Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | D4GTS4 | - |
- |
Haloferax volcanii DSM 3757 | D4GTS4 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N6-[SAMP1]-[MoaE]-L-lysine + H2O | MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1 | Haloferax volcanii | [MoaE]-L-lysine + SAMP1 | - |
? | |
N6-[SAMP1]-[MoaE]-L-lysine + H2O | MoaE, i.e. molybdopterin synthase large subunit homolog. Residue K240 of MoaE is isopeptide-linked to SAMP1 | Haloferax volcanii DSM 3757 | [MoaE]-L-lysine + SAMP1 | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | molybdopterin synthase activity is inhibited by covalent linkage of SAMP1 to the large subunit (MoaE) of MPT synthase. Metalloprotease JAMM1 cleaves the covalently linked inactive form of SAMP1-MoaE to the free functional individual SAMP1 and MoaE subunits of molybdopterin synthase | Haloferax volcanii |