BRENDA - Enzyme Database show
show all sequences of 1.14.13.54

Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase

Franceschini, S.; van Beek, H.L.; Pennetta, A.; Martinoli, C.; Fraaije, M.W.; Mattevi, A.; J. Biol. Chem. 287, 22626-22634 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) CodonPlus cells
Rhodococcus rhodochrous
Crystallization (Commentary)
Crystallization
Organism
sitting drop vapor diffusion method, using 1.8-2.2 M MgSO4, 0.1 M MES/HCl, pH 6.2-6.5
Rhodococcus rhodochrous
Engineering
Amino acid exchange
Commentary
Organism
K295A
the mutant is 3times more active than the wild type enzyme
Rhodococcus rhodochrous
L500Y
the mutant is about 2.5times more active than the wild type enzyme
Rhodococcus rhodochrous
P157Q
the mutant shows wild type activity
Rhodococcus rhodochrous
T345L
the mutation turns the enzyme inactive against progesterone without altering the catalytic efficiency for phenylacetone
Rhodococcus rhodochrous
V291A
the mutant is less active than the wild type enzyme
Rhodococcus rhodochrous
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
-
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication; mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
0.6
-
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
0.8
-
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1
-
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.6
-
phenylacetone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
progesterone + NADPH + H+ + O2
Rhodococcus rhodochrous
-
testosterone acetate + NADP+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus rhodochrous
O50641
-
-
Purification (Commentary)
Commentary
Organism
Ni2+-affinity column chromatography and Superdex 75 gel filtration
Rhodococcus rhodochrous
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phenylacetone + NADPH + H+ + O2
-
727906
Rhodococcus rhodochrous
benzylacetate + NADP+ + H2O
-
-
-
?
progesterone + NADPH + H+ + O2
-
727906
Rhodococcus rhodochrous
testosterone acetate + NADP+ + H2O
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
phenylacetone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
0.6
-
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1
-
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.5
-
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.8
-
phenylacetone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
3
-
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Rhodococcus rhodochrous
NADPH
-
Rhodococcus rhodochrous
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) CodonPlus cells
Rhodococcus rhodochrous
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Rhodococcus rhodochrous
NADPH
-
Rhodococcus rhodochrous
Crystallization (Commentary) (protein specific)
Crystallization
Organism
sitting drop vapor diffusion method, using 1.8-2.2 M MgSO4, 0.1 M MES/HCl, pH 6.2-6.5
Rhodococcus rhodochrous
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K295A
the mutant is 3times more active than the wild type enzyme
Rhodococcus rhodochrous
L500Y
the mutant is about 2.5times more active than the wild type enzyme
Rhodococcus rhodochrous
P157Q
the mutant shows wild type activity
Rhodococcus rhodochrous
T345L
the mutation turns the enzyme inactive against progesterone without altering the catalytic efficiency for phenylacetone
Rhodococcus rhodochrous
V291A
the mutant is less active than the wild type enzyme
Rhodococcus rhodochrous
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
-
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication; mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
0.6
-
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
0.8
-
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1
-
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.6
-
phenylacetone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
progesterone + NADPH + H+ + O2
Rhodococcus rhodochrous
-
testosterone acetate + NADP+ + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
Ni2+-affinity column chromatography and Superdex 75 gel filtration
Rhodococcus rhodochrous
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phenylacetone + NADPH + H+ + O2
-
727906
Rhodococcus rhodochrous
benzylacetate + NADP+ + H2O
-
-
-
?
progesterone + NADPH + H+ + O2
-
727906
Rhodococcus rhodochrous
testosterone acetate + NADP+ + H2O
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
phenylacetone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
0.6
-
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1
-
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.5
-
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.8
-
phenylacetone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
3
-
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.1
-
progesterone
kcat_Km less than 0.1 1/sec*min, mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.2
-
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication; mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.4
-
progesterone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.5
-
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.7
-
progesterone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.8
-
progesterone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.1
-
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.2
-
phenylacetone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.6
-
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
3.9
-
progesterone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
5.2
-
progesterone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.1
-
progesterone
kcat_Km less than 0.1 1/sec*min, mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.2
-
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication; mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.4
-
progesterone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.5
-
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.7
-
progesterone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
1.8
-
progesterone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.1
-
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.2
-
phenylacetone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
2.6
-
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
3.9
-
progesterone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
5.2
-
progesterone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
Rhodococcus rhodochrous
Other publictions for EC 1.14.13.54
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)
728352
Swizdor
Baeyer-Villiger oxidation of s ...
Penicillium lanosocoeruleum
Molecules
18
13812-13822
2013
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3
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-
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1
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-
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2
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2
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-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
727906
Franceschini
Exploring the structural basis ...
Rhodococcus rhodochrous
J. Biol. Chem.
287
22626-22634
2012
-
-
1
1
5
-
-
5
-
-
-
1
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
6
-
-
-
2
-
-
-
-
-
1
2
1
5
-
-
-
-
5
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
11
11
693956
Virus
Molecular evolution of a stero ...
Bacillus megaterium
Lipids
43
1133-1141
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
2
-
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1
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1
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-
2
-
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-
-
-
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-
-
-
-
-
-
-
-
-
659076
Morii
Steroid monooxygenase of Rhodo ...
Rhodococcus rhodochrous
J. Biochem.
126
624-631
1999
-
-
1
-
-
-
-
2
-
-
3
1
-
5
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
2
-
-
3
1
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7389
Itagaki
Studies on steroid monooxygena ...
Ilyonectria destructans, Ilyonectria destructans ATTC 11011
J. Biochem.
99
825-832
1986
-
-
-
-
-
-
5
5
-
-
-
-
-
5
-
-
-
-
-
-
1
-
10
-
1
-
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
5
-
-
-
-
-
-
-
-
-
-
1
-
10
-
1
-
1
-
2
1
-
-
-
-
-
-
-
-
7390
Itagaki
Studies on steroid monooxygena ...
Ilyonectria destructans, Ilyonectria destructans ATTC 11011
J. Biochem.
99
815-824
1986
-
-
-
-
-
-
-
3
-
-
2
-
-
5
-
-
1
-
-
1
-
1
17
1
-
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
2
-
-
-
-
1
-
1
-
1
17
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-