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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.148 D152A inactive mutant enzyme Agrobacterium tumefaciens
2.7.7.60 D152A catalytically inactive Agrobacterium tumefaciens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.148 additional information Agrobacterium tumefaciens in Agrobacterium tumefaciens the ispD and ispF genes are fused to encode a bifunctional enzyme that catalyzes the first (synthesis of 4-diphosphocytidyl-2-C-methyl D-erythritol) and third (synthesis of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate) steps of isoprenoid biosynthetic pathway. Enzyme-generated intermediates are not transferred from the IspD active site in IspDF to the active site of IspE or from the active site in IspE to the active site of the IspF module of IspDF ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.148 Agrobacterium tumefaciens
-
-
-
2.7.7.60 Agrobacterium tumefaciens
-
 enzyme gene ispD is fused to gene ispF to encode a bifunctional enzyme catalyzing synthesis of 4-diphosphocytidyl2-C-methyl D-erythritol and of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
-
4.6.1.12 Agrobacterium tumefaciens
-
 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
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.148
-
 Agrobacterium tumefaciens

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.60 CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol no kinetic evidence for substrate channelling Agrobacterium tumefaciens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.148 additional information in Agrobacterium tumefaciens the ispD and ispF genes are fused to encode a bifunctional enzyme that catalyzes the first (synthesis of 4-diphosphocytidyl-2-C-methyl D-erythritol) and third (synthesis of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate) steps of isoprenoid biosynthetic pathway. Enzyme-generated intermediates are not transferred from the IspD active site in IspDF to the active site of IspE or from the active site in IspE to the active site of the IspF module of IspDF Agrobacterium tumefaciens ?
-
 ?
4.6.1.12 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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.60 monomer sedimentation velocity experiments, both wild-type and mutant D152A Agrobacterium tumefaciens
4.6.1.12 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

Synonyms

EC Number Synonyms Comment Organism
2.7.1.148 IspDF in Agrobacterium tumefaciens the ispD and ispF genes are fused to encode a bifunctional enzyme that catalyzes the first (synthesis of 4-diphosphocytidyl-2-C-methyl D-erythritol) and third (synthesis of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate) steps of isoprenoid biosynthetic pathway Agrobacterium tumefaciens