BRENDA - Enzyme Database show
show all sequences of 3.5.1.26

Autoproteolytic activation of human aspartylglucosaminidase

Saarela, J.; Oinonen, C.; Jalanko, A.; Rouvinen, J.; Peltonen, L.; Biochem. J. 378, 363-371 (2004)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
intramolecular autoproteolytic activation with Gly-258 playing an important structural role, molecular activation mechanism
Homo sapiens
Application
Application
Commentary
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(Commentary)
Commentary
Organism
expression in COS-1 cells and in BHK-21 cells
Homo sapiens
Engineering
Amino acid exchange
Commentary
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 [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Localization
Commentary
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 [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44000
-
1 * 44000, monomeric AGA precursor, SDS-PAGE
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P20933
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
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 (Commentary)
Commentary
Organism
-
Homo sapiens
Reaction
Reaction
Commentary
Organism
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate
mechanism
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose + H2O
-
654537
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
654537
Homo sapiens
N-acetyl-beta-D-glucosaminylamine + L-aspartate
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 44000, monomeric AGA precursor, SDS-PAGE
Homo sapiens
tetramer
(alpha,beta)2, enzymically active AGA
Homo sapiens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Homo sapiens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
intramolecular autoproteolytic activation with Gly-258 playing an important structural role, molecular activation mechanism
Homo sapiens
Application (protein specific)
Application
Commentary
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(Commentary) (protein specific)
Commentary
Organism
expression in COS-1 cells and in BHK-21 cells
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
Localization
Commentary
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44000
-
1 * 44000, monomeric AGA precursor, SDS-PAGE
Homo sapiens
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
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 (Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose + H2O
-
654537
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
654537
Homo sapiens
N-acetyl-beta-D-glucosaminylamine + L-aspartate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 44000, monomeric AGA precursor, SDS-PAGE
Homo sapiens
tetramer
(alpha,beta)2, enzymically active AGA
Homo sapiens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Homo sapiens
Other publictions for EC 3.5.1.26
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735290
Sui
Structural basis of a point mu ...
Elizabethkingia miricola
Structure
22
1855-1861
2014
-
-
1
1
3
-
-
-
1
-
-
-
-
1
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
3
-
-
-
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
2
-
-
-
712162
Vinchon
Molecular and biochemical anal ...
Asobara tabida
Insect Biochem. Mol. Biol.
40
38-48
2010
-
-
-
-
-
-
-
-
1
-
7
1
-
3
-
1
-
-
-
3
-
-
2
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
7
1
-
-
1
-
-
3
-
-
2
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
712651
Dunder
Early initiation of enzyme rep ...
Mus musculus
J. Inherit. Metab. Dis.
33
611-617
2010
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
720247
Wang
Crystallographic snapshot of g ...
Flavobacterium sp.
J. Mol. Biol.
403
120-130
2010
-
-
-
1
1
-
1
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712919
Kelo
Depletion of L-asparagine supp ...
Homo sapiens
Leukemia
23
1167-1171
2009
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681417
Wang
Crystallographic snapshot of a ...
Elizabethkingia meningoseptica
J. Mol. Biol.
366
82-92
2007
-
-
-
1
1
-
-
-
1
-
-
1
-
3
-
-
-
-
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
682793
Mills
Diagnosis of congenital disord ...
Homo sapiens
Proteomics
6
2295-2304
2006
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669745
Jackson
Elevation of plasma aspartylgl ...
Homo sapiens
J. Inherit. Metab. Dis.
28
1197-1198
2005
-
1
-
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654537
Saarela
Autoproteolytic activation of ...
Homo sapiens
Biochem. J.
378
363-371
2004
1
1
1
-
11
-
-
3
2
-
1
-
-
3
-
1
1
1
-
-
-
-
2
2
1
-
-
-
1
-
-
-
-
-
-
1
1
1
-
-
11
-
-
-
-
3
2
-
1
-
-
-
1
1
-
-
-
-
2
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
668879
Saarela
A novel aspartylglucosaminuria ...
Homo sapiens
Hum. Mutat.
24
350-351
2004
-
-
1
-
1
-
-
-
2
-
-
1
-
2
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657367
Qian
A dual role for an aspartic ac ...
Elizabethkingia meningoseptica
Structure
11
997-1003
2003
1
-
-
1
1
-
1
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654334
Risley
Glycosylasparaginase activity ...
Homo sapiens
Arch. Biochem. Biophys.
391
165-170
2001
1
1
-
-
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656376
Risley
Glycosylasparaginase inhibitio ...
Homo sapiens
J. Enzyme Inhib.
16
269-274
2001
1
1
-
-
-
-
11
1
-
-
-
1
-
2
-
1
-
1
-
1
-
-
2
1
1
-
-
-
1
-
-
-
10
-
-
1
1
-
-
-
-
-
-
11
10
1
-
-
-
1
-
-
1
-
-
1
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
209049
Cui
Purification and crystallizati ...
Elizabethkingia meningoseptica
Acta Crystallogr. Sect. D
55
1961-1964
1999
-
-
1
1
1
1
-
-
-
-
-
1
-
3
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209048
Saarela
Activation and oligomerization ...
Homo sapiens
J. Biol. Chem.
273
25320-25328
1998
-
-
1
-
3
-
-
-
1
-
-
1
-
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209047
Noronkoski
Recombinant human glycosylaspa ...
Homo sapiens
FEBS Lett.
412
149-152
1997
-
-
1
-
-
-
2
2
1
-
-
2
-
2
-
-
1
-
-
-
1
-
3
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
-
-
-
2
1
2
1
-
-
2
-
-
-
1
-
-
1
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
209050
Liu
Purification, biochemistry and ...
Bos taurus, Rattus sp., Spodoptera frugiperda
Glycobiology
6
527-536
1996
-
-
-
-
-
-
-
1
-
-
4
4
-
8
-
-
1
-
-
3
1
-
4
4
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
4
4
-
-
-
1
-
3
1
-
4
4
-
-
1
-
-
1
-
-
-
-
-
-
-
-
209051
Tikkanen
Functional analyses of active ...
Homo sapiens
EMBO J.
15
2954-2960
1996
-
-
1
-
6
-
-
1
2
-
-
1
-
2
-
-
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
1
2
-
-
1
-
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209052
Park
Glycosylation and phosphorylat ...
Homo sapiens
Arch. Biochem. Biophys.
328
73-77
1996
-
-
1
-
3
-
-
-
1
-
-
-
-
3
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209053
Mononen
Enzymatic diagnosis of asparty ...
Homo sapiens
Clin. Chem.
40
385-388
1994
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
6
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209054
Tarentino
The first demonstration of a p ...
Elizabethkingia meningoseptica
Biochem. Biophys. Res. Commun.
197
179-186
1993
-
-
-
-
-
-
2
-
2
-
3
3
-
4
-
-
1
-
-
1
1
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
3
3
-
-
-
1
-
1
1
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209055
Enomaa
-
Human aspartylglucosaminidase ...
Homo sapiens
Biochem. J.
286
613-618
1992
-
-
-
-
-
-
2
-
1
-
-
-
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209056
Rip
Purification and structure of ...
Homo sapiens
Biochem. J.
288
1005-1010
1992
-
-
-
-
-
-
-
-
-
-
3
-
-
2
-
1
1
-
-
2
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
1
1
-
2
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
209057
Tollersrud
Comparison of liver glycosylas ...
Bos taurus, Gallus gallus, Homo sapiens, Mus musculus, Rattus sp., Sus scrofa
Biochem. J.
282
891-897
1992
-
-
-
-
-
6
-
-
-
-
2
6
-
14
-
6
6
-
-
12
6
-
6
5
-
-
6
-
6
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
2
6
-
-
6
6
-
12
6
-
6
5
-
-
6
-
6
-
-
-
-
-
-
-
-
-
209058
Kaartinen
Glycoasparaginase in human uri ...
Homo sapiens
Biochim. Biophys. Acta
1097
28-30
1991
-
1
-
-
-
-
-
1
1
-
3
1
-
2
-
-
1
-
-
2
1
-
1
1
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
3
1
-
-
-
1
-
2
1
-
1
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
209059
Kaartinen
Glycosasparaginase from human ...
Homo sapiens
J. Biol. Chem.
266
5860-5869
1991
-
-
-
-
-
-
1
1
-
-
3
1
-
2
-
-
1
-
-
2
1
1
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
3
1
-
-
-
1
-
2
1
1
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
209060
Halila
Human leucocyte aspartylglucos ...
Homo sapiens
Biochem. J.
276
251-256
1991
-
-
-
-
-
-
-
-
-
-
5
1
-
2
-
-
1
-
-
2
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
1
-
-
-
1
-
2
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209061
McGovern
Purification and properties of ...
Homo sapiens
J. Biol. Chem.
258
10743-10747
1983
-
-
-
-
-
-
-
1
2
-
2
1
-
2
-
-
1
-
-
2
1
-
1
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
2
-
2
1
-
-
-
1
-
2
1
-
1
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
209062
Dugal
Effect of different compounds ...
Homo sapiens
Biochem. J.
171
799-802
1978
3
-
-
-
-
-
2
-
-
-
1
1
-
2
-
-
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
2
-
-
-
-
1
1
-
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209063
Dugal
Purification and some properti ...
Homo sapiens
Biochem. J.
165
497-502
1977
-
-
-
-
-
-
5
1
-
-
-
1
-
2
-
-
1
-
-
2
2
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
1
-
-
-
1
-
-
-
1
-
2
2
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
209064
Dugal
Measurement of 1-aspartamido-b ...
Homo sapiens
Biochem. J.
163
9-14
1977
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
6
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
6
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209067
Tanaka
Specificity studies of 4-L-asp ...
Sus scrofa
J. Biochem.
73
1285-1289
1973
-
-
-
-
-
-
2
6
-
-
-
-
-
1
-
-
1
-
-
2
1
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
6
-
-
-
-
-
-
-
1
-
2
1
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
209068
Kohno
Purification and properties of ...
Sus scrofa
Biochim. Biophys. Acta
258
600-617
1972
-
-
-
-
-
1
6
3
-
-
1
-
-
1
-
-
1
-
-
1
1
1
3
-
-
-
-
-
2
-
1
-
1
-
-
-
-
-
-
-
-
1
-
6
1
3
-
-
1
-
-
-
-
1
-
1
1
1
3
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
209065
Tarentino
The purification and propertie ...
Gallus gallus
Arch. Biochem. Biophys.
130
295-303
1969
-
-
-
-
-
-
1
1
-
-
1
-
-
1
-
-
1
-
-
1
-
1
4
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
1
-
1
-
1
4
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
209066
Mahadevan
beta-Aspartylglucosylamine ami ...
Rattus sp.
J. Biol. Chem.
242
4568-4578
1967
-
-
-
-
-
-
4
1
1
-
-
-
-
1
-
-
1
-
-
2
1
1
1
-
-
-
1
-
1
-
2
-
2
-
-
-
-
-
-
-
-
-
-
4
2
1
1
-
-
-
-
-
-
1
-
2
1
1
1
-
-
-
1
-
1
-
2
-
-
-
-
-
-
-