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Literature summary for 3.5.1.26 extracted from

  • Qian, X.; Guan, C.; Guo, H.C.
    A dual role for an aspartic acid in glycosylasparaginase autoproteolysis (2003), Structure, 11, 997-1003.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information autoproteolytic activation, mechanism Elizabethkingia meningoseptica

Crystallization (Commentary)

Crystallization (Comment) Organism
D151N mutant AGA precursor, complexed with glycine and without glycine Elizabethkingia meningoseptica

Protein Variants

Protein Variants Comment Organism
D151N mutation completely abolishes autoproteolysis, mutation eradicates the backbone distortion near the scissile peptide bond Elizabethkingia meningoseptica

Inhibitors

Inhibitors Comment Organism Structure
glycine binding mode Elizabethkingia meningoseptica

Organism

Organism UniProt Comment Textmining
Elizabethkingia meningoseptica
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification Asp-151 plays a dual role in the autoproteolytic processing mechanism, acting as the general base to activate the nucleophile and holding the distorted trans conformation that is critical for initiating an N-O acyl shift, generation of a mature/active enzyme from a single-chain precursor, autoproteolysis into two subunits: alpha and beta, mechanism Elizabethkingia meningoseptica

Purification (Commentary)

Purification (Comment) Organism
-
Elizabethkingia meningoseptica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O active site structure Elizabethkingia meningoseptica N-acetyl-beta-D-glucosaminylamine + L-aspartate
-
?

Synonyms

Synonyms Comment Organism
GA
-
Elizabethkingia meningoseptica
glycosylasparaginase
-
Elizabethkingia meningoseptica
More member of the N-terminal nucleophile hydrolases Elizabethkingia meningoseptica