Cloned (Comment) | Organism |
---|---|
MOCS1B overexpression in Escherichia coli strain BL21(DE3) | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00006 | - |
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | pH 7.6, 25°C, MOCS1B | Homo sapiens | |
0.00079 | - |
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | pH 7.6, 25°C, MoaC | Staphylococcus aureus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | MoaA harbors two [4Fe-4S]2+,1+ clusters, the N-terminal is used for reductive cleavage of S-adenosyl-L-methionine, the C-terminal [4Fe-4S] cluster binds various purine nucleoside 5'-triphosphates including GTP | Staphylococcus aureus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | Staphylococcus aureus | reaction of MoaC | cyclic pyranopterin phosphate + diphosphate | - |
? | |
GTP | Staphylococcus aureus | reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC | (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | - |
? | |
additional information | Staphylococcus aureus | MoaA catalyzes a unique radical C-C bond formation reaction via a 5'-deoxyadenosyl radical intermediate and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Staphylococcus aureus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant MOCS1B from Escherichia coli strain BL21(DE3) by streptomycin sulfate and ammonium sulfate precipitation steps, nickel affinity chromatography, gell filtration, and ultrafiltration | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | reaction of MoaC | Staphylococcus aureus | cyclic pyranopterin phosphate + diphosphate | - |
? | |
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | reaction of MoaC, which is responsible for the formation of the cyclic phosphate | Staphylococcus aureus | cyclic pyranopterin phosphate + diphosphate | NMR spectroscopy product analysis | ? | |
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | reaction of MOCS1B, responsible for the formation of the cyclic phosphate | Homo sapiens | cyclic pyranopterin phosphate + diphosphate | NMR spectroscopy product analysis | ? | |
GTP | reaction of MoaA with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC | Staphylococcus aureus | (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | - |
? | |
GTP | reaction of MoaA | Staphylococcus aureus | (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate | NMR spectroscopy product analysis | ? | |
additional information | MoaA catalyzes a unique radical C-C bond formation reaction via a 5'-deoxyadenosyl radical intermediate and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring | Staphylococcus aureus | ? | - |
? | |
additional information | MoaA/C coupled assay. MoaA catalyzes a unique radical C-C bond formation reaction and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring | Staphylococcus aureus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MoaA | - |
Staphylococcus aureus |
MoaC | - |
Staphylococcus aureus |
MOCS1B | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at, MoaA and MoaC | Staphylococcus aureus |
25 | - |
assay at, MOCS1B | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at, MoaA and MoaC | Staphylococcus aureus |
7.6 | - |
assay at, MOCS1B | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | MoaA as a radical S-adenosyl-L-methionine enzyme | Staphylococcus aureus |