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Literature summary for 4.1.99.22 extracted from

  • Hänzelmann, P.; Schindelin, H.
    Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism (2006), Proc. Natl. Acad. Sci. USA, 103, 6829-6834.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.22

Activating Compound

Activating Compound Comment Organism Structure
MoaC protein the reaction is catalyzed by the S-adenosylmethionine-dependent enzyme MoaA and the accessory protein MoaC Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of wild-type MoaA, MoaA-R17A/R266A/R268A and MoaA in complex with 5'-GTP2.35 A resolution Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
N124A/N165A mutation reduces binding of 5'-GTP Staphylococcus aureus
R17A complete loss of activity Staphylococcus aureus
R17A/R266A/R268A complete loss of activity Staphylococcus aureus
R192A 80% loss of activity Staphylococcus aureus
R266A complete loss of activity Staphylococcus aureus
R268A complete loss of activity Staphylococcus aureus
R71A 80% loss of activity Staphylococcus aureus
S126A mutant enzyme with low activity Staphylococcus aureus
T73A mutant enzyme with low activity Staphylococcus aureus
Y30A mutant enzyme with low activity Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
iron-sulfur centre 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 Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP Staphylococcus aureus the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor cyclic pyranopterin phosphate + diphosphate
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 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus P65388
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor Staphylococcus aureus cyclic pyranopterin phosphate + diphosphate
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 ?
GTP 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 Staphylococcus aureus cyclic pyranopterin phosphate + diphosphate
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 ?

Synonyms

Synonyms Comment Organism
MoaA
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 Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 assay at Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre 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 Staphylococcus aureus