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Results 1 - 10 of 11 > >>
EC Number Cofactor Commentary Reference
Display the reaction diagram Show all sequences 1.8.7.3FAD - 744307
Display the reaction diagram Show all sequences 1.8.7.3FAD required for activity. Conformational changes within the HdrA subunit provide a conformationally gated pathway for electrons to and from the bifurcating flavin adenine dinucleotide (FAD) 765833
Display the reaction diagram Show all sequences 1.8.7.3FAD the enzyme is an iron-sulfur subunit A of the HdrABC complex and contains [4 Fe-4S] clusters 764472
Display the reaction diagram Show all sequences 1.8.7.3FAD the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached 765831
Display the reaction diagram Show all sequences 1.8.7.3Fe-S center subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron (Fe) and 1 sulfur (S), which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines 765831
Display the reaction diagram Show all sequences 1.8.7.3Fe-S center subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron and 1 sulfur, which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines 765831
Display the reaction diagram Show all sequences 1.8.7.3Ferredoxin - 764472, 764654, 764753, 765833
Display the reaction diagram Show all sequences 1.8.7.3more the enzyme contains (4Fe-4S)clusters 765833
Display the reaction diagram Show all sequences 1.8.7.3more the HdrABC·MvhAGD (see also EC 1.8.98.1) complex is abundant in iron-sulfur cofactors, with 11 [4 Fe-4S] clusters, one [2 Fe-2S], a Ni-Fe site for H2 catalysis, and two noncubane iron-sulfur clusters 764472
Display the reaction diagram Show all sequences 1.8.7.3more the thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC) 765831
Results 1 - 10 of 11 > >>