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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.4.19.5
667054
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli
Acta Crystallogr. Sect. D
D60
1173-1176
2004
Escherichia coli
15159592
3.4.19.5
647275
High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli
Biochemistry
42
4874-4882
2003
Escherichia coli
12718528
3.4.19.5
667676
Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli
Biochemistry
44
7115-7124
2005
Escherichia coli
15882050
3.4.19.5
731313
Structural and kinetic characterization of guinea pig L-asparaginase type III
Biochemistry
53
2318-2328
2014
Cavia porcellus
24669941
3.4.19.5
707482
The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity
Biochemistry
48
11026-11031
2009
Homo sapiens
19839645
3.4.19.5
740406
Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog
Eur. J. Biochem.
271
3215-3226
2004
Lupinus luteus
15265041
3.4.19.5
669365
Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate
J. Biol. Chem.
280
28484-28491
2005
Escherichia coli
15946951
3.4.19.5
647273
Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli
J. Biol. Chem.
270
4076-4087
1995
Escherichia coli
7876157
3.4.19.5
698748
The mechanism of autocatalytic activation of plant-type L-asparaginases
J. Biol. Chem.
283
13388-13397
2008
Escherichia coli
18334484
3.4.19.5
754254
Include dispersion in quantum chemical modeling of enzymatic reactions the case of isoaspartyl dipeptidase
J. Chem. Theory Comput.
11
2525-2535
2015
Escherichia coli
26575552
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