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Literature summary for 1.10.3.2 extracted from

  • Hamuro, Y.; Tajima, K.; Matsumoto-Akanuma, A.; Sakamoto, S.; Furukawa, R.; Yamagishi, A.; Ohno, N.; Akanuma, S.
    Characterization of a thermostable mutant of Agaricus brasiliensis laccase created by phylogeny-based design (2017), J. Biosci. Bioeng., 124, 623-629 .
    View publication on PubMed
Search for more literature for 1.10.3.2

Application

Application Comment Organism
synthesis the enzyme will serve as a useful tool for enzymatic polymerization of diphenolic compounds such as caffeic acid and ferulic acid Agaricus brasiliensis

Cloned(Commentary)

Cloned (Comment) Organism
attempts of heterologous expression of the wild-type laccase using a Pichia pastoris secretory expression system are unsuccessful most likely because the enzyme is too unstable and degrades immediately after production. Therefore the stability of the laccase is improved by using a phylogeny-based design method. A mutant laccase is created in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence. The resulting mutant protein is successfully produced using the Pichia pastoris secretory expression system and then purified Agaricus brasiliensis

Organism

Organism UniProt Comment Textmining
Agaricus brasiliensis V5XVN3
-
-

Purification (Commentary)

Purification (Comment) Organism
attempts of heterologous expression of the wild-type laccase using a Pichia pastoris secretory expression system are unsuccessful most likely because the enzyme is too unstable and degrades immediately after production. Therefore the stability of the laccase is improved by using a phylogeny-based design method. A mutant laccase is created in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence. The resulting mutant protein is successfully produced using the Pichia pastoris secretory expression system and then purified Agaricus brasiliensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
-
 Agaricus brasiliensis ?
-
 ?

Synonyms

Synonyms Comment Organism
Lac2a
-
 Agaricus brasiliensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 the mutant enzyme is resistant to heat treatment of 10 min. The mutant protein loses 45% of its original activity after incubation for 1 h. Mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence Agaricus brasiliensis
80
-
 10 min, mutant enzyme retains 70% of its original activity, mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence Agaricus brasiliensis
85
-
 10 min, mutant enzyme retains 30% of its original activity, mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence Agaricus brasiliensis

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5
-
 half live of mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence: 63.0 min (at pH 6.0), 6.1 min (pH 10.5) Agaricus brasiliensis
7.6
-
 half live of mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence: 57.8 min (at pH 6.0) Agaricus brasiliensis