EC Number   |
General Information |
Reference |
|---|
    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 | 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 | malfunction |
mutation of the putative persulfide-forming active-site cysteine residue C412 abolishes the sulfurtransferase activity of MOCS3-RLD completely |
723621 |
| 2.8.1.11 | malfunction |
the moeB mutant of Escherichia coli contains inactive MPT synthase devoid of the thiocarboxylate |
722618 |
| 2.8.1.11 | metabolism |
the enzyme catalyzes the second step of the molybdenum cofactor (Moco) biosynthesis |
722726 |
| 2.8.1.11 | metabolism |
the enzyme is involved in the biosynthesis of the molybdenum cofactor divided into three steps: conversion of GTP to precursor, transformation of the precursor to molybdopterin, and insertion of molybdenum into MPT to form the molybdenum cofactor |
722226 |
| 2.8.1.11 | metabolism |
the enzyme is involved in the biosynthesis of the molybdenum cofactor, catalyzing 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. After the transfer of sulfur from MPT synthase to precursor Z, MPT synthase is present in an inactive, desulfurated form lacking the C-terminal thiocarboxylate group at the MoaD subunit of the protein |
722618 |
| 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 | 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 |
