EC Number   |
General Information |
Reference |
|---|
    2.8.1.11 | physiological function |
conversion of precursor Z to molybdopterin (MPT) by Escherichia coli MPT synthase entails the transfer of the sulfur atom of the C-terminal thiocarboxylate from the small subunit of the synthase to generate the dithiolene group of MPT. The sulfurtransferase is also required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z. The sulfur is transferred as a protein-bound persulfide |
722618 |
| 2.8.1.11 | physiological function |
in Escherichia coli, the L-cysteine desulfurase IscS is the primary sulfur donor for the formation of the thiocarboxylate by MoeB on the small subunit (MoaD) of MPT synthase, which catalyzes the conversion of cyclic pyranopterin monophosphate to molybdopterin, MPT. YnjE, a three-domain rhodanese-like protein from Escherichia coli, interacts with MoeB possibly for sulfur transfer to MoaD. Modeling of molybdopterin formation in the complex containing MoeB, MoaaD, MoaE, YnjE, IscC, and AMP, overview |
722726 |
| 2.8.1.11 | malfunction |
in the moeBA228T mutant strain F36, anaerobic respiratory growth is possible on nitrate but not on DMSO, the cofactor insertion mutation affects the respiratory membrane-bound molybdoenzyme nitrate reductase A (NarGHI), but not respiratory membrane-bound molybdoenzyme dimethylsulfoxide reductase (DmsABC) |
721512 |
| 2.8.1.11 | more |
L-cysteine can serve as the source of the sulfur for the biosynthesis of MPT in vitro but only in the presence of a persulfide-containing sulfurtransferase such as IscS, cysteine sulfinate desulfinase (CSD), or CsdB. But IscS is not required for the in vivo sulfuration of MPT synthase. Development of a fully defined in vitro system in which an inactive form of MPT synthase can be activated by incubation with MoeB, Mg-ATP, L-cysteine, and one of the NifS-like sulfurtransferases, and the addition of precursor Z to the in vitro system gives rise to MPT formation, overview. Three NifS-like sulfurtransferases can catalyze the activation of MPT synthase |
722618 |
| 2.8.1.11 | more |
maturation of the holoenzyme is not cofactor-insertion dependent |
721512 |
| 2.8.1.11 | evolution |
MOCS3 belongs to the class of rhodaneses that is found in combination with another protein domain, and contains one rhodanese domain of 158 amino acids at the C-terminus with a sequence identity of less than 20% with the classic two-domain rhodaneses, phylogenetic analysis of MoeB homologues, overview |
722226 |
| 2.8.1.11 | more |
MOCS3 interacts with both URM1, an ubiquitin-like modifier involved in the specific formation of 2-thiouridine tRNA in humans, and MOCS2A in vivo and in vitro, MOCS2A and URM1 are beta-grasp fold proteins that contain a highly conserved C-terminal double glycine motif. Deletion of the C-terminal glycine of either MOCS2A or URM1 results in a loss of interaction with MOCS3. Extension of the C-terminus with an additional glycine of MOCS2A and URM1 alters the localization of MOCS3from the cytosol to the nucleus |
722756 |
| 2.8.1.11 | physiological function |
MoeB functions to sulfurylate MoaD, and in the structure of the MoeB-MoaD complex, Ala228 is located in the interface region between the two proteins |
721512 |
| 2.8.1.11 | more |
MoeB-MoaD complex formation by protein-protein interactions, MoaD binds to MoeB only in the presence of ATP, while IscS is not essential for the binding of MoeB to YnjE, IscS and MoeB bind independently to YnjE |
722726 |
| 2.8.1.11 | physiological function |
molybdopterin synthase sulfurase is involved in sulfur transfer to the C-terminus of the molybdopterin synthase, which synthesizes the molybdenum cofactor, that play a central role in several enzymes, role of specific conserved residues in the six amino acid active site loop of MOCS3-RLD in thiosulfate sulfurtransferase activity |
722226 |
