EC Number   |
General Information |
Reference |
|---|
    1.13.11.20 | evolution |
analysis of examples for two structural genomics groups of CDOs: a Bacillus subtilis Arg-type enzyme that has cysteine dioxygenase activity (BsCDO), and a Ralstonia eutropha Gln-type CDO homologue of uncharacterized activity (ReCDOhom), overview. The BsCDO active site is well conserved with mammalian CDO, and a cysteine complex captured in the active site confirms that the cysteine binding mode is also similar. The Arg position is not compatible with the mode of Cys binding seen in both Rattus norvegicus CDO and Bacillus subtilis CDO. Gln-type CDO homologues are not authentic CDOs but have substrate specificity more similar to 3-mercaptopropionate dioxygenases |
-, 743757 |
| 1.13.11.20 | evolution |
structure and catalytic mechanism comparisons of nonheme iron enzymes cysteine dioxygenase with sulfoxide synthase EgtB, EC 1.14.99.50, quantum mechanics/molecular mechanics calculations, overview |
742755 |
| 1.13.11.20 | evolution |
the enzyme belongs to the 2-His-1-carboxylate family of non-heme iron containing oxidases and oxygenases |
724297 |
| 1.13.11.20 | malfunction |
deletion of cdoA might enable increased synthesis of polythioesters |
-, 741704 |
| 1.13.11.20 | metabolism |
active-site cluster models and comparison of CDO and 3-mercaptopropionate dioxygenase MDO, EC 1.13.11.91. The enzymes have different iron(III)-superoxo-bound structures due to differences in ligand coordination. The differences in the second-coordination sphere and the position of a positively charged Arg residue result in changes in substrate positioning, mobility and enzymatic turnover. For both enzymes, the second oxygen atom transfer has the highest barriers with magnitudes of 14.2 and 15.8 kcal/mol, respectively. In CDO with its 3-His ligand system, there are close-lying singlet, triplet and quintet spin-state surfaces along the mechanism, and the reaction will be influenced by the equilibration between these spin states and the ease of spin state change |
764498 |
| 1.13.11.20 | metabolism |
design of biomimetic model complexes where the 3-His coordination of theiron ion is simulated by three pyrazole donors of a trispyrazolyl borate ligand and protected cysteine represent substrate ligands. Replacement of phenyl groups attached at the 3-positions of the pyrazole units in a previous model by mesityl residues has massive consequences, as the latter arrange to a more spacious reaction pocket. The reaction with O2 proceeds much faster and the structural characterization of an iron(II) eta2-O,O-sulfinate product became possible |
764496 |
| 1.13.11.20 | metabolism |
in mammals, excess cysteine is generally degraded by oxygenation to 3-sulfino-L-alanine. The majority of cysteine sulphinic acid is then deaminated to sulphinylpyruvate, which decomposes spontaneously byreleasing inorganic sulphite. The latter compound is then further oxidized to sulphate, which is excreted for the most part from the cell. In parallel, a variable proportion of cysteine sulphinic acid is decarboxylated to hypotaurine, then further oxidized to taurine. Although cysteine can be catabolized by some non-oxidative pathways, they are of minor importance. CDO activity is regulated by concentration of cysteine, and in mammals, both have been demonstrated to be important vital factors |
725864 |
| 1.13.11.20 | metabolism |
iron(II) complexes [Fe(L)(MeCN)3](SO3CF3)2 (L are two derivatives of tris(2-pyridyl)-based ligands) as models for cysteine dioxygenase. The molecular structure of one of the complexes exhibits octahedral coordination geometry, and the Fe-Npy bond lengths are similar to those in the Cys-bound FeII-CDO. The iron(II) centers of the complexes exhibit relatively high FeIII/II redox potentials E1/2 0.988-1.380 V vs. ferrocene/ferrocenium electrode. The reaction of in situ generated [Fe(L)(MeCN)(SPh)]+ with excess O2 in acetonitrile yields selectively the doubly oxygenated phenylsulfinic acid product. Both oxygen atoms of O2 are incorporated into the product. A FeIII peroxido intermediate with a rhombic S=1=2 FeIII center is involved in the reaction |
764495 |
| 1.13.11.20 | metabolism |
mononuclear Co(II) complexes with the general formula [Co2+(TpR2)(CysOEt)] (R = Ph or Me, TpR2 = hydrotris(pyrazol-1-yl)borate substituted with R-groups at the 3- and 5-positions, and CysOEt is the anion of L-cysteine ethyl ester) mimic the active-site structure of substrate-bound CDO and are analogous to functional iron-based CDO models. The complexes possess five-coordinate structures featuring facially-coordinatingTpR2 and S,N-bidentate CysOEt ligands. The air-stability of the Ph-variant replicates the inactivity of cobalt-substituted CDO. The Me-variant reversibly binds O2 at reduced temperatures to yield an orange chromophore. Both are high-spin (S = 3/2) complexes. The orange chromophore is a S = 1/2 species featuring a low-spin Co(III) center bound to an end-on (eta1) superoxo ligand |
764839 |
| 1.13.11.20 | metabolism |
nonheme FE(II) complex [Fe(TpMe2)(2-ATP)] , where 2-ATP is 2-aminothiophenolate, models substrate-bound cysteine dioxygenase. The complex reacts with O2 at -80°C to yield a purple intermediat that features a thiolate-ligated Fe(III) center bound to a superoxide radical, mimicking the putative structure of a key CDO intermediate |
764456 |
