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1.2.7.4: anaerobic carbon-monoxide dehydrogenase

This is an abbreviated version!
For detailed information about anaerobic carbon-monoxide dehydrogenase, go to the full flat file.

Word Map on EC 1.2.7.4

Reaction

CO
+
H2O
 + 2 oxidized ferredoxin =
CO2
 + 2 reduced ferredoxin + 2 H+

Synonyms

acetyl coenzyme A synthase/carbon monoxide dehydrogenase, acetyl-CoA synthase/carbon monoxide dehydrogenase, ACS/CODH, Carbon dioxide/carbon monoxide oxidoreductase, Carbon monoxide dehydrogenase, carbon monoxide dehydrogenase-corrinoid enzyme complex, carbon monoxide dehydrogenase/acetyl-CoA synthase, Carbon monoxide oxidoreductase, Cdh, CO dehydrogenase, CO dehydrogenase complex, CO dehydrogenase complex II, CO dehydrogenase II, CO dehydrogenase/acetyl-CoA synthase, Co-DG, CO-DH, CODH, CODH II, CODH-II, CODH/ACS, CODHACS, CODHase, CODHII, coos, Dehydrogenase, carbon monoxide, EC 1.2.99.2, monoxide dehydrogenase/acetyl-CoA synthase, Ni,Fe-CODH, Ni,Fe-dependent carbon monoxide dehydrogenase, Ni-CODH, Ni-containing carbon monoxide dehydrogenase, Ni-Fe carbon monoxide dehydrogenase II

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.7 With an iron-sulfur protein as acceptor
                1.2.7.4 anaerobic carbon-monoxide dehydrogenase

Engineering

Engineering on EC 1.2.7.4 - anaerobic carbon-monoxide dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C56A
-
devoid of CO oxidation activity
K563L
-
very low CO oxidation activity
A110C
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
A222L
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
-
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