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.
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 |
|