EC Number   |
Cofactor |
Reference |
|---|
   1.2.5.3 | benzoquinone |
- |
736514 |
| 1.2.5.3 | FAD |
- |
725392, 736437, 736513 |
| 1.2.5.3 | FAD |
bound by the medium subunit |
725197 |
| 1.2.5.3 | FAD |
FAD is bound in a fold formed by the N-terminal and middle domains. In the N-terminal domain a beta-turn part of a betaalphabeta-unit of a three-stranded parallel beta-sheet contains the motif 32AGGHS36 which interacts with the FAD diphosphate. FAD binding structure, overview |
656481 |
| 1.2.5.3 | FAD |
FAD is bound in the medium subunit, a flavoprotein |
736512 |
| 1.2.5.3 | FAD |
FAD is bound in the medium subunit. The flavoprotein can be removed from CO dehydrogenase by dissociation with sodium dodecylsulfate, the resulting M(LS)2- or (LS)2-structured CO dehydrogenase species can be reconstituted with the recombinant apoflavoprotein produced in Escherichia coli, structural and functional analysis of FAD binding in CO dehydrogenase |
736397 |
| 1.2.5.3 | FAD |
in the medium subunit |
390483 |
| 1.2.5.3 | FAD |
located in the medium subunit |
736514 |
| 1.2.5.3 | FAD |
one noncovalently bound FAD molecule per monomer, FAD-binding occurs on the M subunit and requires conformational changes of subunit M introduced through the binding of subunt M to subunits LS. In air-oxidized CO dehydrogenase, the flavin is fully oxidized |
390482 |
| 1.2.5.3 | FAD |
the GLGTYG sequence, residues 564 to 569, in large subunit CoxL is identical to dinucleotide-binding motif GXGXXG/A, an FAD binding site. The FAD-binding domain of the ferredoxin-NADP+ reductase type is absent |
390479 |
