EC Number |
Protein Variants |
Reference |
---|
6.3.4.15 | A43G |
catalytic efficiency is 2fold lower than catalytic efficiency of wild-type enzyme |
-, 671759 |
6.3.4.15 | D571N |
naturally occuring mutation, important in positioning K579 in the AMP binding site |
691104 |
6.3.4.15 | D615Y |
naturally occuring mutation in the loop between alpha3 and beta6 that cover AMP, may coordinate oxygens of the AMP phosphate |
691104 |
6.3.4.15 | D634Y |
naturally occuring mutation of a solvent exposed residue, distal to active site on alpha4 and alpha5, respectively |
691104 |
6.3.4.15 | D715G |
naturally occuring mutation on beta9, may be involved in capping and stabilising the catalytic domain structure |
691104 |
6.3.4.15 | DELTA1-81 |
elimination of N-terminal domain plus part of the central domain, complete loss of ligase activity |
-, 745788 |
6.3.4.15 | DELTA1-81 |
elimination of N-terminal domain plus part of the central domain, loss of ligase activity |
-, 746268 |
6.3.4.15 | DELTA2-63 |
elimination of N-terminal domain, mutant shows normal ligase activity |
-, 746268 |
6.3.4.15 | DELTA2-65 |
elimination of N-terminal domain, complete loss of ligase activity |
-, 745788 |
6.3.4.15 | DELTA2-65 |
elimination of N-terminal domain, mutant shows normal ligase activity |
-, 746268 |