Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | intramolecular autoproteolytic activation with Gly-258 playing an important structural role, molecular activation mechanism | Homo sapiens |
Application | Comment | Organism |
---|---|---|
medicine | deficient AGA activity results in a lysosomal storage disease, aspartylglucosaminuria, resulting in progressive neurodegeneration, most of disease-causing mutations lead to defective molecular maturation of AGA | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression in COS-1 cells and in BHK-21 cells | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D200A | 87% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
D201A | 93% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
D70A | 44% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
G226A | inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
G258A | inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
K230A | 86% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
additional information | aspartylglucosaminuria-causing mutations, most of them lead to defective molecular maturation of AGA, effects of targeted amino acid substitutions on the activation process of AGA | Homo sapiens |
N225A | 45% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
S238A | 40% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
T33A | 48% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA | Homo sapiens |
T33S | same activity as wild-type AGA | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Homo sapiens | |
0.143 | - |
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose | pH 7, 37°C, purified wild-type AGA | Homo sapiens | |
0.444 | - |
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose | pH 7, 37°C, wild-type AGA | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum | AGA maturation, activation cleavage of the dimerized AGA precursors into the N-terminal alpha- and the C-terminal beta-subunits takes place in the endoplasmic reticulum | Homo sapiens | 5783 | - |
lysosome | enzymic catalysis takes place in lysosomes | Homo sapiens | 5764 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
44000 | - |
1 * 44000, monomeric AGA precursor, SDS-PAGE | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P20933 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 | Homo sapiens |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate | mechanism | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose + H2O | - |
Homo sapiens | ? | - |
? | |
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O | Thr-206 is the N-terminal nucleophile that acts as catalytic residue, Thr-206 is stabilized by hydrogen bonds from Ser-72 and Thr-224, enzyme structure | Homo sapiens | N-acetyl-beta-D-glucosaminylamine + L-aspartate | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 44000, monomeric AGA precursor, SDS-PAGE | Homo sapiens |
tetramer | (alpha,beta)2, enzymically active AGA | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
More | belongs to the N-terminal nucleophile hydrolase superfamily | Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Homo sapiens |