BRENDA - Enzyme Database
show all sequences of 1.18.1.3

Purification and characterisation of the NADH acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWWO of Pseudomonas putida mt-2

Shaw, J.; Harayama, S.; Eur. J. Biochem. 209, 51-61 (1992)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
gel filtration
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
P21394
enzyme acts as reductase component of xylene monooxygenase, EC 1.18.1.3
-
Purification (Commentary)
Commentary
Organism
electron-transfer component XylA
Pseudomonas putida
Subunits
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
1 mol/mol enzyme. The electron flow is from NADH to FAD to [2Fe-2S]
Pseudomonas putida
NADH
electron-transfer component XylA. The electron flow is from NADH to FAD to [2Fe-2S]
Pseudomonas putida
[2Fe-2S]-center
protein contains 2 mol/mol of non-haem iron and 2 mol/mol of acid-labile sulfide. The electron flow is from NADH to FAD to [2Fe-2S]
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
1 mol/mol enzyme. The electron flow is from NADH to FAD to [2Fe-2S]
Pseudomonas putida
NADH
electron-transfer component XylA. The electron flow is from NADH to FAD to [2Fe-2S]
Pseudomonas putida
[2Fe-2S]-center
protein contains 2 mol/mol of non-haem iron and 2 mol/mol of acid-labile sulfide. The electron flow is from NADH to FAD to [2Fe-2S]
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
gel filtration
Pseudomonas putida
Purification (Commentary) (protein specific)
Commentary
Organism
electron-transfer component XylA
Pseudomonas putida
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Pseudomonas putida
Other publictions for EC 1.18.1.3
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)
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745340
Chowdhury
Reduction of flavodoxin by el ...
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745970
Wang
The role of Rnf in ion gradie ...
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e1919
2016
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744269
Nishizawa
Complete pyridine-nucleotide- ...
Acidovorax sp. KKS102
Biochem. J.
462
257-265
2014
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727962
Hess
The ferredoxin: NAD+ oxidoredu ...
Acetobacterium woodii, Acetobacterium woodii DSM 103
J. Biol. Chem.
288
31496-31502
2013
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728235
Tremblay
The Rnf complex of Clostridium ...
Clostridium ljungdahlii, Clostridium ljungdahlii DSM 13528
mBio
4
e00406
2012
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4
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746333
Dutta
-
Purification and properties o ...
Pseudomonas chlororaphis subsp. aureofaciens
Process Biochem.
47
1263-1267
2012
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1
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1
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1
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1
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706994
Umeda
Crystallization and preliminar ...
Novosphingobium sp., Novosphingobium sp. KA1
Acta Crystallogr. Sect. F
66
712-714
2010
-
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1
1
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1
1
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684177
Peng
Crystallization and preliminar ...
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
Acta Crystallogr. Sect. F
63
422-425
2007
-
-
1
1
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1
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2
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11
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1
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4
1
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1
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684179
Senda
Crystallization and preliminar ...
Acidovorax sp.
Acta Crystallogr. Sect. F
63
520-523
2007
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1
1
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1
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658218
Zanno
MT FdR: a ferredoxin reductase ...
Mycobacterium tuberculosis
Biochim. Biophys. Acta
1707
157-169
2005
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1
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2
1
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1
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673520
Sielaff
Kinetic and binding studies wi ...
Mycobacterium sp., Mycobacterium sp. HE5
FEBS J.
272
1148-1159
2005
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2
3
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1
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6
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675830
Sielaff
Analysis of the nearly identic ...
Mycobacterium sp., Mycobacterium sp. HE5
Microbiology
151
2593-2603
2005
-
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2
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3
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2
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2
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1
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1
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2
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2
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658575
Hussain
-
Ferredoxin reductase enhances ...
Streptomyces coelicolor
ENZYME MICROB. TECHNOL.
32
790-800
2003
-
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1
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437852
Senda
Crystal structure of NADH-depe ...
Pseudomonas sp.
J. Mol. Biol.
304
397-410
2000
-
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1
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5
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437854
Shen
-
Biochemical basis for carbon m ...
Butyribacterium methylotrophicum
Appl. Microbiol. Biotechnol.
51
827-832
1999
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285290
Broadus
Purification and characterizat ...
Pseudomonas sp., Pseudomonas sp. LB400
Arch. Microbiol.
170
106-112
1998
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2
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2
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11
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1
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9
1
1
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9
1
1
1
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744831
Shaw
Purification and characterisa ...
Pseudomonas putida
Eur. J. Biochem.
209
51-61
1992
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745194
Suzuki
Primary structure of xylene m ...
Pseudomonas putida
J. Bacteriol.
173
1690-1695
1991
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1
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437842
Haigler
Purification and properties of ...
Pseudomonas sp., Pseudomonas sp. NCIB 9816
J. Bacteriol.
172
457-464
1990
-
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5
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3
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2
10
1
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437844
Chen
Isolation, characterization, a ...
Methylosinus trichosporium OB3b
J. Bacteriol.
171
5012-5016
1989
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1
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7
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437845
Lovitt
Ethanol production by thermoph ...
Thermoanaerobacter thermohydrosulfuricus
J. Bacteriol.
170
2809-2815
1988
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437846
Subramanian
Purification and properties of ...
Pseudomonas putida
J. Biol. Chem.
256
2723-2730
1981
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3
2
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2
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1
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2
5
1
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2
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1
2
5
1
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1
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437847
Blusson
A new, fast, and sensitive ass ...
Clostridium pasteurianum, Clostridium tyrobutyricum, Clostridium tyrobutyricum CNRZ 510
Anal. Biochem.
110
176-181
1981
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3
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437848
Lamed
Ethanol production by thermoph ...
Hungateiclostridium thermocellum, Thermoanaerobacter brockii
J. Bacteriol.
144
569-578
1980
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437849
Petitdemange
Study of the NADH and NADPH-fe ...
Clostridium acetobutylicum
Can. J. Microbiol.
23
152-160
1977
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1
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437850
Petitdemange
Regulation of the NADH and NAD ...
Clostridium acetobutylicum, Clostridium pasteurianum, Clostridium tyrobutyricum
Biochim. Biophys. Acta
421
334-347
1976
3
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6
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437851
Jungermann
Function of reduced pyridine n ...
Clostridium butyricum, Clostridium pasteurianum
Biochim. Biophys. Acta
305
268-280
1973
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437843
Jungermann
Demonstration of NADH-ferredox ...
Clostridium butyricum, Clostridium kluyveri, Clostridium pasteurianum
Arch. Mikrobiol.
80
370-372
1971
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