EC Number   |
Protein Variants |
Reference |
|---|
   3.4.17.21 | DELTA1-42 |
the recombinantly expressed extracellular domain has a cytosolic localization compared to sell surface membrane localization of the full-length enzyme. Less than 5% of the activity of the wild-type enzyme |
656634 |
| 3.4.17.21 | DELTA20-42 |
mutant enzyme omitting the transmembrane domain is associated with the cell surface membrane as is the full-length enzyme. Less than 5% of the activity of the wild-type enzyme |
656634 |
| 3.4.17.21 | E424A |
catalytically inactive, series of X-ray structures of complexes a panel of naturally occurring polyglutamylated folates |
731799 |
| 3.4.17.21 | E424A |
inactive mutant enzyme |
753551 |
| 3.4.17.21 | E424A |
mutant, complete loss of catalytic activity |
696330 |
| 3.4.17.21 | H380G |
site-directed mutagenesis, active site mutant, inactive mutant |
668154 |
| 3.4.17.21 | H475Y |
C1561T single nucleotide polymorphism located in the putative catalytic region of the enzyme |
697394 |
| 3.4.17.21 | H475Y |
X-ray structure in complex with substrate N-acetyl-L-aspartyl-L-glutamate,wild-type and the H475 variant are functionally identical. both proteins share an almost identical arrangement of amino acids in the vicinity of residue 475, and the imidazole ring of wild-type His475 and the benzene ring of Tyr475 overlap spatiallyl |
731799 |
| 3.4.17.21 | K479R |
in the presence of cycloheximide the mutant is less ubiquitinylated and degraded. Decrease in the level of glutamate carboxypeptidase II protein by histone deacetylase is significantly blocked by K479R mutants |
752648 |
| 3.4.17.21 | K491R |
in the presence of cycloheximide the mutant is less ubiquitinylated and degraded |
752648 |
