EC Number |
Reaction |
Reference |
---|
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
catalytic mechanism model using DTT and O2, overview. Stabilization of mixed disulfide intermediates in enzyme sfALR |
741890 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor |
-, 742196 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
enzyme contains a functionally involved redox-active motif CXXC |
659861, 659862 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
enzyme contains a functionally involved redox-active motif YPCCXXC |
659339 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
mechanistic scheme |
657645 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
reaction mechanism |
660455 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
ter bi substituted mechanism, O2 binds first |
393045 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
the CXXC motif in the active site sequence of Erv2p is catalytically essential, reaction mechanism involving reactive cysteine residues C121 and C124 of the A subunit, and C176 and C178 of the B subunit |
657645 |
1.8.3.2 | 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 |
the N-terminal cysteine pair of the enzyme is essential for in vivo activity and interacts with the primary redox centre |
658616 |