EC Number   |
Cofactor |
Reference |
|---|
   1.1.3.9 | Cys-Tyr cofactor |
- |
743101 |
| 1.1.3.9 | Cys-Tyr cofactor |
an inactive, oxidized state of FgrGalOx, which contains a Cu(II) site and a 1-electron reduced Cys-Tyr cofactor, produce a low-temperature EPR spectrum, this inactive state can be activated under typical assay conditions |
743337 |
| 1.1.3.9 | Cys-Tyr cofactor |
the active-site Cu is coordinated by a unique cysteinylated tyrosine (Cys-Tyr) ligand that serves as a second redox-active cofactor. Post-translational biogenesis of Cys-Tyr is copper- and O2-dependent, resulting in a self-processing enzyme system. Mechanism of cofactor biogenesis in galactose oxidase, overview. The role of cysteinylation (as well asPi-stacking of an adjacent conserved Trp) is to stabilize the (Cys-Tyr)radical and allow its function as a redox cofactor at a more biologically accessible potential. In turnover the Cu/(Cys-Tyr) unit accomplishes 2e- redox by shuttling between CuI/(Cys-Tyr)- and CuII/(Cys-Tyr) radical states in a ping-pong type mechanism |
742748 |
| 1.1.3.9 | Cys-Tyr cofactor |
the enzyme contains a unique metalloradical complex consisting of a copper atom and a tyrosine residue covalently attached to the sulfur of a cysteine. The Tyr-Cys crosslink is essential for the catalytic activity of GalOx. The formation of the TyrN-Cys redox cofactor in GalOx is a self-processing reaction requiring only the apoprotein, copper, and dioxygen; no other proteins or enzymes are required for the processing and assembly of the catalytically active enzyme |
743642 |
| 1.1.3.9 | FAD |
- |
712522 |
| 1.1.3.9 | more |
mechanism of cofactor biogenesis, overview, metalloradical complex, comprised of a protein radical coordinated to a copper ion in the active site, the unusually stable protein radical is formed from the redox-active side chain of a cross-linked tyrosine residue, TyrCys |
671578 |
| 1.1.3.9 | more |
radical cofactor, the active site consists of two one-electron redox units involving residues Y495, H496, H581, Y272, and W290, a Cu2+ ion, and a crosslinked Y272-C228 radical cofactor, which together are responsible for the catalytic activity |
674186 |
| 1.1.3.9 | pyrroloquinoline quinone |
one pyrroquinoline covalently bound to one molecule, additional two-electron redox center |
389856 |
