Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | autoproteolytic activation, mechanism | Elizabethkingia meningoseptica |
Crystallization (Comment) | Organism |
---|---|
D151N mutant AGA precursor, complexed with glycine and without glycine | Elizabethkingia meningoseptica |
Protein Variants | Comment | Organism |
---|---|---|
D151N | mutation completely abolishes autoproteolysis, mutation eradicates the backbone distortion near the scissile peptide bond | Elizabethkingia meningoseptica |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
glycine | binding mode | Elizabethkingia meningoseptica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Elizabethkingia meningoseptica | - |
- |
- |
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 (Comment) | Organism |
---|---|
- |
Elizabethkingia meningoseptica |
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 | Comment | Organism |
---|---|---|
GA | - |
Elizabethkingia meningoseptica |
glycosylasparaginase | - |
Elizabethkingia meningoseptica |
More | member of the N-terminal nucleophile hydrolases | Elizabethkingia meningoseptica |