EC Number   |
Protein Variants |
Reference |
|---|
   3.2.1.62 | E373Q |
almost no activity |
680835 |
| 3.2.1.62 | E483Q |
inactive |
-, 732073 |
| 3.2.1.62 | G1363S |
the mutant protein is malfolded and enzymatically inactive and can not exit the endoplasmic reticulum. The mutation creates an additional N-glycosylation site that is characteristic of a temperature-sensitive protein. The potential glycosylation site generated by the mutation is not the cause of defective trafficking of LPH-G1363S or its reduced enzymatic activity. Intracellular transport and enzymatic activity, but not correct folding are partially restored by expression at 20°C. The mutant is responsible for an increased turnover rate |
698078 |
| 3.2.1.62 | G1363S/N1361A |
eliminates the N-glycosylation site, does not restore the features of wild-type LPH |
698078 |
| 3.2.1.62 | I1697N |
introduction of a glycosylation site, reduced transport rate to the plasma membrane |
208744 |
| 3.2.1.62 | I1697N |
introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency |
208744 |
| 3.2.1.62 | more |
loop-out mutagenesis and construction of deletion or individual domain forms of LPH. Removal of domain IV, which contains lactase, results in a diminished phlorizin hydrolase activity, lack of dimerization in the endoplasmic reticulum, but accelerated transport kinetics from the endoplasmic reticulum to the Golgi apparatus. By contrast, deletion of domain III, which harbors phlorizin hydrolase, generates a malfolded protein that is blocked in the endoplasmic reticulum. Transport kinetics and enzyme activity of LPH and deletion mutants differ |
709142 |
| 3.2.1.62 | more |
removal of domain I (LPHDELTA1) results in a malfolded ER-localized protein. Enzyme without domain II (LPHDELTA2) is normally transported along the secretory pathway, but does not dimerize nor is enzymatically active. The lactase activity is not detectable in LPHDELTA1 and LPHDELTA2. Phlorizin hydrolase activity is only detectable in LPHDELTA2, albeit at substantially reduced levels of 4.3% |
756114 |
| 3.2.1.62 | more |
the naturally occurring polymorphism T13910C, i.e. rs4988235, causes lactose intolerance in the C-variant, associated with lower dietary calcium intake and serum calcium levels but not with BMD or fractures. Genotyping and phenotype, overview. The polymorphism is not associated with the genetic variations in the VDR gene, and no interactions between the two genotypes |
709206 |
| 3.2.1.62 | P1743S |
introduction of a glycosylation site, reduced transport rate to the plasma membrane |
208744 |
