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Literature summary extracted from

  • Yoshida, I.; Koyama, T.; Ogura, K.
    Protection of hexaprenyl-diphosphate synthase of Micrococcus luteus B-P 26 against inactivation by sulphydryl reagents and arginine-specific reagents (1989), Biochim. Biophys. Acta, 995, 138-143.
    View publication on PubMed

Inhibitors

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

Organism

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
-

Substrates and Products (Substrate)

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
-
 ?

Subunits

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