EC Number   |
General Information |
Reference |
|---|
   2.7.7.67 | evolution |
structural comparisons and analyses, combined with functional studies, not only elucidated the mechanism governing the biosynthesis of phospholipids with ether-bonded isoprenoid chains by CTP transferase, but also provided insights into the evolution of this enzyme superfamily from archaea to bacteria and eukaryotes |
-, 760843 |
| 2.7.7.67 | metabolism |
the enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes |
-, 643326 |
| 2.7.7.67 | metabolism |
the enzyme is involved in the biosynthesis of polar lipids in archaea |
-, 692823 |
| 2.7.7.67 | more |
the enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP, modeling of the specific lipophilic substrate-binding site. Archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. CTP binds to one side of the central cavity of ApCarS and stabilizes the CPD through tight contacts. Recognition of CTP by ApCarS occurs through a combination of extensive polar and hydrophobic interactions, detailed overview |
-, 760843 |
| 2.7.7.67 | physiological function |
ApCarS is a CTP transferase |
-, 760843 |
