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Literature summary for 3.5.1.26 extracted from

  • Sui, L.; Lakshminarasimhan, D.; Pande, S.; Guo, H.C.
    Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria (2014), Structure, 22, 1855-1861.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes Elizabethkingia miricola

Crystallization (Commentary)

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

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

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
Elizabethkingia miricola 5764
-

Organism

Organism UniProt Comment Textmining
Elizabethkingia miricola Q47898
-
-

Posttranslational Modification

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 (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes, the latter as single-chain precursors Elizabethkingia miricola

Synonyms

Synonyms Comment Organism
glycosylasparaginase
-
Elizabethkingia miricola

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Elizabethkingia miricola

General Information

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