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Literature summary for 4.6.1.12 extracted from

  • Lherbet, C.; Pojer, F.; Richard, S.B.; Noel, J.P.; Poulter, C.D.
    Absence of substrate channeling between active sites in the Agrobacterium tumefaciens IspDF and IspE enzymes of the methyl erythritol phosphate pathway (2006), Biochemistry, 45, 3548-3553.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens
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 ispD and ispF genes are fused and encode a bifunctional 4-diphosphocytidyl-2C-methyl-D-erythritol synthase and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information bifunctional 4-diphosphocytidyl-2C-methyl-D-erythritol synthase/2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase enzyme associates in solution with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, i.e. ispE protein. No evidence for substrate channeling during the three enzyme’s subsequent catalytic reactions Agrobacterium tumefaciens ?
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 ?

Subunits

Subunits Comment Organism
More bifunctional 4-diphosphocytidyl-2C-methyl-D-erythritol synthase/2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase enzyme associates in solution with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, i.e. ispE protein. No evidence for substrate channeling during the three enzyme’s subsequent catalytic reactions Agrobacterium tumefaciens