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Information on EC 3.5.1.26 - N4-(beta-N-acetylglucosaminyl)-L-asparaginase and Organism(s) Elizabethkingia miricola and UniProt Accession Q47898

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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]
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Elizabethkingia miricola
UNIPROT: Q47898
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The taxonomic range for the selected organisms is: Elizabethkingia miricola
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
glycosylasparaginase
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AGA
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-
-
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aspartylglucosaminidase
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-
-
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aspartylglucosylaminase
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-
-
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aspartylglucosylamine deaspartylase
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-
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aspartylglycosylamine amidohydrolase
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-
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beta-aspartylglucosylamine amidohydrolase
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-
-
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glucosylamidase
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-
-
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N-aspartyl-beta-glucosaminidase
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-
-
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N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
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-
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PATHWAY SOURCE
PATHWAYS
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme point mutation G172D inactivates the enzyme and causes the genetic disease aspartylglucosaminuria, a lysosomal storage disease due to metabolic disorder of lysosomes to digest Asn-linked glycoproteins, structural basis, overview
additional information
a surface loop blocks the catalytic center of the mature hydrolase, autoproteolysis is therefore required to remove this P loop and open up the hydrolase center. Structures of the precursor and the mature form are found in a single crystal, structure comparisons, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASPG_ELIMR
340
0
37263
Swiss-Prot
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant G172D enzyme precursor in presence of L-aspartic acid beta-hydroxamate, X-ray diffraction structure determination and analysis at 2.1 A resolution. Structures of the precursor and the mature form are found in a single crystal
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G172D
the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines, the mutant can be stabilized by L-aspartic acid beta-hydroxamate for crystallization against proteolysis by other enzymes
T203I
the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines. The mutant shows increased thermostability but 93% reduced enzyme activity compared to the wild-type enzyme. The mutant is unstable to proteolysis by other enzymes
additional information
in vitro activation of autoproteolysis can be applied to enhance the hydrolase activity of the AGU mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes, the latter as single-chain precursors
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of wild-type and mutant enzymes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sui, L.; Lakshminarasimhan, D.; Pande, S.; Guo, H.C.
Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria
Structure
22
1855-1861
2014
Elizabethkingia miricola (Q47898)
Manually annotated by BRENDA team