Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Elizabethkingia miricola |
Crystallization (Comment) | Organism |
---|---|
purified recombinant mutant G172D enzyme precursor in presence of L-aspartic acid beta-hydroxamate, X-ray diffraction structure determination and analysis at 2.1 A resolution. Structures of the precursor and the mature form are found in a single crystal | Elizabethkingia miricola |
Protein Variants | Comment | Organism |
---|---|---|
G172D | the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines, the mutant can be stabilized by L-aspartic acid beta-hydroxamate for crystallization against proteolysis by other enzymes | Elizabethkingia miricola |
additional information | in vitro activation of autoproteolysis can be applied to enhance the hydrolase activity of the AGU mutant | Elizabethkingia miricola |
T203I | the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines. The mutant shows increased thermostability but 93% reduced enzyme activity compared to the wild-type enzyme. The mutant is unstable to proteolysis by other enzymes | Elizabethkingia miricola |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
lysosome | - |
Elizabethkingia miricola | 5764 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Elizabethkingia miricola | Q47898 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | - |
Elizabethkingia miricola |
proteolytic modification | autoproteolytic removal of a surface P loop blocking the catalytic center of the mature hydrolase is required to open up the hydrolase center, wild-type Genzyme autocleaves spontaneously | Elizabethkingia miricola |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes, the latter as single-chain precursors | Elizabethkingia miricola |
Synonyms | Comment | Organism |
---|---|---|
glycosylasparaginase | - |
Elizabethkingia miricola |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Elizabethkingia miricola |
General Information | Comment | Organism |
---|---|---|
malfunction | enzyme point mutation G172D inactivates the enzyme and causes the genetic disease aspartylglucosaminuria, a lysosomal storage disease due to metabolic disorder of lysosomes to digest Asn-linked glycoproteins, structural basis, overview | Elizabethkingia miricola |
additional information | a surface loop blocks the catalytic center of the mature hydrolase, autoproteolysis is therefore required to remove this P loop and open up the hydrolase center. Structures of the precursor and the mature form are found in a single crystal, structure comparisons, overview | Elizabethkingia miricola |