
-
-
1
-
-
-
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-
1
1
1
2
-
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-
-
12
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
12
-
-
-
-
-
-
-
-
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-
667577
Dewanti
Role of glycine 81 in (S)-mand ...
Pseudomonas putida
Biochemistry
43
10692-10700
2004
-
-
-
-
5
-
1
36
-
-
-
-
-
4
-
-
1
-
-
-
-
-
13
-
-
-
-
-
36
-
-
-
1
-
-
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-
-
-
1
-
5
-
-
1
-
36
-
-
-
-
-
-
-
1
-
-
-
-
13
-
-
-
-
36
-
-
-
-
-
-
-
-
-
-
669259
Sukumar
High resolution structures of ...
Pseudomonas putida
J. Biol. Chem.
279
3749-3757
2004
-
-
-
1
-
-
-
-
-
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3
-
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1
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2
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1
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1
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2
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678128
Dewanti
Esters of mandelic acid as sub ...
Pseudomonas putida
Biochemistry
43
1883-1890
2004
-
-
-
-
2
-
4
9
-
-
-
-
-
5
-
-
1
-
-
-
-
-
4
-
1
-
-
-
9
-
-
-
1
2
-
-
-
-
-
1
-
2
-
-
4
2
9
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
667575
Dewanti
A transient intermediate in th ...
Pseudomonas putida
Biochemistry
42
12893-12901
2003
-
-
-
-
-
-
-
2
-
-
-
-
-
5
-
-
1
-
-
-
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1
-
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-
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2
-
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1
-
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-
-
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1
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2
-
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1
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1
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-
-
2
-
-
-
-
-
-
-
-
-
-
667572
Xu
Arginine 165/arginine 277 pair ...
Pseudomonas putida
Biochemistry
41
12313-12319
2002
-
-
-
-
10
-
3
9
-
-
-
-
-
5
-
-
1
-
-
-
-
1
1
-
-
-
-
-
9
-
-
-
1
13
-
-
-
-
-
1
-
10
-
-
3
13
9
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
-
-
9
-
-
-
-
-
-
-
-
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-
667570
Sukumar
Structure of an active soluble ...
Pseudomonas putida
Biochemistry
40
9870-9878
2001
-
-
-
1
-
-
-
-
-
-
-
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-
3
-
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-
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1
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-
-
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-
667567
Lehoux
Role of arginine 277 in (S)-ma ...
Pseudomonas putida
Biochemistry
39
10055-10065
2000
-
-
-
-
4
-
-
7
-
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4
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1
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2
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7
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4
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7
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1
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2
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7
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667565
Xu
A highly active, soluble mutan ...
Pseudomonas putida
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1999
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14
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15
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14
1
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14
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15
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667566
Lehoux
(S)-Mandelate dehydrogenase fr ...
Pseudomonas putida
Biochemistry
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9948-9955
1999
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3
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1
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5
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1
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678122
Lehoux
(S)-Mandelate dehydrogenase fr ...
Pseudomonas putida
Biochemistry
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1999
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11
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14
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Illias
L-Mandelate dehydrogenase from ...
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Mitra
A novel structural basis for m ...
Pseudomonas putida
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