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Literature summary for 4.1.99.22 extracted from

  • Iobbi-Nivol, C.; Leimkuehler, S.
    Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli (2013), Biochim. Biophys. Acta, 1827, 1086-1101.
    View publication on PubMed

Metals/Ions

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/ Products (Substrates)

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
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP
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Escherichia coli cyclic pyranopterin phosphate + diphosphate
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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
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Synonyms

Synonyms Comment Organism
MoaA
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Escherichia coli
MoaC
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Escherichia coli

Cofactor

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