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Literature summary for 4.3.1.1 extracted from

  • Gou, X.j.; Li, S.; Kong, X.d.; Liu, W.; Sun, Y.h.; Zhang, J.
    Directed evolution of L-aspartase by mobility of domains (2004), Chem. Res. Chin. Univ., 20, 50-54.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2
-
L-aspartate native enzyme Escherichia coli
1.23
-
L-aspartate tetrameric mutant enzyme maspase 3 Escherichia coli
2.6
-
L-aspartate dimeric mutant enzyme maspase 2 Escherichia coli
5.5
-
L-aspartate monomeric mutant enzyme maspase 1 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ maximal activity: 1.0 mM for native enzyme, 2.2 mM for monomeric mutant enzyme maspase 1, 1.8 mM for dimeric mutant enzyme maspase 2, 1.6 mM for tetrameric mutant enzyme maspase 3 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
1 * 56000, mutant enzyme maspase 1, SDS-PAGE Escherichia coli
56000
-
2 * 56000, mutant enzyme maspase 2, SDS-PAGE Escherichia coli
56000
-
4 * 56000, mutant enzyme maspase 3, SDS-PAGE Escherichia coli
56200
-
monomeric mutant enzyme maspase 1, gel filtration Escherichia coli
109600
-
dimeric mutant enzyme maspase 2, gel filtration Escherichia coli
213800
-
tetrameric mutant enzyme maspase 3, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
plasmid carrying the L-aspartase gene
-
Escherichia coli J2
-
plasmid carrying the L-aspartase gene
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
Escherichia coli fumarate + NH3
-
?
L-aspartate
-
Escherichia coli J2 fumarate + NH3
-
?

Subunits

Subunits Comment Organism
dimer 2 * 56000, mutant enzyme maspase 2, SDS-PAGE Escherichia coli
monomer 1 * 56000, mutant enzyme maspase 1, SDS-PAGE Escherichia coli
tetramer 4 * 56000, mutant enzyme maspase 3, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
maspase 1 insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained Escherichia coli
maspase 2 insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained Escherichia coli
maspase 3 insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
30 min, native enzyme loses 83% of initial activity, monomeric mutant enzyme maspase 1 loses 23% of initial activity, dimeric mutant enzyme maspase 2 loses 48% of initial activity, tetrameric mutant enzyme maspase 3 loses 59% of initial activity Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
163
-
L-aspartate monomeric mutant enzyme maspase 1 Escherichia coli
165
-
L-aspartate dimeric mutant enzyme maspase 2 Escherichia coli
170
-
L-aspartate tetrameric mutant enzyme maspase 3 Escherichia coli
180
-
L-aspartate native enzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3
-
monomeric mutant enzyme maspase 1 Escherichia coli
6.8
-
dimeric mutant enzyme maspase 2 Escherichia coli
7.1
-
tetrameric mutant enzyme maspase 3 Escherichia coli
7.5
-
native enzyme Escherichia coli