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