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Literature summary 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

Activating Compound

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

Crystallization (Commentary)

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

Protein Variants

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.99.22 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)

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

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.22 Staphylococcus aureus P65388
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.22 GTP the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor Staphylococcus aureus cyclic pyranopterin phosphate + diphosphate
-
 ?
4.1.99.22 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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.22 MoaA
-
 Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.22 22
-
 assay at Staphylococcus aureus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.22 9
-
 assay at Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.22 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