BRENDA - Enzyme Database show
show all sequences of 1.14.13.69

Alkene monooxygenase from Xanthobacter strain Py2. Purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes

Small, F.J.; Ensign, S.A.; J. Biol. Chem. 272, 24913-24920 (1997)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
propyne
mechanism-based inactivator of the 21200 Da protein
Xanthobacter sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, 2. a 13300 Da ferredoxin containing a Rieske-type 2Fe-2S cluster, 3. a 11000 Da monomeric protein that contains no detectable cofactors, 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron. The physiological electron acceptor for the reductase is the Rieske-type ferredoxin, which is proposed to be an intermediate electron carrier between the reductase and terminal catalytic component of the system
Xanthobacter sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
propene + NADH + H+ + O2
Xanthobacter sp.
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
1,2-epoxypropane + NAD+ + H2O
-
-
?
propene + NADH + H+ + O2
Xanthobacter sp. Py2
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
1,2-epoxypropane + NAD+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Xanthobacter sp.
-
-
-
Xanthobacter sp. Py2
-
-
-
Purification (Commentary)
Commentary
Organism
-
Xanthobacter sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Xanthobacter sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
propene + NADH + H+ + O2
-
285342
Xanthobacter sp.
1,2-epoxypropane + NAD+ + H2O
-
285342
Xanthobacter sp.
?
propene + NADH + H+ + O2
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
285342
Xanthobacter sp.
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
-
285342
Xanthobacter sp. Py2
1,2-epoxypropane + NAD+ + H2O
-
285342
Xanthobacter sp. Py2
?
propene + NADH + H+ + O2
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
285342
Xanthobacter sp. Py2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, mass spectrometry 2. a dimeric ferredoxin consisting of two 13300 Da subunits, each containing a Rieske-type 2Fe-2S cluster, SDS-PAGE 3. a 11000 Da monomeric protein that contains no detectable cofactors, mass spectrometry 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron
Xanthobacter sp.
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
the 35500 Da NADH reductase component contains 1 mol of FAD
Xanthobacter sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
the 35500 Da NADH reductase component contains 1 mol of FAD
Xanthobacter sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
propyne
mechanism-based inactivator of the 21200 Da protein
Xanthobacter sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, 2. a 13300 Da ferredoxin containing a Rieske-type 2Fe-2S cluster, 3. a 11000 Da monomeric protein that contains no detectable cofactors, 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron. The physiological electron acceptor for the reductase is the Rieske-type ferredoxin, which is proposed to be an intermediate electron carrier between the reductase and terminal catalytic component of the system
Xanthobacter sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
propene + NADH + H+ + O2
Xanthobacter sp.
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
1,2-epoxypropane + NAD+ + H2O
-
-
?
propene + NADH + H+ + O2
Xanthobacter sp. Py2
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
1,2-epoxypropane + NAD+ + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Xanthobacter sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Xanthobacter sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
propene + NADH + H+ + O2
-
285342
Xanthobacter sp.
1,2-epoxypropane + NAD+ + H2O
-
285342
Xanthobacter sp.
?
propene + NADH + H+ + O2
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
285342
Xanthobacter sp.
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
-
285342
Xanthobacter sp. Py2
1,2-epoxypropane + NAD+ + H2O
-
285342
Xanthobacter sp. Py2
?
propene + NADH + H+ + O2
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
285342
Xanthobacter sp. Py2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, mass spectrometry 2. a dimeric ferredoxin consisting of two 13300 Da subunits, each containing a Rieske-type 2Fe-2S cluster, SDS-PAGE 3. a 11000 Da monomeric protein that contains no detectable cofactors, mass spectrometry 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron
Xanthobacter sp.
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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7
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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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7
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2
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1
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1
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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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677851
Mattes
Mechanism controlling the exte ...
Nocardioides sp., Nocardioides sp. JS614 / ATCC BAA-499
Arch. Microbiol.
187
217-226
2007
1
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1
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1
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6
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8
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6
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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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3
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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
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1
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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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658683
Fosdike
Adventitious reactions of alke ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276
FEBS J.
272
2661-2669
2005
1
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2
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1
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2
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9
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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
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1
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3
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1
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1
1
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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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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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285341
Zhou
The alkene monooxygenase from ...
Xanthobacter sp., Xanthobacter sp. Py2
Appl. Environ. Microbiol.
65
1589-1595
1999
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2
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14
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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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285337
Gallagher
Alkene monooxygenase from Noca ...
Gordonia rubripertincta, Gordonia rubripertincta B-276
Eur. J. Biochem.
247
635-641
1997
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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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285336
Ensign
Aliphatic and chlorinated alke ...
Xanthobacter sp., Xanthobacter sp. Py2
Appl. Environ. Microbiol.
62
61-66
1996
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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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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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285334
Habets-Cruetzen
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Inactivation of alkene oxidati ...
Mycobacterium sp., Mycobacterium sp. E20, Mycobacterium sp. E3
Appl. Microbiol. Biotechnol.
22
428-433
1985
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