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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
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
731313
Structural and kinetic characterization of guinea pig L-asparaginase type III
Biochemistry
53
2318-2328
2014
Cavia porcellus
24669941
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
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
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
647274
X-ray Structure of isoaspartyl dipeptidase from E. coli: a dinuclear zinc peptidase evolved from amidohydrolases
J. Mol. Biol.
332
243-256
2003
Escherichia coli
12946361
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