EC Number   |
General Information |
Reference |
|---|
   1.13.11.19 | metabolism |
design of biomimetic model complexes where the 3-His coordination of the iron ion is simulated by three pyrazole donors of a trispyrazolyl borate ligand and protected cysteamine 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 |
| 1.13.11.19 | metabolism |
functional roles of ADO in metabolism include removal of thiol substrates (cysteamine), thus regulating cysteine or cysteamine levels in body tissues and fluids and production of hypotaurine/taurine from cysteine metabolite cysteamine |
710836 |
| 1.13.11.19 | metabolism |
in the presence of nitric oxide as a spin probe and oxygen surrogate, both cysteamine and the peptide substrate regulator of G protein signaling 5 coordinate the iron center with their free thiols in a monodentate binding mode. A substrate-bound B-type dinitrosyl iron center complex is observed, as well as a substrate-mediated reduction of the iron center from ferric to the ferrous oxidation state with possible disulfide formation of the substrates |
765067 |
| 1.13.11.19 | metabolism |
presence of a Cys-Tyr cofactor, crosslinked between Cys220 and Tyr222 through a thioether (C-S) bond. An autocatalytic oxidative carbon-fluorine bond activation and fluoride release is observed. The crosslinking results in a minimal structural change of the protein. A sequence motif C-X-Y-Y(F) is proposed for identifying Cys-Tyr crosslink |
763888 |
| 1.13.11.19 | metabolism |
substrates 2-aminoethanol and 3-mercaptopropionic acid bind to ADO in the same manner, potentially in a monodentate fashion through the terminal thiolate. The high-spin ferric species exhibit a more axial zero-field splitting relative to that reported for Cys-bound FeIIICDO |
764185 |
| 1.13.11.19 | metabolism |
the enzyme is involved in the taurine biosynthetic pathway. addition of taurine to cells grown in taurine-free medium has little effect on transcript levels of the biosynthetic pathway genes for cysteine dioxygenase (CDO), cysteine sulfinate decarboxylase (CSAD), or cysteamine dioxygenase (ADO). In contrast, supplementation with taurine causes a 30% reduction in transcript levels of the taurine transporter, TauT. Hypotaurine can be produced via of cysteamine, the end product of coenzyme A degradation, via oxidation by 2-aminoethanethiol dioxygenase (ADO). Taurine biosynthetic pathway from methionine?derived cysteine, overview |
-, 743204 |
| 1.13.11.19 | physiological function |
ADO catalyzes conversion of N-terminal cysteine to cysteine sulfinic acid, reaction of EC 1.13.11.20, and is related to the plant cysteine oxidases that mediate responses to hypoxia by an identical post-translational modification. In human cells ADO regulates the RGS4/5 (regulator of G-protein signalling) N-degron substrates, modulates G-protein coupled Ca2+ signals and MAPK activity, and acts on N-terminal cysteine proteins including the angiogenic cytokine IL-32. Inactivation of ADO leads to constitutive upregulation of endogenous and transfected RGS4 and RGS5 proteins irrespective of oxygen levels |
765832 |
