3.5.1.26: N4-(beta-N-acetylglucosaminyl)-L-asparaginase
This is an abbreviated version!
For detailed information about N4-(beta-N-acetylglucosaminyl)-L-asparaginase, go to the full flat file.
Word Map on EC 3.5.1.26
-
3.5.1.26
-
lysosomal
-
aspartylglucosaminuria
-
lepidoptera
-
mitogenome
-
protein-coding
-
microsatellite-like
-
attta
-
poly-a
-
butterfly
-
a+t-rich
-
glycoasparagines
-
nymphalidae
-
aspartylglucosamine
-
dihydrouridine
-
trnaseragn
-
autoproteolysis
-
meningosepticum
-
hesperiidae
-
papilionidae
-
lrrna
-
pieridae
-
non-finnish
-
glcnac-asn
-
clover-leaf
-
medicine
-
lycaenidae
-
trnamet
-
diagnostics
- 3.5.1.26
- lysosomal
- aspartylglucosaminuria
- lepidoptera
-
mitogenome
-
protein-coding
-
microsatellite-like
-
attta
- poly-a
- butterfly
-
a+t-rich
- glycoasparagines
- nymphalidae
- aspartylglucosamine
- dihydrouridine
-
trnaseragn
-
autoproteolysis
- meningosepticum
- hesperiidae
- papilionidae
-
lrrna
- pieridae
-
non-finnish
- glcnac-asn
-
clover-leaf
- medicine
- lycaenidae
- trnamet
- diagnostics
Reaction
Synonyms
1-aspartamido-beta-N-acetylglucosamine amidohydrolase, 4-L-aspartylglucosylamine amido hydrolase, AGA, amidase-1, amidase-2, amidase-3, aspartylglucosaminidase, aspartylglucosylaminase, aspartylglucosylamine deaspartylase, aspartylglycosylamine amidohydrolase, AtAGA, beta-aspartylglucosylamine amidohydrolase, EC 3.5.1.37, GA, glucosylamidase, glycoasparaginase, glycosylasparaginase, LhAGA, More, N-aspartyl-beta-glucosaminidase, N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
ECTree
Advanced search results
Posttranslational Modification
Posttranslational Modification on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
glycoprotein
proteolytic modification
two potential N-glycosylation sites are detected along the sequence at Asn52 and Asn153
glycoprotein
only the alpha AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview
glycoprotein
-
Aurelia AGA possesses potential N-glycosylation sites, Asn36, Asn48, Asn168, and Asn213
glycoprotein
only the beta AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview
the enzyme is processed through autocatalytic cleavage, extracellular autocleavage and autoactivation
proteolytic modification
-
in the lysosomes, the C-termini of both alpha- and beta-subunits are trimmed by proteases, resulting in the mature form of AGA, though these trimming steps are not necessary for the catalytic activity of AGA
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
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
proteolytic modification
-
intramolecular autoproteolytic activation reaction
proteolytic modification
intramolecular autoproteolytic activation with Gly-258 playing an important structural role, molecular activation mechanism, dimerization and correct folding of the AGA precursor, activation cleavage of the dimerized AGA precursors into the N-terminal alpha- and the C-terminal beta-subunits takes place in the endoplasmic reticulum and results in the tetrameric, enzymically active (alpha,beta)2 molecule
proteolytic modification
the enzyme contains a subcellular targeting signal sequence
proteolytic modification
processing and activation of aspartylglucosaminidase by autocatalytic cleavage, overview. AGA is synthesized in the endoplasmic reticulum as a 346 amino acid (aa) polypeptide from which 23 residues of the signal peptide are removed. Very soon after synthesis in the endoplasmic reticulum, two AGA precursors homodimerize, inducing an autocatalytic cleavage of both precursors N-terminally to Thr206 into 27 kDa pro-alpha and 17 kDa subunits. After transport to lysosomes, the pro-alpha is C-terminally cleaved into 24 kDa mature alpha-subunit, whereas processing of the beta-subunit gives rise to the 14 kDa beta'-subunit. Neither of these lysosomal processing steps displays an effect on the enzyme activity
proteolytic modification
the enzyme is processed through autocatalytic cleavage. A subsequent autoprocessing results in a main-chain cleavage at the P-loop by a self-catalyzed peptide bond rearrangement via an N -> O acyl shift. This autoproteolysis event results in an active form of the hydrolase with separate alpha- and beta-subunits
proteolytic modification
the enzyme is synthesized as a single-chain precursor that requires an intramolecular autoprocessing to form a mature amidase
proteolytic modification
the enzyme is precessed through autocatalytic cleavage, extracellular autocleavage and autoactivation