BRENDA - Enzyme Database show
show all sequences of 5.3.2.6

Kinetic, stereochemical, and structural effects of mutations of the active site arginine residues in 4-oxalocrotonate tautomerase

Harris, T.K.; Czerwinski, R.M.; Johnson, W.H.; Legler, P.M.; Abeygunawardana, C.; Massiah, M.A.; Stivers, J.T.; Whitman, C.P.; Mildvan, A.S.; Biochemistry 38, 12343-12357 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression of wild-type and mutants in Escherichia coli strain BL21(DE3)pLysS, subcloning in Escherichia coli strain JM109
Pseudomonas putida
Engineering
Amino acid exchange
Commentary
Organism
R11A
site-directed mutagenesis, no kinetic effects of the R11A mutation, the stereoselectivity of the R11A-catalyzed protonation at C-5 of the dicarboxylate substrate decreases, while the stereoselectivity of protonation at C-3 of the monocarboxylate substrate increases in comparison with wild-type 4-OT
Pseudomonas putida
R11A/R39A
site-directed mutagenesis, inactive mutant
Pseudomonas putida
R39A
site-directed mutagenesis, with 2-hydroxymuconate the R39A mutant shows decreased kcat by 125fold and increased Km by 1.5fold
Pseudomonas putida
R39Q
site-directed mutagenesis, with 2-hydroxymuconate the R39Q mutant shows decreased kcat by 389fold and increased Km by 2.6fold, only the tight binding sites function catalytically in the R39Q mutant, structural changes in the R39Q mutant were mainly in the beta-hairpin from residues 50 to 57 which covers the active site
Pseudomonas putida
R61A
site-directed mutagenesis, Arg61 mutation does not affect either substrate binding or catalysis
Pseudomonas putida
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-Oxo-3-pentynoate
mechanism-based inhibitor
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics, overview
Pseudomonas putida
0.18
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
0.29
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A/R39A; pH 7.3, 23°C, mutant R39A
Pseudomonas putida
0.47
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39Q
Pseudomonas putida
1.11
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, mutant R11A; pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
1.6
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-oxo-4-hexenedioate
Pseudomonas putida
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
2-oxo-3-hexenedioate
-
-
?
2-oxo-4-hexenedioate
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
2-oxo-3-hexenedioate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutants from Escherichia coli strain BL21(DE3)pLysS to homogeneity
Pseudomonas putida
Reaction
Reaction
Commentary
Organism
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate
catalytic reaction mechanism, detailed overview
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxy-2,4-hexadienedioate
-
718830
Pseudomonas putida
2-oxo-3-hexenedioate
-
-
-
?
2-hydroxy-2,4-hexadienedioate
-
718830
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3-hexenedioate
-
-
-
?
2-hydroxy-2,4-pentadienoate
enzyme-catalyzed ketonization of 2-hydroxy-2,4-pentadienoate to (3R)-2-oxo-[3-D]-4-pentenoate is only stereoselective
718830
Pseudomonas putida
2-oxo-3,4-pentenoate
-
-
-
?
2-hydroxy-2,4-pentadienoate
enzyme-catalyzed ketonization of 2-hydroxy-2,4-pentadienoate to (3R)-2-oxo-[3-D]-4-pentenoate is only stereoselective
718830
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3,4-pentenoate
-
-
-
?
2-oxo-4-hexenedioate
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
718830
Pseudomonas putida
2-oxo-3-hexenedioate
-
-
-
?
2-oxo-4-hexenedioate
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
718830
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3-hexenedioate
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
structure-function relationship, NMR analysis, overview
Pseudomonas putida
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
23
-
assay at
Pseudomonas putida
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.4
-
2-hydroxy-2,4-hexadienedioate
below, pH 7.3, 23°C, mutant R11A/R39A
Pseudomonas putida
0.4
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
1
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
2
8
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39A
Pseudomonas putida
9
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39Q
Pseudomonas putida
40
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
3500
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression of wild-type and mutants in Escherichia coli strain BL21(DE3)pLysS, subcloning in Escherichia coli strain JM109
Pseudomonas putida
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
R11A
site-directed mutagenesis, no kinetic effects of the R11A mutation, the stereoselectivity of the R11A-catalyzed protonation at C-5 of the dicarboxylate substrate decreases, while the stereoselectivity of protonation at C-3 of the monocarboxylate substrate increases in comparison with wild-type 4-OT
Pseudomonas putida
R11A/R39A
site-directed mutagenesis, inactive mutant
Pseudomonas putida
R39A
site-directed mutagenesis, with 2-hydroxymuconate the R39A mutant shows decreased kcat by 125fold and increased Km by 1.5fold
Pseudomonas putida
R39Q
site-directed mutagenesis, with 2-hydroxymuconate the R39Q mutant shows decreased kcat by 389fold and increased Km by 2.6fold, only the tight binding sites function catalytically in the R39Q mutant, structural changes in the R39Q mutant were mainly in the beta-hairpin from residues 50 to 57 which covers the active site
Pseudomonas putida
R61A
site-directed mutagenesis, Arg61 mutation does not affect either substrate binding or catalysis
Pseudomonas putida
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-Oxo-3-pentynoate
mechanism-based inhibitor
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics, overview
Pseudomonas putida
0.18
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
0.29
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A/R39A; pH 7.3, 23°C, mutant R39A
Pseudomonas putida
0.47
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39Q
Pseudomonas putida
1.11
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, mutant R11A; pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
1.6
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-oxo-4-hexenedioate
Pseudomonas putida
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
2-oxo-3-hexenedioate
-
-
?
2-oxo-4-hexenedioate
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
2-oxo-3-hexenedioate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutants from Escherichia coli strain BL21(DE3)pLysS to homogeneity
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxy-2,4-hexadienedioate
-
718830
Pseudomonas putida
2-oxo-3-hexenedioate
-
-
-
?
2-hydroxy-2,4-hexadienedioate
-
718830
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3-hexenedioate
-
-
-
?
2-hydroxy-2,4-pentadienoate
enzyme-catalyzed ketonization of 2-hydroxy-2,4-pentadienoate to (3R)-2-oxo-[3-D]-4-pentenoate is only stereoselective
718830
Pseudomonas putida
2-oxo-3,4-pentenoate
-
-
-
?
2-hydroxy-2,4-pentadienoate
enzyme-catalyzed ketonization of 2-hydroxy-2,4-pentadienoate to (3R)-2-oxo-[3-D]-4-pentenoate is only stereoselective
718830
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3,4-pentenoate
-
-
-
?
2-oxo-4-hexenedioate
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
718830
Pseudomonas putida
2-oxo-3-hexenedioate
-
-
-
?
2-oxo-4-hexenedioate
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
718830
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3-hexenedioate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
structure-function relationship, NMR analysis, overview
Pseudomonas putida
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
23
-
assay at
Pseudomonas putida
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.4
-
2-hydroxy-2,4-hexadienedioate
below, pH 7.3, 23°C, mutant R11A/R39A
Pseudomonas putida
0.4
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
1
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
2
8
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39A
Pseudomonas putida
9
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39Q
Pseudomonas putida
40
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
3500
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Pseudomonas putida
General Information
General Information
Commentary
Organism
metabolism
the enzyme is part of a degradative pathway that converts various aromatic hydrocarbons to intermediates in the Krebs cycle
Pseudomonas putida
additional information
structure-function relationship, spectroscopic NMR analysis, detailed overview. Three arginine residues, Arg11, Arg39, and Arg61, are localized in the active site of 4-oxalocrotonate tautomerase. Importance of Arg11 in properly orienting the dicarboxylate substrate by interacting with the charged 6-carboxylate group. Arg39 interacts with the 1-carboxylate and the 2-keto group of the substrate to promote carbonyl polarization and catalysis, while Pro-1 transfers protons from C-3 to C-5. Arg61 does not play a significant role in either substrate binding or catalysis
Pseudomonas putida
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is part of a degradative pathway that converts various aromatic hydrocarbons to intermediates in the Krebs cycle
Pseudomonas putida
additional information
structure-function relationship, spectroscopic NMR analysis, detailed overview. Three arginine residues, Arg11, Arg39, and Arg61, are localized in the active site of 4-oxalocrotonate tautomerase. Importance of Arg11 in properly orienting the dicarboxylate substrate by interacting with the charged 6-carboxylate group. Arg39 interacts with the 1-carboxylate and the 2-keto group of the substrate to promote carbonyl polarization and catalysis, while Pro-1 transfers protons from C-3 to C-5. Arg61 does not play a significant role in either substrate binding or catalysis
Pseudomonas putida
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.36
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
0.9
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
19
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39Q
Pseudomonas putida
25
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
97
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39A
Pseudomonas putida
12000
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A/R39A
Pseudomonas putida
19000
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.36
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
0.9
-
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
19
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39Q
Pseudomonas putida
25
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A
Pseudomonas putida
97
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R39A
Pseudomonas putida
12000
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, mutant R11A/R39A
Pseudomonas putida
19000
-
2-hydroxy-2,4-hexadienedioate
pH 7.3, 23°C, wild-type enzyme
Pseudomonas putida
Other publictions for EC 5.3.2.6
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)
747133
Stack
Inactivation of 4-oxalocroton ...
Leptothrix cholodnii, Leptothrix cholodnii SP-6, Pseudomonas putida
Biochemistry
57
1012-1021
2018
-
-
-
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18
-
-
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-
3
-
4
-
-
2
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3
1
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18
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3
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2
-
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3
1
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-
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-
-
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-
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-
-
-
749336
Diemen
The S. aureus 4-oxalocrotonat ...
Staphylococcus aureus, Staphylococcus aureus MRSA252
Sci. Rep.
7
1745
2017
-
-
1
-
3
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
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1
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3
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2
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748503
Lazic
-
Importance of N-terminal prol ...
Pseudomonas putida
J. Serb. Chem. Soc.
81
871-881
2016
-
-
1
-
-
-
-
-
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1
-
1
-
-
-
-
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4
-
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1
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1
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4
-
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-
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-
-
-
-
748742
van der Meer
Using mutability landscapes o ...
Pseudomonas putida
Nat. Commun.
7
10911
2016
-
-
1
1
6
-
-
-
-
-
-
2
-
1
-
-
1
-
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
6
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
10
-
-
-
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747290
Djokic
Immobilization of Escherichia ...
Pseudomonas putida
Bioprocess Biosyst. Eng.
38
2389-2395
2015
-
-
1
-
-
-
-
-
-
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-
1
-
3
-
-
-
-
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2
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1
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1
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2
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747537
Poddar
Evidence for the formation of ...
Pseudomonas putida
ChemBioChem
16
738-741
2015
-
-
-
-
-
-
1
-
-
-
-
1
-
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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-
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-
746910
Huddleston
Identification and characteri ...
Pseudomonas putida
Arch. Biochem. Biophys.
564
189-196
2014
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747782
Baas
Demethionylation of Pro-1 var ...
Pseudomonas putida
FEBS Open Bio
4
651-658
2014
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1
749284
Radivojevic
-
Synthesis of gamma-nitroaldeh ...
Pseudomonas putida
RSC Adv.
4
60502-60510
2014
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1
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726816
Terrell
Structural and kinetic charact ...
Methylibium petroleiphilum
Arch. Biochem. Biophys.
537
113-124
2013
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4
727187
Narancic
Highly efficient Michael-type ...
Pseudomonas putida
Biores. Technol.
142
462-468
2013
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727314
Miao
Promiscuous catalysis of asymm ...
Bacillus subtilis
ChemBioChem
14
191-194
2013
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727327
Geertsema
Biocatalytic Michael-type addi ...
Escherichia coli
Chemistry
19
14407-14410
2013
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720309
Wu
Catalytic mechanism of 4-oxalo ...
Pseudomonas putida
J. Phys. Chem. B
116
6889-6897
2012
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3
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726964
Burks
Kinetic, crystallographic, and ...
Pseudomonas putida
Biochemistry
50
7600-7611
2011
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6
6
718874
Burks
Kinetic and structural charact ...
Chloroflexus aurantiacus, Chloroflexus aurantiacus J-10-fl
Biochemistry
49
5016-5027
2010
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1
5
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12
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2
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12
1
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3
3
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12
12
721792
Almrud
Kinetic and structural charact ...
Archaeoglobus fulgidus, Helicobacter pylori
Bioorg. Chem.
38
252-259
2010
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2
2
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8
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2
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8
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704310
Kasai
Uncovering the protocatechuate ...
Paenibacillus sp., Paenibacillus sp. JJ-1b
J. Bacteriol.
191
6758-6768
2009
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718847
Wang
Kinetic and stereochemical ana ...
Bacillus subtilis, Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
Biochemistry
46
11919-11929
2007
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21
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2
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1
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718844
Poelarends
Evolution of enzymatic activit ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
Biochemistry
45
7700-7708
2006
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21
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1
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1
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4
4
718840
Azurmendi
Half-of-the-sites binding of r ...
Pseudomonas putida
Biochemistry
44
7725-7737
2005
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718830
Harris
Kinetic, stereochemical, and s ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
Biochemistry
38
12343-12357
1999
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1
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5
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6
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2
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19
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1
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6
1
1
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7
1
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2
2
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7
7
718825
Subramanya
Enzymatic ketonization of 2-hy ...
Pseudomonas sp., Pseudomonas sp. CF 600
Biochemistry
35
792-802
1996
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2
2
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718826
Stivers
Catalytic role of the amino-te ...
Pseudomonas sp., Pseudomonas sp. CF 600
Biochemistry
35
803-813
1996
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1
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9
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2
1
1
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1
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719636
Fitzgerald
-
Total chemical synthesis and c ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Am. Chem. Soc.
117
11075-11080
1995
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2
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2
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19
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1
1
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1
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4
1
1
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2
1
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1
1
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2
2
719634
Whitman
-
Stereospecific ketonization of ...
Escherichia coli, Escherichia coli C, Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Am. Chem. Soc.
114
10104-10110
1992
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27
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4
2
2
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2
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4
4
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719633
Whitman
-
Chemical and enzymatic ketoniz ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Am. Chem. Soc.
113
3154-3162
1991
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19
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2