EC Number   |
General Information |
Reference |
|---|
    1.13.11.18 | evolution |
CstB is a multifunctional Fe(II)-containing persulfide dioxygenase (PDO), analogous to the vertebrate protein ETHE1, ethylmalonic encephalopathy protein 1 |
741915 |
| 1.13.11.18 | evolution |
enzyme persulfide dioygenase, PDO, is a member of the 2His-1Asp mononuclear iron-containing enzyme superfamily |
742906 |
| 1.13.11.18 | malfunction |
by overexpressing sdo in strain ATCC 23270, a 91fold increased sdo transcriptional level and a 2.5fold increase in SDO activity are observed when sulfur S0 is used as sole energy source. The sdo knockout mutant displays a slightly reduced growth capacity in S0-medium compared with the wild type but still maintains high S0-oxidizing activity, suggesting that there is at least one other S0-oxidizing enzyme besides SDO in Acidithiobacillus ferrooxidans ATCC 23270 cells |
741742 |
| 1.13.11.18 | malfunction |
ethylmalonic encephalopathy is caused by mutations in the mitochondrial matrix sulfur dioxygenase ETHE1 leading to failure to detoxify sulfide, a product of intestinal anaerobes and, in trace amounts, tissues |
713090 |
| 1.13.11.18 | malfunction |
seeds homozygous for a DNA insertion in ETHE1 exhibit alterations in endosperm development that are accompanied by a delay in embryo development followed by embryo arrest by early heart stage |
726227 |
| 1.13.11.18 | malfunction |
stB C201S and C408S mutants are unable to rescue a NaHS-induced DELTAcstB |
741915 |
| 1.13.11.18 | more |
residue Cys314, located in the rhodanese-active site, is captured in its persulfidated Cys-SSH form. The PDO-active site is located at the bottom of a large pocket framed on one side by a positively charged ridge comprising residues Arg193-Lys216 and by Tyr176 on the other |
742906 |
| 1.13.11.18 | physiological function |
ETHE1 appears to play an essential role in regulating sulfide levels in seeds, it is essential for early seed development |
726227 |
| 1.13.11.18 | physiological function |
natural fusions between the non-heme iron containing PDO and rhodanese, a thiol sulfurtransferase, exist in some bacteria, e.g. in Burkholderia phytofirmans. The two active sites in PRF are distant and do not show evidence of direct communication. The Burkholderia phytofirmans PRF exhibits robust PDO activity and preferentially catalyzes sulfur transfer in the direction of thiosulfate to sulfite and glutathione persulfide, while sulfur transfer in the reverse direction is detectable only under limited turnover conditions. Burkholderia phytofirmans PRF is poised to metabolize thiosulfate to sulfite in a sulfur assimilation pathway rather than in sulfide stress response |
742906 |
| 1.13.11.18 | physiological function |
shading of the siliques has no morphological effect on embryogenesis in wild-type plants. In a knock-down line ethe1-1 with about 1% residual sulfur dioxygenase activity, the developmental delay is already visible in seeds under control conditions and is further enhanced in the darkness. Dark conditions strongly affect seed uality parameters of both wild-ype and mutant plants. Sulfur dioxygenase deficiency leads to defects in endosperm development |
764794 |
