EC Number   |
Protein Variants |
Reference |
|---|
   2.4.1.345 | DELTA59-70 |
mutation of the beta3-beta2 loop: mutant enzyme is still able to bind GDP with affinities in the submicromolar but PimA is completely inactivated and the ability of the protein to bind phospholipid aggregates is drastically impaired |
680790 |
| 2.4.1.345 | E199A |
complete loss of activity |
-, 704519 |
| 2.4.1.345 | E274A |
mutation results in complete enzyme inactivation |
680790 |
| 2.4.1.345 | H118A |
mutation results in complete enzyme inactivation |
680790 |
| 2.4.1.345 | K123A |
23% loss of activity |
-, 704519 |
| 2.4.1.345 | more |
a PimA mutant in which the beta3-alpha2 loop is deleted by mutagenesis (PimA5970) is still able to bind GDP with affinities in the submicromolar range but inactive and impaired the abilityto bind phospholipid aggregates |
-, 680790 |
| 2.4.1.345 | more |
in a polyprotein containing PimA flanked by four copies of the I27 protein, which provides a mechanical fingerprint, PimA exhibits weak mechanical stability albeit displaying beta-sheet topology expected to unfold at much higher forces. PimA unfolds following heterogeneous multiple step mechanical unfolding pathways at low force akin to molten globule states. The open and closed conformations of the GT-B glycosyltransferase are largely present in solution, and in addition, PimA experiences remarkable flexibility that corresponds to the N-terminal Rossmann fold domain |
-, 736430 |
| 2.4.1.345 | N63A |
complete loss of activity |
704519 |
| 2.4.1.345 | N79A |
29% loss of actiity |
704519 |
| 2.4.1.345 | Q18A |
90% loss of activity |
704519 |
