EC Number   |
Protein Variants |
Reference |
|---|
   2.7.7.83 | A229T |
naturally occuring enzyme AGX1 mutation, and site-directed mutagenesis, the A229T mutation causes a reduction of protein thermal stability compared to wild-type AGX1, and AGX1A229T has lower activity in producing UDP-GlcNA. In diploid organisms, haploinsufficiency is a phenomenon in which a single copy of a functional gene is not sufficient to produce the normal/wild-type phenotype. The patient is only heterozygous for the UAP1 A229T missense mutation. The UAP1 gene is potentially haploinsufficient and LoF intolerant, and the heterozygous UAP1 A229T mutation is potentially pathogenic. The recombinant mutant enzyme shows a reduction of the melting temperature (Tm) by approximately 5.3°C compared to wild-type. The A229T mutation induces structural changes. The R228-E44 interaction is abolished in the AGX1A229T structure caused by the position shift of R228. The pushing effect is likely due to the bulkier side chain of threonine compared to that of alanine. Along with the conformational change of the N-terminal domain in the AGX1A229T structure, M218 is shifted by 0.8 A away from R169, weakening the Q112-R169-M218 interaction |
761091 |
| 2.7.7.83 | H308A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type |
729696 |
| 2.7.7.83 | K337A |
site-directed mutagenesis |
729696 |
| 2.7.7.83 | K340A |
site-directed mutagenesis |
729696 |
| 2.7.7.83 | more |
all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein |
760395 |
| 2.7.7.83 | more |
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein |
729696 |
| 2.7.7.83 | N331A |
site-directed mutagenesis |
729696 |
| 2.7.7.83 | R115A |
activity drastically affected |
722110 |
| 2.7.7.83 | R115A |
activity drastically affected, no dimer formation |
722110 |
| 2.7.7.83 | T80A |
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type |
760395 |
