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 (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 | 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 | 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 | 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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | P65388 | - |
- |
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
MoaA | - |
Staphylococcus aureus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Staphylococcus aureus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
assay at | Staphylococcus aureus |
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 |