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Literature summary for 4.3.1.1 extracted from

  • Asano, Y.; Kira, I.; Yokozeki, K.
    Alteration of substrate specificity of aspartase by directed evolution (2005), Biomol. Eng., 22, 95-101.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type enzyme and His-tagged mutant enzyme K327N in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
K327N mutant enzyme catalyzes the deamination of L-aspartic acid alpha-amide, 13.5fold increase in Km-value for L-aspartate compared to wild-type value Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1
-
L-aspartic acid pH 8.5, 30°C, wild-type enzyme Escherichia coli
28.3
-
L-aspartic acid pH 8.5, 30°C, mutant enzyme K327N Escherichia coli
1450
-
L-aspartic acid alpha-amide pH 7.0, 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AC38
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate highly selective towards L-aspartate Escherichia coli fumarate + NH3
-
r
L-aspartic acid alpha-amide catalyzed by mutant enzyme K327N, no activity with wild-type enzyme Escherichia coli (2E)-4-amino-4-oxobut-2-enoate + NH3
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
deamination of L-aspartic acid alpha-amide, mutant enzyme K327N Escherichia coli
8.5
-
deamination of L-aspartate, wild-type enzyme and mutant enzyme K327N Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7 9 pH 7.0: about 40% of maximal activity, pH 9.0: about 90% of maximal activity, substrate: L-aspartate, wild-type enzyme Escherichia coli
7.5 9 pH 7.5: about 70% of maximal activity, pH 9.0: about 85% of maximal activity, substrate: L-aspartic acid, mutant enzyme K327N Escherichia coli