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Literature summary 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

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

Application

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.1.1 overview Escherichia coli

Protein Variants

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.1 2,3-diphosphoglycerate
-
Escherichia coli
4.3.1.1 3-nitropropanoate
-
Escherichia coli
4.3.1.1 D-malate
-
Escherichia coli
4.3.1.1 DL-2amino-3-phosphonopropanoate
-
Escherichia coli
4.3.1.1 additional information overview on inhibitors Escherichia coli
4.3.1.1 o-phospho-D-serine
-
Escherichia coli

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.1 52000
-
4 * 52000, SDS-PAGE Escherichia coli
4.3.1.1 52000
-
4 * 52000, overview Pseudomonas fluorescens

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.1 overview Escherichia coli

Reaction

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

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.3.1.1 denaturation by addition of high concentrations of guanidine-HCl leads to reversible dissociation and reassembly of the tetrameric structure Escherichia coli
4.3.1.1 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)

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

Subunits

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.1.1 0.2
-
o-phospho-D-serine
-
Escherichia coli
4.3.1.1 0.66
-
D-malate
-
Escherichia coli
4.3.1.1 0.66
-
DL-2amino-3-phosphonopropanoate
-
Escherichia coli
4.3.1.1 0.83
-
3-nitropropanoate
-
Escherichia coli
4.3.1.1 1.1
-
2,3-diphosphoglycerate
-
Escherichia coli