BRENDA - Enzyme Database show
show all sequences of 1.14.13.69

Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions

Champreda, V.; Choi, Y.J.; Zhou, N.Y.; Leak, D.J.; Appl. Microbiol. Biotechnol. 71, 840-847 (2006)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
AamD
the enzyme requires interaction with the small catalytic coupling/effector protein, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling
Xanthobacter autotrophicus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
the enzyme is a non-heme diiron monooxygenase and contains a Rieske-type ferredoxin
Xanthobacter autotrophicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Xanthobacter autotrophicus
O87082
gene xamoA, oxygenase alpha subunitgene xamoA
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Xanthobacter autotrophicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-styrene oxide + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
(S)-styrene oxide + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
2-cresol + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
3-cresol + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
4-cresol + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
additional information
the enzyme catalyses the asymmetric epoxidation of a broad range of alkenes, stereo- and regioselectivity, residues Asn34 and Arg57 are involved, AMO requires a small catalytic coupling/effector protein, AamD, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview
671530
Xanthobacter autotrophicus
?
-
-
-
-
toluene + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the enzyme contains NADH-oxidoreductase and a Rieske-type ferredoxin components and the binuclear non-haem iron active site, it requires a small catalytic coupling/effector protein, AamD
Xanthobacter autotrophicus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Xanthobacter autotrophicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Xanthobacter autotrophicus
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the enzyme contains a Rieske-type ferredoxin. AMO requires a small catalytic coupling/effector protein, AamD, the coupling protein cannot or very poorly be substituted by coupling proteins of AMOs of other species, e.g. IsoD from Rhodococcus sp. strain AD45, or PmoB from Mycobacterium sp. strain M156, substitution with IsoD changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview
Xanthobacter autotrophicus
NADH
-
Xanthobacter autotrophicus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
AamD
the enzyme requires interaction with the small catalytic coupling/effector protein, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling
Xanthobacter autotrophicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the enzyme contains a Rieske-type ferredoxin. AMO requires a small catalytic coupling/effector protein, AamD, the coupling protein cannot or very poorly be substituted by coupling proteins of AMOs of other species, e.g. IsoD from Rhodococcus sp. strain AD45, or PmoB from Mycobacterium sp. strain M156, substitution with IsoD changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview
Xanthobacter autotrophicus
NADH
-
Xanthobacter autotrophicus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
the enzyme is a non-heme diiron monooxygenase and contains a Rieske-type ferredoxin
Xanthobacter autotrophicus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Xanthobacter autotrophicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-styrene oxide + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
(S)-styrene oxide + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
2-cresol + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
3-cresol + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
4-cresol + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
additional information
the enzyme catalyses the asymmetric epoxidation of a broad range of alkenes, stereo- and regioselectivity, residues Asn34 and Arg57 are involved, AMO requires a small catalytic coupling/effector protein, AamD, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview
671530
Xanthobacter autotrophicus
?
-
-
-
-
toluene + NADH + H+ + O2
-
671530
Xanthobacter autotrophicus
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme contains NADH-oxidoreductase and a Rieske-type ferredoxin components and the binuclear non-haem iron active site, it requires a small catalytic coupling/effector protein, AamD
Xanthobacter autotrophicus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Xanthobacter autotrophicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Xanthobacter autotrophicus
Other publictions for EC 1.14.13.69
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)
728009
Saitoh
Genomic sequencing-based detec ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276
J. Biosci. Bioeng.
116
309-312
2013
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-
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2
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7
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2
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1
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2
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703485
Chuang
Proteomic analysis of ethene-e ...
Nocardioides sp. JS614
Environ. Sci. Technol.
44
1594-1601
2010
-
-
-
-
-
-
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1
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-
3
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710973
Taylor
Extending the alkene substrate ...
Nocardioides sp., Nocardioides sp. JS614 / ATCC BAA-499
Appl. Microbiol. Biotechnol.
87
2293-2302
2010
-
-
-
-
-
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2
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7
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1
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2
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2
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1
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2
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-
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1
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-
1
-
-
698495
Lara
Oxidative enzymatic alkene cle ...
Trametes hirsuta
J. Am. Chem. Soc.
131
5368-5369
2009
-
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1
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1
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1
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1
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-
677851
Mattes
Mechanism controlling the exte ...
Nocardioides sp., Nocardioides sp. JS614 / ATCC BAA-499
Arch. Microbiol.
187
217-226
2007
1
-
1
-
-
-
1
-
-
-
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6
-
8
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2
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6
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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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6
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2
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6
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-
671530
Champreda
Alteration of the stereo- and ...
Xanthobacter autotrophicus
Appl. Microbiol. Biotechnol.
71
840-847
2006
1
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1
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3
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1
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7
1
1
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1
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2
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1
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1
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1
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7
1
1
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1
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674944
Perry
Protocol for mutagenesis of al ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276
J. Biomol. Screen.
11
553-556
2006
-
-
1
-
1
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1
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5
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4
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1
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1
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1
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1
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4
-
1
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-
658683
Fosdike
Adventitious reactions of alke ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276
FEBS J.
272
2661-2669
2005
1
-
-
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-
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2
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1
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2
-
9
-
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1
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1
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4
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1
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1
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1
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2
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1
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2
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1
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1
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4
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658775
Champreda
Heterologous expression of alk ...
Xanthobacter autotrophicus
FEMS Microbiol. Lett.
239
309-318
2004
-
-
1
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1
3
1
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4
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1
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1
1
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1
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1
1
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1
3
1
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1
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1
1
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-
-
-
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-
-
-
285335
Gallagher
Electron transfer reactions in ...
Gordonia rubripertincta, Gordonia rubripertincta B-276
Biochem. J.
339
79-85
1999
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-
-
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2
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4
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2
1
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1
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1
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2
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2
1
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285338
Saeki
Degradation of trichloroethene ...
Gordonia rubripertincta, Gordonia rubripertincta B-276, Rhodococcus ruber, Xanthobacter sp., Xanthobacter sp. Py2
Microbiology
145
1721-1730
1999
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2
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23
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9
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2
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9
-
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285341
Zhou
The alkene monooxygenase from ...
Xanthobacter sp., Xanthobacter sp. Py2
Appl. Environ. Microbiol.
65
1589-1595
1999
-
-
-
-
-
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2
-
5
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-
14
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2
1
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2
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5
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2
1
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-
285339
Zhou
The alkene monooxygenase from ...
Xanthobacter sp., Xanthobacter sp. Py2
FEBS Lett.
430
181-185
1998
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1
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12
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2
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1
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2
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-
-
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-
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285337
Gallagher
Alkene monooxygenase from Noca ...
Gordonia rubripertincta, Gordonia rubripertincta B-276
Eur. J. Biochem.
247
635-641
1997
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2
1
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1
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2
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6
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1
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4
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1
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1
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2
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1
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1
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4
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285342
Small
Alkene monooxygenase from Xant ...
Xanthobacter sp., Xanthobacter sp. Py2
J. Biol. Chem.
272
24913-24920
1997
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1
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1
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2
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15
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1
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4
1
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1
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2
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1
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1
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4
1
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-
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285336
Ensign
Aliphatic and chlorinated alke ...
Xanthobacter sp., Xanthobacter sp. Py2
Appl. Environ. Microbiol.
62
61-66
1996
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2
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13
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10
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2
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10
-
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285343
Zhou
-
Cloning and expression of the ...
Xanthobacter sp., Xanthobacter sp. Py2
Appl. Microbiol. Biotechnol.
44
582-588
1996
-
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1
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11
-
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2
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1
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2
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285340
Hartmans
Alkene monooxygenase from Myco ...
Mycobacterium sp., Mycobacterium sp. E3, Mycolicibacterium aurum, Mycolicibacterium aurum L1
J. Gen. Microbiol.
137
2555-2560
1991
-
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4
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7
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4
2
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4
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4
2
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285334
Habets-Cruetzen
-
Inactivation of alkene oxidati ...
Mycobacterium sp., Mycobacterium sp. E20, Mycobacterium sp. E3
Appl. Microbiol. Biotechnol.
22
428-433
1985
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1
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4
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3
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1
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3
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