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Literature summary for 4.3.1.1 extracted from

  • Viola, R.E.
    L-aspartase: new tricks from an old enzyme (2000), Adv. Enzymol. Relat. Areas Mol. Biol., 74, 295-341.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-Aspartate
-
Escherichia coli
o-phospho-D-serine
-
Escherichia coli

Application

Application Comment Organism
biotechnology overview on commercial applications Escherichia coli
medicine involvement of enzyme in blood clotting and activation of plasminogen, overview Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment) Organism
overview Escherichia coli

Protein Variants

Protein Variants Comment Organism
C141S/C274A elimination of sensitivity to inactivation Escherichia coli
K140I Km value 10fold higher than wild type, comparable increase in Ki for competitive inhibitors Escherichia coli
additional information overview Escherichia coli
additional information overview Hafnia alvei

Inhibitors

Inhibitors Comment Organism Structure
2,3-diphosphoglycerate
-
Escherichia coli
3-nitropropanoate
-
Escherichia coli
D-malate
-
Escherichia coli
DL-2amino-3-phosphonopropanoate
-
Escherichia coli
additional information overview on inhibitors Escherichia coli
o-phospho-D-serine
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activation Hafnia alvei
Mn2+ activation Hafnia alvei
additional information absolute requirement for divalent metal ion at higher pH Escherichia coli
additional information no activation by Ca2+, minimal activation by Co2+, pH-dependent activation by divalent cations at high pH values Hafnia alvei
Zn2+ activation Hafnia alvei
Zn2+ most potent activating metal ion Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
4 * 52000, SDS-PAGE Escherichia coli
52000
-
4 * 52000, overview Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Haemophilus influenzae
-
-
-
Hafnia alvei
-
-
-
Pseudomonas fluorescens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
overview Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
L-aspartate = fumarate + NH3 mechanism Escherichia coli
L-aspartate = fumarate + NH3 mechanism: overview Hafnia alvei

Renatured (Commentary)

Renatured (Comment) Organism
denaturation by addition of high concentrations of guanidine-HCl leads to reversible dissociation and reassembly of the tetrameric structure Escherichia coli
denaturation by addition of high concentrations of guanidine-HCl leads to reversible dissociation and reassembly of the tetrameric structure Pseudomonas fluorescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
Escherichia coli fumarate + NH3
-
r
additional information no activity with D-aspartic acid or crotonic acid, overview substrate specificity Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 52000, overview Pseudomonas fluorescens
More overview Hafnia alvei
tetramer 4 * 52000, SDS-PAGE Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.2
-
o-phospho-D-serine
-
Escherichia coli
0.66
-
D-malate
-
Escherichia coli
0.66
-
DL-2amino-3-phosphonopropanoate
-
Escherichia coli
0.83
-
3-nitropropanoate
-
Escherichia coli
1.1
-
2,3-diphosphoglycerate
-
Escherichia coli