Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase and Organism(s) Mus musculus

for references in articles please use BRENDA:EC3.5.1.26
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free alpha-amino and alpha-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase]
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glycosylasparaginase, aspartylglucosaminidase, ataga, glycoasparaginase, amidase-2, 1-aspartamido-beta-n-acetylglucosamine amidohydrolase, n-aspartyl-beta-glucosaminidase, aspartylglucosylaminase, amidase-3, n4-(n-acetyl-beta-glucosaminyl)-l-asparagine amidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartylglucosaminidase
-
-
-
-
aspartylglucosylaminase
-
-
-
-
aspartylglucosylamine deaspartylase
-
-
-
-
aspartylglycosylamine amidohydrolase
-
-
-
-
beta-aspartylglucosylamine amidohydrolase
-
-
-
-
glucosylamidase
-
-
-
-
glycosylasparaginase
-
-
N-aspartyl-beta-glucosaminidase
-
-
-
-
N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free alpha-amino and alpha-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase]
CAS REGISTRY NUMBER
COMMENTARY hide
9075-24-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
aspartylglycosaminuria is a lysosomal storage disease caused by deficient activity of glycosylasparaginase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASPG_MOUSE
346
0
37022
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
each polypeptide N-glycosylated
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 80
-
irreversible inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable at higher pH values, stable in the presence of SDS
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
a high dose enzyme replacement therapy with glycosylasparaginase in newborn aspartylglycosaminuria mice is up to 2fold more effective in reducing the amount of the accumulated storage material from the brain tissue than enzyme replacement therapy in adult aspartylglycosaminuria animals
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tollersrud, O.K.; Aronson, N.
Comparison of liver glycosylasparaginases from six vertebrates
Biochem. J.
282
891-897
1992
Bos taurus, Gallus gallus, Homo sapiens, Mus musculus, Rattus sp., Sus scrofa
Manually annotated by BRENDA team
Dunder, U.; Valtonen, P.; Kelo, E.; Mononen, I.
Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice
J. Inherit. Metab. Dis.
33
611-617
2010
Mus musculus
Manually annotated by BRENDA team