Near the molybdopterin
cofactor, one of the binding sites to which flavonoids are bound to is responsible for the xanthine oxidation, resulting to the uric acid product.
Comparative genome analysis revealed that most genes for biosynthesis of the molybdopterin
cofactor (Moco), the cofactor of formylmethanofuran dehydrogenase (fmd), are absent from the genome of this methanogen.
These compounds will be prepared with a focus on distinct aspects of the biomolecules (first coordination sphere, different functional groups of the complex molybdopterin
ligand, hydrogen bonding sites); their stability and ability to catalyse oxygen atom transfer (in particular the oxidation of sulfite) will be assessed and their suitability to bind in the active site pocket of the protein and restore activity will be tested.
XOR is a dimeric metalloflavoprotein comprising two identical subunits of approximately 145 kDa each, including one molybdenum-containing molybdopterin
cofactor (Moco) and one flavin adenine dinucleotide (FAD) cofactor, as well as two nonidentical iron-sulfur redox centers.
CAPE has a higher hydrophobicity and stronger inhibition potency toward XO and it inhibits the enzymatic activity via binding to the molybdopterin
region of its active site.
Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin
in Escherichia coli.
Among the proteins containing two cysteines, only two proteins (arsenate reductase and molybdopterin
binding domain, Table 1) did not form a disulfide bond.
Arsenite binds to sulfhydryl groups of molybdopterin
and in doing so ultimately displaces molybdenum (Gardlik et al.
Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin
nitroreducens" comprises several genes including the catalytic alpha (NarG, molybdopterin
) and beta (NarH, iron sulfur cluster) subunit of nitrate reductase [28, 43].
The presence of enzymes and pathways of nitrate reduction proposals was also compared between biovar Ovis and biovar Equi strains and with respect to enzymes, the main difference was the presence of the nitrate locus that contains the genes encoding the molybdopterin
and the genes encoding the nitrate reductase and a region situated upstream of the ansA gene and this locus has a 19,606 pb length.
Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin