BRENDA - Enzyme Database
show all sequences of 2.3.1.169

Reductive activation of the coenzyme A/acetyl-CoA isotopic exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by nitrous oxide and carbon monoxide

Lu, W.P.; Ragsdale, S.W.; J. Biol. Chem. 266, 3554-3564 (1991) View publication on PubMed

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
CO
two effects: stimulation and inhibition on CoA/acetylCoA exchange
Moorella thermoacetica
General Stability
General Stability
Organism
reactions in presence of DTT, since enzyme requires strictly anaerobic conditions for stability
Moorella thermoacetica
Inhibitors
Inhibitors
Commentary
Organism
Structure
CN-
inhibitor on the CoA/acetyl-CoA exchange, 98% inhibition at 1.2 mM
Moorella thermoacetica
CO
non-competitive inhibitor on the CoA/acetyl-CoA exchange, the Ni-Fe-C-center appears to be the inhibitor site for CO
Moorella thermoacetica
CO2
inhibitor on the CoA/acetyl-CoA exchange
Moorella thermoacetica
dephospho-CoA
inhibitor on the CoA/acetyl-CoA exchange, 75% inhibition at 0.44 mM
Moorella thermoacetica
desulfo-CoA
inhibitor on the CoA/acetyl-CoA exchange, 30% mM at 2.1 mM
Moorella thermoacetica
N2O
inhibitor on the CoA/acetyl-CoA exchange
Moorella thermoacetica
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
corrinoid/iron-sulfur protein required
Moorella thermoacetica
Fe
the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex
Moorella thermoacetica
Ni
the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex
Moorella thermoacetica
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
150000
-
-
Moorella thermoacetica
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Moorella thermoacetica
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
?
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Moorella thermoacetica
-
-
-
Reaction
Reaction
Commentary
Organism
Reaction ID
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
pathway
Moorella thermoacetica
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
Enzyme accepts the methyl group from the methylated corrinoid/iron-sulfur protein, binds a carbonyl group from CO, CO2, or the carboxyl of pyruvate, and binds coenzyme A. Then the enzyme catalyses the synthesis of acetyl-CoA from these enzyme bound groups. Additionally the enzyme catalyses two exchange reactions between the methylated corrinoid/iron-sulfur protein and methylated enzyme and between methylated enzyme and the methyl moiety of acetyl-CoA.
Moorella thermoacetica
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the enzyme-bound complex is an [NiFe3-4S4]-acetyl complex
Moorella thermoacetica
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
28
-
40°C, CoA/acetyl-CoA exchange
Moorella thermoacetica
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
under anaerobic conditions
390475
Moorella thermoacetica
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
390475
Moorella thermoacetica
?
CO + methyl-X + HS-CoA
-
390475
Moorella thermoacetica
CH3-CO-S-CoA + HX
-
390475
Moorella thermoacetica
?
additional information
enzyme catalyses the CoA/acetyl-CoA exchange
390475
Moorella thermoacetica
?
-
-
-
?
additional information
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
390475
Moorella thermoacetica
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
alpha,beta
Moorella thermoacetica
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Moorella thermoacetica
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.7
7
optimum for CoA/acetyl-CoA exchange
Moorella thermoacetica
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
CO
pH 7.0, 25°C, under anaerobic conditions, noncompetitive with respect to acetyl-CoA
Moorella thermoacetica
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
CO
two effects: stimulation and inhibition on CoA/acetylCoA exchange
Moorella thermoacetica
General Stability (protein specific)
General Stability
Organism
reactions in presence of DTT, since enzyme requires strictly anaerobic conditions for stability
Moorella thermoacetica
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CN-
inhibitor on the CoA/acetyl-CoA exchange, 98% inhibition at 1.2 mM
Moorella thermoacetica
CO
non-competitive inhibitor on the CoA/acetyl-CoA exchange, the Ni-Fe-C-center appears to be the inhibitor site for CO
Moorella thermoacetica
CO2
inhibitor on the CoA/acetyl-CoA exchange
Moorella thermoacetica
dephospho-CoA
inhibitor on the CoA/acetyl-CoA exchange, 75% inhibition at 0.44 mM
Moorella thermoacetica
desulfo-CoA
inhibitor on the CoA/acetyl-CoA exchange, 30% mM at 2.1 mM
Moorella thermoacetica
N2O
inhibitor on the CoA/acetyl-CoA exchange
Moorella thermoacetica
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
CO
pH 7.0, 25°C, under anaerobic conditions, noncompetitive with respect to acetyl-CoA
Moorella thermoacetica
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
corrinoid/iron-sulfur protein required
Moorella thermoacetica
Fe
the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex
Moorella thermoacetica
Ni
the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex
Moorella thermoacetica
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
150000
-
-
Moorella thermoacetica
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Moorella thermoacetica
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
?
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
28
-
40°C, CoA/acetyl-CoA exchange
Moorella thermoacetica
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
under anaerobic conditions
390475
Moorella thermoacetica
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
390475
Moorella thermoacetica
?
CO + methyl-X + HS-CoA
-
390475
Moorella thermoacetica
CH3-CO-S-CoA + HX
-
390475
Moorella thermoacetica
?
additional information
enzyme catalyses the CoA/acetyl-CoA exchange
390475
Moorella thermoacetica
?
-
-
-
?
additional information
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
390475
Moorella thermoacetica
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
alpha,beta
Moorella thermoacetica
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Moorella thermoacetica
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.7
7
optimum for CoA/acetyl-CoA exchange
Moorella thermoacetica
Other publictions for EC 2.3.1.169
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
Synonyms
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)
758239
Adam
Evolutionary history of carbo ...
bacterium, archaeon
Proc. Natl. Acad. Sci. USA
115
E1166-E1173
2018
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736020
Ali
Physiological characterization ...
Candidatus Jettenia caeni
Environ. Microbiol.
17
2172-2189
2015
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728242
Zhu
Structural and functional inve ...
Clostridioides difficile, Clostridioides difficile 630
Metallomics
5
551-558
2013
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736683
Chmielowska
Redox potentials and protonati ...
Carboxydothermus hydrogenoformans
J. Phys. Chem. A
117
12484-12496
2013
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719744
Matschiavelli
Function and regulation of iso ...
Methanosarcina acetivorans
J. Bacteriol.
194
5377-5387
2012
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714240
Bender
Evidence that ferredoxin inter ...
Moorella thermoacetica
Biochemistry
50
276-286
2011
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1
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720372
Grahame
Methods for analysis of acetyl ...
Carboxydothermus hydrogenoformans
Methods Enzymol.
494
189-217
2011
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719862
Gencic
Tight coupling of partial reac ...
Carboxydothermus hydrogenoformans, Methanosarcina thermophila, Carboxydothermus hydrogenoformans DSM 6008, Methanosarcina thermophila TM-1
J. Biol. Chem.
285
15450-15463
2010
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3
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6
6
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696351
Kung
Crystallographic snapshots of ...
Moorella thermoacetica
Biochemistry
48
7432-7440
2009
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696354
Volbeda
Novel domain arrangement in th ...
Moorella thermoacetica
Biochemistry
48
7916-7926
2009
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700996
Ito
Dinuclear nickel complexes mod ...
synthetic construct
Proc. Natl. Acad. Sci. USA
106
11862-11866
2009
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685228
Doukov
Xenon in and at the end of the ...
Moorella thermoacetica
Biochemistry
47
3474-3483
2008
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687803
Seravalli
Pulse-chase studies of the syn ...
Moorella thermoacetica
J. Biol. Chem.
283
8384-8394
2008
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687824
Tan
Tunnel mutagenesis and Ni-depe ...
Moorella thermoacetica
J. Biol. Inorg. Chem.
13
771-778
2008
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672199
Bramlett
Moessbauer and EPR study of re ...
Moorella thermoacetica
Biochemistry
45
8674-8685
2006
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674177
Tan
Kinetics of CO insertion and a ...
Moorella thermoacetica
J. Am. Chem. Soc.
128
12331-12338
2006
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674925
Tan
Function of the tunnel in acet ...
Moorella thermoacetica
J. Biol. Inorg. Chem.
11
371-378
2006
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The tunnel of acetyl-coenzyme ...
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A quantum chemical study of th ...
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A functional Ni-Ni-[4Fe-4S] cl ...
Carboxydothermus hydrogenoformans
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446-451
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Reduction and methyl transfer ...
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Inactivation of acetyl-CoA syn ...
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658436
Golden
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Capture of NiII, CuI and ZnII ...
Moorella thermoacetica
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1824-1825
2003
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Structural analogues of the bi ...
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660349
Seravalli
Functional copper at the acety ...
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3689-3694
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644679
Doukov
A Ni-Fe-Cu center in a bifunct ...
Moorella thermoacetica
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567-572
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Stopped-flow kinetics of methy ...
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644864
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Acetyl Coenzyme A synthesis fr ...
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Evidence for intersubunit comm ...
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The role of an iron-sulfur clu ...
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Menon
Role of the [4Fe-4S] cluster i ...
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Kasmi
Anaerobic pathway for conversi ...
Moorella thermoacetica
Biochemistry
33
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1994
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Grahame
Substrate and cofactor reactiv ...
Methanosarcina barkeri
Biochemistry
32
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1993
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Jablonski
Characterization of the metal ...
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Acetyl-coenzyme A synthesis fr ...
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Catalysis of acetyl-CoA cleava ...
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Reductive activation of the co ...
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Controlled potential enzymolog ...
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Roberts
Cloning and expression of the ...
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Acetate biosynthesis by acetog ...
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