Information on EC 1.2.99.2 - carbon-monoxide dehydrogenase (acceptor)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.2.99.2
-
RECOMMENDED NAME
GeneOntology No.
carbon-monoxide dehydrogenase (acceptor)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CO + H2O + A = CO2 + AH2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
carbon-monoxide:acceptor oxidoreductase
Contains a [Ni3Fe-4S] cluster and [4Fe-4S] clusters. It uses many electron acceptors, including ferredoxin, methyl viologen and benzyl viologen and flavins, but not pyridine nucleotides. Forms part of a membrane-bound multienzyme complex with EC 1.12.99.6, hydrogenase (acceptor), which catalyses the overall reaction: CO + H2O = CO2 + H2.
CAS REGISTRY NUMBER
COMMENTARY hide
64972-88-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Autotrophic methanogenic bacterium
-
-
-
Manually annotated by BRENDA team
gram-negativ soil bacterium
-
-
Manually annotated by BRENDA team
strain Z-2901 (DSM 6008)
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
chemolithoautotrophic
-
-
Manually annotated by BRENDA team
chemolithoautotrophic
-
-
Manually annotated by BRENDA team
large subunit, fragment; synonym Stappia aggregata
UniProt
Manually annotated by BRENDA team
more than threefold induction of enzyme activity and increase in enzyme expression in a mutant lacking the membrane-bound energy-conserving hydrogenase Ehb
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain G1
-
-
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
-
-
-
Manually annotated by BRENDA team
strain JC1; strain JC1 DSM 3803
-
-
Manually annotated by BRENDA team
strain H37Ra; strain H37Ra ATCC 35835
-
-
Manually annotated by BRENDA team
strain ATCC 15483
-
-
Manually annotated by BRENDA team
no activity in heterotrophic methanogenic bacteria
-
-
-
Manually annotated by BRENDA team
no activity in Methanobrevibacter ruminantium
-
-
-
Manually annotated by BRENDA team
no activity in Methanobrevibacter smithii
-
-
-
Manually annotated by BRENDA team
no activity in Methanococcus voltae
-
-
-
Manually annotated by BRENDA team
no activity in Methanospirillum hungatei
-
-
-
Manually annotated by BRENDA team
P19919 large subunit, P19920 medium subunit, P19921 small subunit
P19919 and P19920 and P19921
UniProt
Manually annotated by BRENDA team
Stappia carboxidovorans
-
-
-
Manually annotated by BRENDA team
large subunit, fragment
UniProt
Manually annotated by BRENDA team
large subunit, fragment
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Stappia sp.
large subunit, fragment
UniProt
Manually annotated by BRENDA team
synthetic construct
grows on acetate if cocultured with hydrogen-consuming methanogenic partner Methanothermobacter thermautrophicus
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-SCoA + CO
acetyl-SCoA + CO
show the reaction diagram
-
acetyl-CoA/CO exchange reaction, 14C experiments prove that the enzyme can cleave both the carbon-carbon and carbon-sulfur bonds of acetyl-CoA as well as to store methyl, CO, and CoA fragments at the active site
-
r
acetyl-SCoA + CoASH
acetyl-SCoA + CoASH
show the reaction diagram
-
acetyl-CoA/CoA exchange reaction
-
r
CO + ferredoxin
?
show the reaction diagram
CO + H2O
CO2 + H2
show the reaction diagram
-
-
-
?
CO + H2O + 1,1'-trimethylene-4,4'-dimethyl-2,2'dipyridylium dibromide
CO2 + reduced 1,1'-trimethylene-4,4'-dimethyl-2,2'dipyridylium dibromide
show the reaction diagram
-
-
-
?
CO + H2O + 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
show the reaction diagram
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
show the reaction diagram
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
CO + H2O + acceptor
CO2 + reduced acceptor + H+
show the reaction diagram
-
-
-
-
?
CO + H2O + benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
CO + H2O + coenzyme F420
CO2 + reduced coenzyme F420
show the reaction diagram
CO + H2O + cytochrome b
CO2 + reduced cytochrome b
show the reaction diagram
-
-
-
?
CO + H2O + cytochrome c3
CO2 + reduced cytochrome c3
show the reaction diagram
-
cytochrome 3 from Desulfovibrio vulgaris
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
show the reaction diagram
-
a proton gradient across the cytoplasmic membrane is generated by channeling the electrons formed via cytochrome b561 into a CO-insensitive respiratory chain
-
?
CO + H2O + FAD
CO2 + FADH2
show the reaction diagram
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
show the reaction diagram
CO + H2O + flavodoxin
CO2 + reduced flavodoxin
show the reaction diagram
-
-
-
?
CO + H2O + FMN
CO2 + FMNH2
show the reaction diagram
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
CO + H2O + methyl viologen
CO2 + reduced methyl viologen + H+
show the reaction diagram
CO + H2O + methylene blue
CO2 + reduced methylene blue
show the reaction diagram
CO + H2O + methylene blue
CO2 + reduced methylene blue + H2
show the reaction diagram
-
-
-
-
?
CO + H2O + NAD+
CO2 + NADH + H+
show the reaction diagram
CO + H2O + NADP+
CO2 + NADPH + H+
show the reaction diagram
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
show the reaction diagram
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
CO + H2O + phenazine methosulfate
CO2 + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
CO + H2O + rubredoxin
CO2 + reduced rubredoxin
show the reaction diagram
H2 + reduced methyl viologen
methyl viologen
show the reaction diagram
-
-
-
-
r
propionyl-SCoA + CoASH
propionyl-SCoA + CoASH
show the reaction diagram
-
acetyl-CoA/CoA exchange reaction
-
r
tetrahydrosarcinapterin + acetyl-SCoA + H2O
methyltetrahydrosarcinapterin + CO2 + CoASH
show the reaction diagram
trichloroethylene + ?
cis-dichloroethylene + trans-dichlororethylene + 1,1-dichloroethylene + vinyl chloride + ethylene
show the reaction diagram
-
-
-
?
additional information
?
-
-
Thermacetogenium phaeum operates the CO dehydrogenase/acetyl-CoA pathway reversibly both in acetate oxidation and in reductive acetogenesis by using the same biochemical apparatus
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CO + ferredoxin
?
show the reaction diagram
CO + H2O
CO2 + H2
show the reaction diagram
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
CO + H2O + acceptor
CO2 + reduced acceptor + H+
show the reaction diagram
-
-
-
-
?
CO + H2O + electron acceptor
?
show the reaction diagram
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
show the reaction diagram
-
a proton gradient across the cytoplasmic membrane is generated by channeling the electrons formed via cytochrome b561 into a CO-insensitive respiratory chain
-
?
additional information
?
-
-
Thermacetogenium phaeum operates the CO dehydrogenase/acetyl-CoA pathway reversibly both in acetate oxidation and in reductive acetogenesis by using the same biochemical apparatus
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin adenine dinucleotide
iron-sulfur centre
-
-
molybdopterin cytosine dinucleotide
Ni-4Fe-5S center
-
active site cluster
Ni-Fe-4S center
-
active site called the C-cluster
Ni-Fe-S center
-
uses a Ni-Fe-S center called the C-cluster to reduce carbon dioxide to carbon monoxide and uses a second Ni-Fe-S center, called the A-cluster, to assemble acetyl-CoA from a methyl group, coenzyme A, and C-cluster-generated CO
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S cluster
-
core extrusion experiments indicate 6 [4Fe-4S] clusters per tetramer, and electron paramagnetic resonance spectroscopy detects at least one of these clusters, in the reduced form
Co2+
-
the multifunctional enzyme complex contains Co2+
copper
Fe-S center
-
the multifunctional enzyme complex contains iron-sulfur centers
Molybdenum
Ni-Fe-S center
-
-
S2-
-
contains a [NiFe4S5] center called cluster C
Zn2+
-
the multifunctional enzyme complex contains Zn2+
[2Fe-2S]-center
-
the small subunit contains two [2Fe-2S] centers
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM, inactivates CO/acetyl-CoA exchange activity completely but has no effect on CO oxidation
2,3-Butanedione
-
-
Butyryl-CoA
-
-
COS
-
rapid-equilibrium inhibitor largely competitive versus CO, uncompetitive versus methyl viologen
crotonyl-CoA
-
-
cyanide
D-glucose
partially inhibited by incubation with 0.5 mM exogenous D-glucose
dephospho-CoASH
-
-
desulfo-CoA
-
-
Glyoxaldehyde
-
inactivation requires enzymatic turnover
Hg+
Methanothermobacter thermautotrophicum
-
-
methyl iodide
-
CO promotes inhibition
N2O
-
inhibition of the exchange reaction between acetyl-CoA and CoA
PCMB
Methanothermobacter thermautotrophicum
-
-
pivaloylpantetheine-SH
-
-
potassium cyanide
-
competitive inhibitor of reduced CODHII with respect to the substrate CO, inhibition of dithionite- or Ti(III) citrate-reduced CODHII by potassium cyanide is fully reversible since the enzyme can be completely reactivated, sodium sulfide has no effect on the reactivation of cyanide-inhibited CODHII in the presence of dithionite
propionyl-CoA
-
-
SCN-
-
binds to C-center, mixed partial inhibition
Sulfide
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
corrinoid cofactor
-
the multifunctional enzyme complex contains a corrinoid cofactor
-
Nickel
-
Ni-activated alpha subunit rapidly and reversibly accepts a methyl group
sodium nitroprusside
Ti(III)citrate
-
1mM for 1 min at 65C, 45fold increase in initial activity
additional information
-
CooC proteins are ATPases involved in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenases
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
2,3,5-triphenyltetrazolium chloride
-
below 0.5 mM
0.6 - 1.5
acetyl-CoA
0.01 - 5
CO
0.05
CoA
-
acetyl-CoA/CoA exchange reaction
0.008
Ferredoxin
-
-
-
0.065 - 7.1
methyl viologen
0.00295 - 0.0107
methylene blue
5
propionyl-CoA
-
-
1.7
Trichloroethylene
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.17 - 15900
CO
8.2 - 93.3
methylene blue
additional information
additional information
Moorella thermoacetica
-
42000/min/Ni, substrate methyl viologen
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2780 - 8700
methylene blue
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.45
Butyryl-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
0.4 - 1.5
CO
0.007
CoASH
0.0023 - 0.0158
COS
1.4
crotonyl-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
0.0217
cyanide
-
at 23C, in 4 mM dithionite, and 4 mM dithiothreitol
0.035
dephospho-CoASH
-
inhbition of CO/acetyl-CoA exchange reaction
6
desulfo-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
1.2
pivaloylpantetheine-SH
-
inhbition of CO/acetyl-CoA exchange reaction
1.3
propionyl-CoA
-
inhbition of CO/acetyl-CoA exchange reaction
16 - 830
SCN
0.00004 - 0.00006
Sulfide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001 - 0.002
-
CO2/acetyl-CoA exchange in cell extracts at 85C
0.006
-
at 37C
0.0175
-
at 37C
0.04
-
pH 7.5, 65C, cell extract
0.1
-
pH 7.5, 65C
0.32
-
CO/acetyl-CoA exchange reaction
0.9
-
pH 8.1, 80C
0.96
-
after 12.92fold purification, at 95C, pH 8.0, using methylene blue as electron acceptor
2.08
-
after 12.92fold purification, at 95C, pH 8.0, using methyl viologen as electron acceptor
2.45
-
after 12.92fold purification, at 95C, pH 8.0, using NADP+ as electron acceptor
2.47
-
after 12.92fold purification, at 95C, pH 8.0, using NAD+ as electron acceptor
5.2
-
pH 7.5, 65C, cell extract
5.7
-
CO oxidation in cell-extracts at 85C, electron acceptor methylviologen
6.9
-
mutant C531A, pH 7.5
7
-
acetyl-CoA/CoA exchange reaction at pH 6.0 and 45C, 100% CO in the gas phase
28
-
acetyl-CoA/CoA exchange reaction at pH 6.0 and 45C, CO in the gas phase replaced by N2
76.8
-
cells grown in pure culture on pyruvate, pH 7.5, 55C
86.3
-
mutant C451S, pH 7.5
100
-
25C, mutant A265M
120
-
electron acceptor ferredoxin
163
-
cells grown syntrophically on acetate, pH 7.5, 55C
200
-
25C, wild type
216
-
pH 7.0, 37C
250
-
CO oxidation
280
-
25C, mutant A110C
300
-
25C, mutant A222L
675
-
electron acceptor methyl viologen
6230
-
wild-type, pH 7.5
14000
-
carbon monoxide dehydrogenase II
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
both for enzyme and complex
6.7
Methanothermobacter thermautotrophicum
-
in cell-free extracts
8.6
-
wild-type
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
pH 6.5: about 25% of maximal activity, pH 8-9: maximal activity
8 - 11.5
-
pH 8: about 55% of maximal activity, pH 11.5: about 50% of maximal activity
8
-
about 60% of activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75 - 100
-
about 65% activity at 75C, about 75% activity at 80C, about 80% activity at 85C, about 90% activity at 90C, 100% activity at 95C, about 30% activity at 100C, respectively
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17390
D5G1Y2 and D5G1Y0 and D5G1Y1
small subunit, calculated from sequence of cDNA
30620
D5G1Y2 and D5G1Y0 and D5G1Y1
medium subunit, calculated from sequence of cDNA
61600
-
gel filtration
72000
-
beta subunit, SDS-PAGE
85970
D5G1Y2 and D5G1Y0 and D5G1Y1
large subunit, calculated from sequence of cDNA
120000
-
gel filtration, enzyme
161000
-
dialyzed enzyme, gel filtration
163700
-
calculated from amino acid sequence
190000
-
gel filtration
210000
-
gel filtration
220000
-
nondenaturing PAGE
230000
-
native PAGE
235000
-
gel filtration
250000
273500
-
deduced from amino acid sequence
300000
-
sedimentation equilibrium ultracentrifugation
410000
-
gel filtration
436000
-
gel filtration
450000
-
gel filtration, complex
1000000
-
the native enzyme (MW 250000 Da) forms aggregates with an MW of approximately 1000000, gradient gel electrophoresis
1600000
-
carbon monoxide dehydrogenase-corrinoid enzyme complex, gel filtration
3000000
-
high molecular weight form exists under conditions of high ionic strength, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 62000, SDS-PAGE, enzyme
heterohexamer
heterotetramer
hexamer
homodimer
monomer
-
1 * 61800, SDS-PAGE
octamer
-
2 * 62000, enzyme, + electron transfer protein CooF and membrane bound [Ni-Fe] hydrogenase, six differentsubunits
oligomer
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
tetramer
additional information
-
properties of enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carbon monoxide dehydrogenase II, hanging drop vapor diffusion, 20% 2-propanol, 20% polyethylene glycol 3000, 100 mM HEPES, pH 7.5
-
in presence of dithiothreitol or dithionite and under an atmosphere of N2 or CO
-
native and cyanide bound CODH/ACS complex
vapor diffusion, 800 mM KH2PO4, 800 mM NaH2PO4, 2% 2-methyl-2,4-pentanediol, 100 mM HEPES, pH 7.3
-
EPR studies of enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase, in presence and absence of nickel
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
-
wild-type and mutants apo-enzymes, stable for at least 30 min within this range
674921
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
10 min, about 30% loss of activity in presence of CO, stable in absence of CO
39
-
10 min, 45% loss of activity in presence of CO, stable in absence of CO
60
-
10 min, about 10% loss of activity
62
-
10 min, about 65% loss of activity in presence of CO, about 5% loss of activity in absence of CO
72
-
10 min, complete inactivation
80
-
10 min, about 85% loss of activity in presence of CO, about 20% loss of activity in absence of CO
104
-
10 min, complete loss of activity in presence or in absence of CO
additional information
-
CO renders the enzyme more susceptible to temperature inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
72 h exposure to air at 4C, about 10% loss of activity
-
98% loss of activity after 15 min in an aerobic buffer
-
CN- inactivates
-
CO renders the enzyme more susceptible to temperature inactivation
-
the presence of CO has no apparent effect on the stability
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
100% of activity remains after 48 h of oxygen exposure, and after 168 h of air exposure, activity is 88% of the initial activity
-
725052
extreme oxygen lability
extremely oxygen-labile, even in N2 atmosphere with less than 5 ppm O2 the pure enzyme loses a significant amount of its activity within 18 h, 2 mM dithionite protects from inactivation
-
390450
extremely sensitive to air, most of the enzyme activity is lost upon exposure to air for 1 min, longer incubation results in complete inactivation
-
390449
oxygen stable, 10% loss in activity after 72 h exposure to air at 4C
-
390473
Oxygen treatment results in an activity loss of 90% within 30 min. Treatment of oxygen-inactivated enzyme with CO, H2, or dithionite does not restore activity
-
727713
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or 5C, 50 mM Tris/HCl, pH 7.5, 2 mM sodium dithionite, 0.2 mM methyl viologen, 50% v/v glycerol, stable for more than 1 month
-
4C, 1 month, 100% inactivation
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anion-exchange, hydrophobic interaction, gel filtration
-
carbon monoxide dehydrogenase II
-
Cosmogel His-Accept column chromatography, and gel filtration
-
Ni-NTA agarose column chromatography
-
Q-Sepharose column chromatography and Sephacryl S-300 gel filtration
-
Q-Sepharose column chromatography, CHT-I column chromatography, and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli DH5 alpha cells
expressed in Escherichia coli Rosetta2 (DE3) cells
-
expressed in Escherichia coli strain JM109
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the synthesis of CO-DH is induced in the presence of CO. The CutR protein is involved in the induction of CO-DH synthesis in the presence of CO. When the wild type strain grown on 0.2% (w/v) glucose is further grown on 0.002% (w/v) glucose for 5 h, the CO-DH activity is increased by 1.6fold relative to that detected in the same strain grown on 0.2% (w/v) glucose for additional 5 h as a control
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C56A
-
devoid of CO oxidation activity
K563L
-
very low CO oxidation activity
A121H/H122A
-
11% of wild type activity
A219F
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
A265M
-
mutation within tunnel region of alpha subunit, absence of strong cooperative inhibition of CO, little synthesis of acetyl-CoA
A578C
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
C316S
-
0.3% of wild type activity
E115H/H116A
-
24% of wild type activity
F70W
-
mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
H113A
-
44% of wild type activity, in presence of imidazole, 45% of wild type activity
H113A/H116A/H119A
-
no activity
H113A/H119A
-
15% of wild type activity
H116A
-
6% of wild type activity, in presence of imidazole, 3% of wild type activity
H116A/G117H
-
0.8% of wild type activity
H116C
-
46% of wild type activity
H116D
-
0.4% of wild type activity
H119A
-
27% of wild type activity
H122A
-
3% of wild type activity
H122A/A123H
-
72% of wild type activity
K587A
-
42% of wild type activity
K587A/H113A
-
0.7% of wild type activity
L215F
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
N101Q
-
mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
N284A
-
41% of wild type activity
N284A/H119A
-
36% of wild type activity
C338A
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complete loss of activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C451A
-
complete loss of activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C451S
-
1.4% of wild-type specific activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C481A
-
unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C531A
-
0.1% of wild-type specific activity
H265V
-
no CO oxidation activity in presence or absence of nickel, production of formate at same level as wild type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
assay method for enzyme in complex with protein CooF which mediates electron transfer from enzyme to the CO-induced hydrogenase based on membranes containing high levels of CO-induced hydrogenase
Show AA Sequence (2234 entries)
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