EC Number   |
General Information |
Reference |
|---|
   4.1.99.18 | evolution |
MoaA belongs to the S-adenosyl-L-methionine-dependent radical enzyme superfamily, members of which catalyse the formation of protein or substrate radicals by reductive cleavage of SAM by a [4Fe-4S] cluster |
-, 728595 |
| 4.1.99.18 | evolution |
MoaA is a member of the radical-SAM superfamily of proteins and harbors two [4Fe-4S]2+1+ clusters |
727013 |
| 4.1.99.18 | evolution |
MoaA is a member of the S-adenosylmethionine (SAM)-dependent radical enzyme superfamily |
727079 |
| 4.1.99.18 | metabolism |
MoaA and MoaC catalyze the first step in molybdopterin biosynthesis. This reaction involves a complex rearrangement in which C8 of guanosine triphosphtate is inserted between the C2' and the C3' carbons of the ribose |
727013 |
| 4.1.99.18 | metabolism |
MoaA and MoaC together catalyze the first step in molybdopterin biosynthesis, converting GTP to cyclic pyranopterin monophosphate |
727684 |
| 4.1.99.18 | metabolism |
the enzyme catalyzes teh first step of molybdenum cofactor biosynthesis, the formation of cyclic pyranopterin monophosphate, cPMP |
727079 |
| 4.1.99.18 | metabolism |
the enzymes is involved in the molybdenum cofactor (Moco) biosynthesis pathway. Together with MoaA, MoaC is involved in the conversion of guanosine triphosphate (GTP) to precursor Z, the first step in Moco synthesis |
-, 726621 |
| 4.1.99.18 | metabolism |
the formation of precursor Z from guanosine triphosphate in the Molybdenum cofactor (Moco) biosynthesis pathway is catalysed by two enzymes, MoaA and MoaC |
-, 728595 |
| 4.1.99.18 | more |
detailed structure analysis, docking, and molecular-dynamics simulations, active site structure and structure comparisons, overview |
-, 723849 |
| 4.1.99.18 | physiological function |
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor |
714888, 715257, 715420, 715468, 716730, 716738 |
