The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). In bacteria and plants the reaction is catalysed by MoaA and Cnx2, respectively. In mammals it is catalysed by the MOCS1A domain of the bifunctional MOCS1 protein, which also catalyses EC 4.6.1.17, cyclic pyranopterin monophosphate synthase. The enzyme belongs to the superfamily of radical S-adenosyl-L-methionine (radical SAM) enzymes, and contains two oxygen-sensitive FeS clusters.
The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). In bacteria and plants the reaction is catalysed by MoaA and Cnx2, respectively. In mammals it is catalysed by the MOCS1A domain of the bifunctional MOCS1 protein, which also catalyses EC 4.6.1.17, cyclic pyranopterin monophosphate synthase. The enzyme belongs to the superfamily of radical S-adenosyl-L-methionine (radical SAM) enzymes, and contains two oxygen-sensitive FeS clusters.
product has a methylene bridge in place of an oxygen between the alpha and beta phosphate groups and product is an uncleavable substrate analogue of cyclic pyranopterin monophosphate synthase accessory protein MoaC
pyranopterin triphosphate is formed as a by-product, the amount is 0.4Ā3% of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine formed
the reaction is catalyzed by the S-adenosyl-L-methionine-dependent enzyme MoaA and the accessory protein MoaC. This reaction involves the radical-initiated intramolecular rearrangement of the guanine C8 atom
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
MoaA catalyzes a unique radical C-C bond formation reaction via a 5'-deoxyadenosyl radical intermediate and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring
MoaA/C coupled assay. MoaA catalyzes a unique radical C-C bond formation reaction and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring
MoaA catalyzes a unique radical C-C bond formation reaction via a 5'-deoxyadenosyl radical intermediate and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring
binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate
MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of S-adenosyl-L-methionine and generates a 5'-deoxyadenosyl radical, and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding andor activation. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
MoaA harbors two [4Fe-4S]2+,1+ clusters, the N-terminal is used for reductive cleavage of S-adenosyl-L-methionine, the C-terminal [4Fe-4S] cluster binds various purine nucleoside 5'-triphosphates including GTP
binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate
MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of S-adenosyl-L-methionine and generates a 5'-deoxyadenosyl radical, and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding andor activation. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
the GG motif is essential for the activity of MoaA to produce (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate from GTP, and synthetic peptides corresponding to the C-terminal region of wild-type MoaA rescue the GTP 3',8-cyclase activity of the GG-motif mutants. The C-terminal tail containing the GG motif interacts with the SAM-binding pocket of MoaA, and is essential for the binding of SAM and subsequent radical initiation
the physiological function of MoaA is the conversion of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate (GTP 3?,8-cyclase), and that of MoaC is to catalyze the rearrangement of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate into cyclic pyranopterin
crystals are grown under anaerobic conditions, hanging drop vapor diffusion technique, crystals belong to space group P2(1)2(1)2(1) with cell dimensions of a = 48.1, b = 102.4, and c = 191.2 A and contain two molecules per asymmetric unit, structures of MoaA in the apo-state (2.8 A) and in complex with S-adenosyl-L-methionine (2.2 A)