EC Number   |
Subunits |
Reference  |
|---|
    4.6.1.12 | trimer |
3 * 17300 |
-, 654130 |
| 4.6.1.12 | ? |
x * 21348, electrospray mass spectrometry |
655417 |
| 4.6.1.12 | trimer |
homotrimeric quarternary structure built around a central hydrophobic cavity and three externally facing active sites |
656112 |
| 4.6.1.12 | hexamer |
complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution |
656263 |
| 4.6.1.12 | More |
complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution |
656263 |
| 4.6.1.12 | More |
the monofunctional enzyme 2C-methyl-D-erythritol-4-phosphate cytidyltransferase and 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase shows physical association |
656263 |
| 4.6.1.12 | trimer |
- |
656498, 657196 |
| 4.6.1.12 | ? |
x * 17000, SDS-PAGE |
657177 |
| 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 enzymes subsequent catalytic reactions |
672138 |
| 4.6.1.12 | ? |
x * 26100, calculated |
681826 |
