1.2.5.3: aerobic carbon monoxide dehydrogenase
This is an abbreviated version!
For detailed information about aerobic carbon monoxide dehydrogenase, go to the full flat file.
Reaction
Synonyms
aerobic Mo/Cu-containing CO dehydrogenase, Carbon monoxide dehydrogenase, CO dehydrogenase, CODH, CoxS, coxSML, CutL, CutM, CutS, EC 1.2.2.4, EC 1.2.3.10, Mo-CODH, Mo-Cu carbon monoxide dehydrogenase, Mo/Cu CODH, MoCu-CODH, molybdenum- and copper-containing carbon monoxide dehydrogenase, molybdenum- and copper-dependent CO dehydrogenase, molybdenum-containing carbon monoxide dehydrogenase, molybdenum-containing CO dehydrogenase, molybdenum-copper carbon monoxide dehydrogenase, molybdenum-copper CO dehydrogenase, molybdenum/copper-containing carbon monoxide dehydrogenase, molybdoenzyme carbon monoxide dehydrogenase
ECTree
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Subunits
Subunits on EC 1.2.5.3 - aerobic carbon monoxide dehydrogenase
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heterohexamer
oligomer
additional information
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the functional enzyme is a (alphabetagamma)2 hexamer that consists of a small 17.8 kDa subunit (CoxS) containing two [2Fe-2S] clusters, a medium 30.2 kDa subunit (CoxM) containing an FAD cofactor, and a large 88.7 kDa subunit (CoxL) that possesses the molybdenum center
heterohexamer
(abc)2 structure, each protomer of the enzyme has a small subunit (CoxS, 18 kDa) with two [2Fe-2S] iron-sulfur clusters, a medium subunit (CoxM, 30 kDa) that possesses FAD, and a large subunit (CoxL, 89 kDa) that has the active site binuclear center
heterohexamer
(alphabetagamma)2 hexamer, with a large subunit (coxL, 88.7 kDa) containing the binuclear active site, a medium subunit (coxM, 30.2 kDa) with FAD, and a small subunit (coxS, 30.2 kDa) containing two spinach ferredoxin-like [2Fe-2S] clusters
heterohexamer
(alphabetagamma)2, 2 * 88700, large subunit, + 2 * 30200, medoum subunit, + 2 * 17800, small subunit, SDS-PAGE
heterohexamer
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(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE
heterohexamer
CO dehydrogenase is composed of a 88.7 kDa molybdoprotein (L subunit), a 30.2 kDa flavoprotein (M subunit), and a 17.8 kDa iron-sulfur protein (S subunit) in a (LMS)2 subunit composition
heterohexamer
CO dehydrogenase is composed of an 88.7-kDa molybdoprotein (subunit L), a 30.2-kDa flavoprotein (subunit M), and a 17.8-kDa iron-sulfur protein (subunit S). It is organized as a dimer of LMS heterotrimers
heterohexamer
Afipia carboxidovorans ATCC 49405
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the functional enzyme is a (alphabetagamma)2 hexamer that consists of a small 17.8 kDa subunit (CoxS) containing two [2Fe-2S] clusters, a medium 30.2 kDa subunit (CoxM) containing an FAD cofactor, and a large 88.7 kDa subunit (CoxL) that possesses the molybdenum center
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heterohexamer
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(alphabetagamma)2, 2 * 88700, large subunit, + 2 * 30200, medoum subunit, + 2 * 17800, small subunit, SDS-PAGE
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heterohexamer
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CO dehydrogenase is composed of a 88.7 kDa molybdoprotein (L subunit), a 30.2 kDa flavoprotein (M subunit), and a 17.8 kDa iron-sulfur protein (S subunit) in a (LMS)2 subunit composition
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heterohexamer
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(alphabetagamma)2, 2 * 75000, large subunit, + 1 * 28400, medium subunit, + 1 * 17200, small subunit, SDS-PAGE
heterohexamer
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(alphabetagamma)2, 2 * 75000, large subunit, + 1 * 28400, medium subunit, + 1 * 17200, small subunit, SDS-PAGE
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LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE
oligomer
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LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE
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oligomer
x * 87224, large subunit, + x * 30694, medium subunit, + x * 17752, small subunit, sequence calculation
oligomer
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x * 87224, large subunit, + x * 30694, medium subunit, + x * 17752, small subunit, sequence calculation
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Mo-CODH is composed of a heterotrimer, each heterotrimer has a molybdopterin (L-subunit) that contains the molybdopterin-cytosine dinucleotide (MCD)-type of molybdenum cofactor, a flavoprotein (M-subunit) that contains the flavin adenine dinucleotide (FAD) cofactor, and an iron-sulfur protein (S-subunit) carrying type I and II [2Fe-2S] clusters
additional information
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Mo-CODH is composed of a heterotrimer, each heterotrimer has a molybdopterin (L-subunit) that contains the molybdopterin-cytosine dinucleotide (MCD)-type of molybdenum cofactor, a flavoprotein (M-subunit) that contains the flavin adenine dinucleotide (FAD) cofactor, and an iron-sulfur protein (S-subunit) carrying type I and II [2Fe-2S] clusters
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additional information
the enzyme is an S-selanylcysteine-containing 88.7-kDa molybdoprotein, a 17.8-kDa iron-sulfur protein, and a 30.2-kDa flavoprotein in a (LMS)2 subunit structure
additional information
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the enzyme is an S-selanylcysteine-containing 88.7-kDa molybdoprotein, a 17.8-kDa iron-sulfur protein, and a 30.2-kDa flavoprotein in a (LMS)2 subunit structure
additional information
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the the active site molybdenum center is located in the large subunit, while the medium subunit contains FAD, and the small subunit contains the [2Fe-2S]-clusters
additional information
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the enzyme is an S-selanylcysteine-containing 88.7-kDa molybdoprotein, a 17.8-kDa iron-sulfur protein, and a 30.2-kDa flavoprotein in a (LMS)2 subunit structure
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additional information
active site and cofactor binding structure, overview
additional information
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active site and cofactor binding structure, overview
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