EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.33 | - |
Staphylococcus epidermidis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.1.33 | hanging drop vapor diffusion method, using 0.25 M sodium formate and 16% (w/v) PEG 3350 | Staphylococcus epidermidis |
4.1.1.33 | wild-type and mutant S192A and D283A ternary complexes with inbhibitor 6-fluoromevalonate 5-diphosphate and ATPgammaS. During the catalytic mechanism, Asp283 correctly positions the mevalonate diphosphate acceptor substrate, while functioning as a catalytic base to abstract the acidic proton found on its C3-hydroxyl. This deprotonation facilitates an in-line transfer of the gamma-phosphoryl from the ATP donor. The Ser 107 side chain is appropriately positioned to hydrogen bond with both the beta- and gamma-phosphoryl groups of ATPgammaS within the ternary structure | Staphylococcus epidermidis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.33 | D283A | catalytically deficient enzyme with 100000fold decreased kcat value | Staphylococcus epidermidis |
4.1.1.33 | D283A | 10000fold decrease in kcat value | Staphylococcus epidermidis |
4.1.1.33 | S192A | catalytically deficient enzyme with 1000fold decreased kcat value | Staphylococcus epidermidis |
4.1.1.33 | S192A | 1000fold decrease in kcat value | Staphylococcus epidermidis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.33 | 6-fluoromevalonate diphosphate | competitive | Staphylococcus epidermidis | |
4.1.1.33 | diphosphoglycolyl-L-proline | competitive | Staphylococcus epidermidis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.33 | Mg2+ | required, bound to ATP | Staphylococcus epidermidis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.33 | ATP + (R)-5-diphosphomevalonate | Staphylococcus epidermidis | - |
ADP + phosphate + isopentenyl diphosphate + CO2 | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.33 | Staphylococcus epidermidis | Q9FD73 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.33 | - |
Staphylococcus epidermidis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.33 | ATP + (R)-5-diphosphomevalonate | - |
Staphylococcus epidermidis | ADP + phosphate + isopentenyl diphosphate + CO2 | - |
ir |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.33 | MDD | - |
Staphylococcus epidermidis |
4.1.1.33 | mevalonate diphosphate decarboxylase | - |
Staphylococcus epidermidis |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.33 | 0.00005 | - |
diphosphoglycolyl-L-proline | pH and temperature not specified in the publication | Staphylococcus epidermidis | |
4.1.1.33 | 0.0043 | - |
6-fluoromevalonate diphosphate | pH and temperature not specified in the publication | Staphylococcus epidermidis |