EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.83 | 1,2-Cyclohexanedione | results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue | Micrococcus luteus | |
2.5.1.83 | 2,3-Butanedione | results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue | Micrococcus luteus | |
2.5.1.83 | iodoacetamide | results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue | Micrococcus luteus | |
2.5.1.83 | N-ethylmaleimide | results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue | Micrococcus luteus | |
2.5.1.83 | p-chloromercuribenzoate | results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue | Micrococcus luteus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.83 | Micrococcus luteus | O66127 and O66129 | O66127: component A of hexaprenyl diphosphate synthase, O66129: component B of hexaprenyl diphosphate synthase | - |
2.5.1.83 | Micrococcus luteus B-P 26 | O66127 and O66129 | O66127: component A of hexaprenyl diphosphate synthase, O66129: component B of hexaprenyl diphosphate synthase | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.83 | (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate | - |
Micrococcus luteus | 3 diphosphate + all-trans-hexaprenyl diphosphate | - |
? | |
2.5.1.83 | (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate | - |
Micrococcus luteus B-P 26 | 3 diphosphate + all-trans-hexaprenyl diphosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.83 | ? | catalytic site of the synthase is formed by cooperative interaction between components A and B | Micrococcus luteus |