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show all sequences of 1.2.2.4

The redox centers in the molybdo iron-sulfur flavoprotein CO dehydrogenase from the thermophilic carboxidotrophic bacterium Pseudomonas thermocarboxydovorans

Hanzelmann, P.; Hofmann, B.; Meisen, S.; Meyer, O.; FEMS Microbiol. Lett. 176, 139-145 (1999)
No PubMed abstract available

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mo5+
1.9 mol per mol of enzyme dimer, a 1:1 mononuclear complex of molybdopterin-cytosine dinucleotide and the Mo ion
Pseudomonas thermocarboxydovorans
[2Fe-2S]-center
6.9 mol per mol of enzyme dimer, type I and type II [2Fe-2S]-centers
Pseudomonas thermocarboxydovorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
140000
-
2 * 140000, SDS-PAGE
Pseudomonas thermocarboxydovorans
279000
-
PAGE
Pseudomonas thermocarboxydovorans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas thermocarboxydovorans
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
molybdoironflavoprotein
-
Pseudomonas thermocarboxydovorans
Subunits
Subunits
Commentary
Organism
dimer
2 * 140000, SDS-PAGE
Pseudomonas thermocarboxydovorans
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
2.2 mol per mol of enzyme dimer
Pseudomonas thermocarboxydovorans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
2.2 mol per mol of enzyme dimer
Pseudomonas thermocarboxydovorans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mo5+
1.9 mol per mol of enzyme dimer, a 1:1 mononuclear complex of molybdopterin-cytosine dinucleotide and the Mo ion
Pseudomonas thermocarboxydovorans
[2Fe-2S]-center
6.9 mol per mol of enzyme dimer, type I and type II [2Fe-2S]-centers
Pseudomonas thermocarboxydovorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
140000
-
2 * 140000, SDS-PAGE
Pseudomonas thermocarboxydovorans
279000
-
PAGE
Pseudomonas thermocarboxydovorans
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
molybdoironflavoprotein
-
Pseudomonas thermocarboxydovorans
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 140000, SDS-PAGE
Pseudomonas thermocarboxydovorans
Other publictions for EC 1.2.2.4
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)
698576
Swingley
The complete genome sequence o ...
Roseobacter denitrificans OCh 114
J. Bacteriol.
189
683-690
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1
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1
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673552
Su
Three mammalian cytochromes b5 ...
Homo sapiens, Mus musculus, Rattus norvegicus
FEBS J.
273
3722-3734
2006
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1
-
21
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3
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3
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1
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21
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2
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656481
Hanzelmann
The effect of intracellular mo ...
Hydrogenophaga pseudoflava
J. Mol. Biol.
301
1221-1235
2000
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2
1
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4
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2
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390482
Dobbek
Crystal structure and mechanis ...
Oligotropha carboxidovorans
Proc. Natl. Acad. Sci. USA
96
8884-8889
1999
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-
-
1
-
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3
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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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3
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1
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1
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390483
Kang
Cloning and molecular characte ...
Hydrogenophaga pseudoflava
J. Bacteriol.
181
5581-5590
1999
-
-
1
-
-
-
-
-
-
2
3
-
-
2
-
1
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1
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1
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1
1
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2
3
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1
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1
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655594
Hanzelmann
-
The redox centers in the molyb ...
Pseudomonas thermocarboxydovorans
FEMS Microbiol. Lett.
176
139-145
1999
-
-
-
-
-
-
-
-
-
2
2
-
-
1
-
1
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-
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1
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1
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1
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2
2
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1
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1
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11606
Jacobitz
Removal of CO dehydrogenase fr ...
Oligotropha carboxidovorans
J. Bacteriol.
171
6294-6299
1989
-
-
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3
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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11607
Meyer
-
Biochemistry, and physiology o ...
Hydrogenibacillus schlegelii, Hydrogenophaga pseudoflava, Oligotropha carboxidovorans, Pseudomonas carboxydohydrogena, Pseudomonas thermocarboxydovorans
FEMS Microbiol. Rev.
39
161-179
1986
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2
2
9
14
5
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5
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10
3
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8
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8
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2
2
9
14
5
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10
3
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