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Natural Substrates
Commentary (Nat. Sub.)
2.8.1.11
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MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C-terminus of each protein The sulfur is mobilized from L-cysteine by NFS1, a pyridoxal phosphate-dependent L-cysteine desulfurase, which forms a persulfide group on its conserved Cys-381 residue. The persulfide group is further transferred to Cys-412 of the C-terminal rhodanese-like domain of MOCS3
2.8.1.11
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MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A during Moco biosynthesis in humans. In humans and most eukaryotes thiosulfate is not the physiologic sulfur donor for MOCS3
2.8.1.11
[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine
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