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Literature summary for 2.7.7.60 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

Protein Variants Comment Organism
D152A catalytically inactive Agrobacterium tumefaciens

Organism

Organism UniProt Comment Textmining
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
-

Reaction

Reaction Comment Organism Reaction ID
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

Subunits

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