BRENDA - Enzyme Database show
show all sequences of 1.17.9.1

Purification and characterization of active site components of the putative p-cresol methylhydroxylase membrane complex from Geobacter metallireducens

Johannes, J.; Bluschke, A.; Jehmlich, N.; von Bergen, M.; Boll, M.; J. Bacteriol. 190, 6493-6500 (2008)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
4-Hydroxybenzyl alcohol
mixed-type inhibition of 4-cresol oxidation
Geobacter metallireducens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0017
-
4-Cresol
-
Geobacter metallireducens
0.0027
-
4-Hydroxybenzyl alcohol
-
Geobacter metallireducens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
a tightly membrane-bound PCMH complex exists in anaerobic organisms in contrast to aerobic ones, where the enzyme is soluble and periplasmic, nevertheless the membrane complex has soluble components, overview
Geobacter metallireducens
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
cytochrome c-containing enzyme
Geobacter metallireducens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4-cresol + 2 acceptor + H2O
Geobacter metallireducens
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
4-hydroxybenzaldehyde + 2 reduced acceptor
-
-
?
4-hydroxybenzyl alcohol + acceptor
Geobacter metallireducens
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
4-hydroxybenzaldehyde + reduced acceptor
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Geobacter metallireducens
-
-
-
Purification (Commentary)
Commentary
Organism
380fold purification of the soluble components including the active site of the enzyme membrane complex by membrane preparation, solubilization of the complex with lauryldimethylamine N-oxide, gel filtration, and hydrophobic interaction chromatography
Geobacter metallireducens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
2.2
-
purified soluble components including the active site of the enzyme membrane complex
Geobacter metallireducens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-cresol + 2 acceptor + H2O
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + 2 reduced acceptor
-
-
-
?
4-cresol + Fe3+ + H2O
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + Fe2+
-
-
-
?
4-hydroxybenzyl alcohol + acceptor
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-hydroxybenzyl alcohol + Fe3+ + H2O
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + Fe2+
-
-
-
?
additional information
functional modelling, overview
687426
Geobacter metallireducens
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
the enzyme complex shows a unique alphaalpha'beta2 subunit composition, with alpha and alpha' representing isoforms of the FAD-containing subunit and beta representing a c-type cytochrome
Geobacter metallireducens
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome
the enzyme complex shows a a unique alphaalpha'beta2 subunit composition, with beta representing a c-type cytochrome
Geobacter metallireducens
FAD
the enzyme complex shows a unique alphaalpha'beta2 subunit composition, with alpha and alpha' representing isoforms of the FAD-containing subunit, one FAD is covalently linked to Tyr394 of the alpha subunit. In contrast, the alpha' subunit does not contain any FAD cofactor and is therefore considered to be catalytically inactive
Geobacter metallireducens
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.018
-
4-Hydroxybenzyl alcohol
competitive inhibition
Geobacter metallireducens
0.235
-
4-Hydroxybenzyl alcohol
uncompetitive inhibition
Geobacter metallireducens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome
the enzyme complex shows a a unique alphaalpha'beta2 subunit composition, with beta representing a c-type cytochrome
Geobacter metallireducens
FAD
the enzyme complex shows a unique alphaalpha'beta2 subunit composition, with alpha and alpha' representing isoforms of the FAD-containing subunit, one FAD is covalently linked to Tyr394 of the alpha subunit. In contrast, the alpha' subunit does not contain any FAD cofactor and is therefore considered to be catalytically inactive
Geobacter metallireducens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-Hydroxybenzyl alcohol
mixed-type inhibition of 4-cresol oxidation
Geobacter metallireducens
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.018
-
4-Hydroxybenzyl alcohol
competitive inhibition
Geobacter metallireducens
0.235
-
4-Hydroxybenzyl alcohol
uncompetitive inhibition
Geobacter metallireducens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0017
-
4-Cresol
-
Geobacter metallireducens
0.0027
-
4-Hydroxybenzyl alcohol
-
Geobacter metallireducens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
a tightly membrane-bound PCMH complex exists in anaerobic organisms in contrast to aerobic ones, where the enzyme is soluble and periplasmic, nevertheless the membrane complex has soluble components, overview
Geobacter metallireducens
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
cytochrome c-containing enzyme
Geobacter metallireducens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4-cresol + 2 acceptor + H2O
Geobacter metallireducens
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
4-hydroxybenzaldehyde + 2 reduced acceptor
-
-
?
4-hydroxybenzyl alcohol + acceptor
Geobacter metallireducens
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
4-hydroxybenzaldehyde + reduced acceptor
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
380fold purification of the soluble components including the active site of the enzyme membrane complex by membrane preparation, solubilization of the complex with lauryldimethylamine N-oxide, gel filtration, and hydrophobic interaction chromatography
Geobacter metallireducens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
2.2
-
purified soluble components including the active site of the enzyme membrane complex
Geobacter metallireducens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-cresol + 2 acceptor + H2O
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + 2 reduced acceptor
-
-
-
?
4-cresol + Fe3+ + H2O
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + Fe2+
-
-
-
?
4-hydroxybenzyl alcohol + acceptor
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors, the in vivo function of PCMH is to oxidize both 4-cresol and 4-hydroxybenzyl alcohol
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-hydroxybenzyl alcohol + Fe3+ + H2O
PCMH catalyzes both the hydroxylation of 4-cresol to 4-hydroxybenzyl alcohol and the subsequent oxidation of the latter to 4-hydroxybenzaldehyde in the presence of artificial electron acceptors
687426
Geobacter metallireducens
4-hydroxybenzaldehyde + Fe2+
-
-
-
?
additional information
functional modelling, overview
687426
Geobacter metallireducens
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme complex shows a unique alphaalpha'beta2 subunit composition, with alpha and alpha' representing isoforms of the FAD-containing subunit and beta representing a c-type cytochrome
Geobacter metallireducens
Other publictions for EC 1.17.9.1
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)
744935
Chaurasia
Genetic evidence that the deg ...
Geobacter metallireducens
FEMS Microbiol. Lett.
362
fnv145
2015
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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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1
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-
-
-
-
726788
Chen
-
The catabolism of 2,4-xylenol ...
Pseudomonas putida
Appl. Microbiol. Biotechnol.
98
1349-1356
2014
-
-
1
-
-
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2
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1
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1
1
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744141
Chen
The catabolism of 2,4-xylenol ...
Pseudomonas putida, Pseudomonas putida NCIMB 9866
Appl. Microbiol. Biotechnol.
98
1349-1356
2014
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-
1
-
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4
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3
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1
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8
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1
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4
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1
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8
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1
1
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715044
Joesaar
Diversity of the transcription ...
Pseudomonas fluorescens, Pseudomonas fluorescens PC24
FEMS Microbiol. Ecol.
72
464-475
2010
-
1
1
-
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4
-
7
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4
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1
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2
2
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-
4
-
-
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-
-
-
-
-
4
-
-
-
-
-
2
-
-
-
2
2
4
3
-
-
687426
Johannes
Purification and characterizat ...
Geobacter metallireducens
J. Bacteriol.
190
6493-6500
2008
-
-
-
-
-
-
1
2
1
1
-
2
-
3
-
-
1
-
-
-
1
-
5
1
-
-
-
-
-
-
-
2
2
-
-
-
-
-
2
-
-
-
-
1
2
2
1
1
-
2
-
-
-
1
-
-
1
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
674335
Peters
Genes, enzymes, and regulation ...
Geobacter metallireducens
J. Bacteriol.
189
4729-4738
2007
-
-
-
-
-
-
-
-
1
1
-
2
-
4
-
-
-
-
-
-
2
-
6
1
1
-
-
-
1
-
-
6
-
-
-
-
-
-
6
-
-
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
2
-
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
658110
Cunane
p-Cresol methylhydroxylase: al ...
Pseudomonas putida
Biochemistry
44
2963-2973
2005
-
-
1
1
-
-
-
-
-
-
3
1
-
1
-
-
1
-
-
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2
1
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-
1
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1
1
1
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-
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3
1
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-
1
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-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
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658990
Efimov
Relationship between charge-tr ...
Pseudomonas putida
J. Am. Chem. Soc.
127
732-741
2005
-
-
1
-
-
-
-
-
-
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2
1
-
1
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1
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1
1
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2
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3
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1
3
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2
1
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1
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1
1
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-
2
-
-
-
-
-
-
-
-
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-
658018
Efimov
A study of the spectral and re ...
Pseudomonas putida
Biochemistry
43
10532-10546
2004
-
-
1
-
1
-
-
-
-
-
2
1
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1
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1
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1
1
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2
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1
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1
1
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1
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2
1
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1
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1
1
-
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2
-
-
-
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658077
Efimov
Insight into covalent flavinyl ...
Pseudomonas putida, Pseudomonas putida NCIMB 9869
Biochemistry
43
6138-6148
2004
-
-
1
-
1
-
-
-
-
-
2
2
-
2
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1
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2
1
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2
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1
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1
1
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1
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2
2
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1
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2
1
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2
-
-
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-
437885
Efimov
Effects of noncovalent and cov ...
Pseudomonas putida
Biochemistry
40
2155-2166
2001
-
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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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1
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1
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437882
Cunane
Structures of the flavocytochr ...
Pseudomonas putida
J. Mol. Biol.
295
357-374
2000
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1
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1
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3
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3
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2
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2
1
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1
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3
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437886
Cronin
Heterologous expression in Pse ...
Pseudomonas putida
Protein Expr. Purif.
19
74-83
2000
-
-
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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1
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1
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1
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437883
Engst
Properties of p-cresol methylh ...
Pseudomonas putida
Biochemistry
38
16620-16628
1999
-
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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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1
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1
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437884
Kim
The cytochrome subunit is nece ...
Pseudomonas putida
J. Biol. Chem.
270
31202-31209
1995
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1
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3
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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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1
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437876
Kim
Cloning, sequencing, and expre ...
Pseudomonas putida, Pseudomonas putida NCIB 9866, Pseudomonas putida NCIB 9869
J. Bacteriol.
176
6349-6361
1994
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1
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13
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1
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3
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2
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2
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3
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288313
Bossert
Anaerobic oxidation of p-creso ...
denitrifying bacterium, denitrifying bacterium PC-07
J. Bacteriol.
171
2956-2962
1989
-
-
-
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6
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1
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3
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1
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2
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14
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2
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2
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6
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1
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1
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2
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14
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-
437879
McIntire
Steady-state and stopped-flow ...
Pseudomonas putida, Pseudomonas putida NCIB 9869
Biochemistry
26
4107-4117
1987
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-
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7
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1
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4
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1
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4
-
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-
1
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-
437877
Shamala
Structure of an intermolecular ...
Pseudomonas putida
Proc. Natl. Acad. Sci. USA
83
4626-4630
1986
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-
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2
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1
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1
1
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2
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2
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2
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1
1
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-
437878
McIntire
Amino acid and sequence analys ...
Pseudomonas putida
Biochemistry
25
5975-5981
1986
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-
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2
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2
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1
1
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1
1
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-
437871
Hopper
Periplasmic location of p-cres ...
Pseudomonas putida
FEBS Lett.
182
485-488
1985
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-
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2
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1
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3
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2
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2
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1
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2
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437872
Bhattacharyya
Laser-flash-photolysis studies ...
Pseudomonas putida
Biochem. J.
228
337-345
1985
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-
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1
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1
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2
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2
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-
1
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-
437873
Shamala
Preliminary X-ray study of p-c ...
Pseudomonas putida
J. Mol. Biol.
183
517-518
1985
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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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-
437874
McIntire
p-Cresol methylhydroxylase. as ...
Pseudomonas putida
Biochem. J.
228
325-335
1985
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-
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-
7
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2
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21
-
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1
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1
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1
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7
-
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21
-
-
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-
1
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-
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-
437875
Koerber
Resolution of the flavocytochr ...
Pseudomonas putida
Biochemistry
24
5276-5280
1985
-
-
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2
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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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1
-
1
1
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-
437869
Causer
-
Azurin from Pseudomonas putida ...
Pseudomonas putida, Pseudomonas putida NCIB 9869
Biochem. Soc. Trans.
12
1131-1132
1984
-
-
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1
1
2
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7
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4
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1
1
2
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4
-
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437870
McIntire
Stereochemistry of 1-(4-hydrox ...
Pseudomonas putida
Biochem. J.
224
617-621
1984
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2
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2
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-
2
-
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-
437868
Hopper
Redox potential of the cytochr ...
Comamonas testosteroni, Comamonas testosteroni NCIB 8955, Pseudomonas alcaligenes, Pseudomonas alcaligenes NCIB 9867, Pseudomonas putida, Pseudomonas putida NCIB 9866, Pseudomonas putida NCIB 9869
FEBS Lett.
161
100-102
1983
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17
-
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7
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3
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3
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7
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437867
McIntire
8 alpha-(O-Tyrosyl)flavin aden ...
Pseudomonas putida
Biochemistry
20
3068-3075
1981
-
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2
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1
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1
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1
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-
1
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437866
McIntire
8 alpha-O-Tyrosyl-FAD: a new f ...
Pseudomonas putida
J. Biol. Chem.
255
6553-6555
1980
-
-
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1
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1
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3
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3
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1
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437865
Hopper
Incorporation of [18O]water in ...
Pseudomonas putida
Biochem. J.
175
345-347
1978
-
-
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2
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3
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3
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-
437880
Keat
p-Cresol and 3,5-xylenol methy ...
Pseudomonas putida, Pseudomonas putida NCIB 9869
Biochem. J.
175
649-658
1978
-
-
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4
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6
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8
-
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1
-
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-
3
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12
1
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4
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6
-
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1
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3
-
12
1
-
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-
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-
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-
-
-
-
-
-
437864
Hopper
The purification and propertie ...
Pseudomonas putida
Biochem. J.
167
155-162
1977
-
-
-
-
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5
-
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2
1
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2
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-
1
-
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1
1
8
1
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-
-
-
-
2
-
-
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-
-
-
2
-
-
-
-
-
-
5
-
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2
1
-
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-
1
-
-
1
1
8
1
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-