BRENDA - Enzyme Database show
show all sequences of 1.2.2.4

Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine

Dobbek, H.; Gremer, L.; Meyer, O.; Huber, R.; Proc. Natl. Acad. Sci. USA 96, 8884-8889 (1999)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
air-oxidized form
Oligotropha carboxidovorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17800
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
30200
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
88700
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oligotropha carboxidovorans
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
molybdoironflavoprotein
molybdenum with three oxygen ligands, molybdopterin-cytosine dinucleotide and S-selanylcysteine at active site
Oligotropha carboxidovorans
Reaction
Reaction
Commentary
Organism
CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561
mechanism, necessity of S-selanyl-cysteine for catalysis
Oligotropha carboxidovorans
Subunits
Subunits
Commentary
Organism
heterohexamer
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
air-oxidized form
Oligotropha carboxidovorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17800
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
30200
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
88700
-
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
molybdoironflavoprotein
molybdenum with three oxygen ligands, molybdopterin-cytosine dinucleotide and S-selanylcysteine at active site
Oligotropha carboxidovorans
Subunits (protein specific)
Subunits
Commentary
Organism
heterohexamer
2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
Oligotropha carboxidovorans
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
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673552
Su
Three mammalian cytochromes b5 ...
Homo sapiens, Mus musculus, Rattus norvegicus
FEBS J.
273
3722-3734
2006
-
-
1
-
21
-
-
-
-
-
3
-
-
3
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
21
-
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656481
Hanzelmann
The effect of intracellular mo ...
Hydrogenophaga pseudoflava
J. Mol. Biol.
301
1221-1235
2000
-
-
-
-
-
-
-
-
2
1
-
-
-
4
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390482
Dobbek
Crystal structure and mechanis ...
Oligotropha carboxidovorans
Proc. Natl. Acad. Sci. USA
96
8884-8889
1999
-
-
-
1
-
-
-
-
-
-
3
-
-
4
-
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390483
Kang
Cloning and molecular characte ...
Hydrogenophaga pseudoflava
J. Bacteriol.
181
5581-5590
1999
-
-
1
-
-
-
-
-
-
2
3
-
-
2
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
3
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655594
Hanzelmann
-
The redox centers in the molyb ...
Pseudomonas thermocarboxydovorans
FEMS Microbiol. Lett.
176
139-145
1999
-
-
-
-
-
-
-
-
-
2
2
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
2
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
11606
Jacobitz
Removal of CO dehydrogenase fr ...
Oligotropha carboxidovorans
J. Bacteriol.
171
6294-6299
1989
-
-
-
-
-
-
-
-
3
1
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
11607
Meyer
-
Biochemistry, and physiology o ...
Hydrogenibacillus schlegelii, Hydrogenophaga pseudoflava, Oligotropha carboxidovorans, Pseudomonas carboxydohydrogena, Pseudomonas thermocarboxydovorans
FEMS Microbiol. Rev.
39
161-179
1986
-
-
-
-
-
-
-
2
2
9
14
5
-
5
-
-
-
-
-
-
-
-
10
3
-
-
-
-
-
-
-
8
-
-
-
-
-
-
8
-
-
-
-
-
-
2
2
9
14
5
-
-
-
-
-
-
-
-
10
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-