Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | MoaA contains two oxygen-sensitive [4Fe-4S] clusters, one typical for S-adenosylmethionine-dependent radical enzymes at the N-terminus and an additional C-terminal cluster unique to MoaA proteins | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP | Escherichia coli | MoaA cleaves GTP by a radical mechanism, a 5'-desoxyadenosyl radical is generated from S-adenosyl-L-methionine at the N-terminal cluster facilitating hydrogen abstraction at either the C8 of the guanine or the C2' or C3' atoms of the ribose. Insertion of the formyl group between the ribose C2' and C3' carbons might also require radical mediation. MoaC is involved in the cleavage of the dihydropyrazine-type intermediate pyrophosphate group and formation of the cPMP cyclic phosphate group | cyclic pyranopterin phosphate + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP | - |
Escherichia coli | cyclic pyranopterin phosphate + diphosphate | - |
? | |
GTP | MoaA cleaves GTP by a radical mechanism, a 5'-desoxyadenosyl radical is generated from S-adenosyl-L-methionine at the N-terminal cluster facilitating hydrogen abstraction at either the C8 of the guanine or the C2' or C3' atoms of the ribose. Insertion of the formyl group between the ribose C2' and C3' carbons might also require radical mediation. MoaC is involved in the cleavage of the dihydropyrazine-type intermediate pyrophosphate group and formation of the cPMP cyclic phosphate group | Escherichia coli | cyclic pyranopterin phosphate + diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MoaA | - |
Escherichia coli |
MoaC | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | MoaAis a radical S-adenosyl-L-methionine (SAM) enzyme. S-adenosyl-L-methionine serves as the free radical initiator and undergoes cleavage to methionine and a 5'-deoxyadenosyl radical that in turn initiates radical formation of substrate molecules or of glycyl residues within the target enzymes to activate them for radical-based chemistry. The source of the electron required for the cleavage of SAM is a reduced form of a conserved FeS cluster within the protein | Escherichia coli |