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Literature summary extracted from

  • Ni, J.; Takehara, M.; Watanabe, H.
    Identification of activity related amino acid mutations of a GH9 termite cellulase (2010), Biores. Technol., 101, 6438-6446.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.4 DNA and amino acid sequence determination and comparison, expression of wild-type and mutant enzymes in Escherichia coli strain JM109 Reticulitermes speratus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.4 A170S site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 A87S site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 D53X site-directed mutagenesis, inactive mutant Reticulitermes speratus
3.2.1.4 D56X site-directed mutagenesis, inactive mutant Reticulitermes speratus
3.2.1.4 E411X site-directed mutagenesis, inactive mutant Reticulitermes speratus
3.2.1.4 G147R site-directed mutagenesis, inactive mutant Reticulitermes speratus
3.2.1.4 G91A site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme Reticulitermes speratus
3.2.1.4 G91A/K429A site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects Reticulitermes speratus
3.2.1.4 G91A/Y97W site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects Reticulitermes speratus
3.2.1.4 G91A/Y97W/G147R site-directed mutagenesis, inactive mutant Reticulitermes speratus
3.2.1.4 G91A/Y97W/K429A site-directed mutagenesis, the triple mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects Reticulitermes speratus
3.2.1.4 G91I site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 I347V site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 K429A site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme Reticulitermes speratus
3.2.1.4 L103I site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 N245S site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 N38D site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 Q202K site-directed mutagenesis, almost inactive mutant Reticulitermes speratus
3.2.1.4 Q42N/K43N site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 S173A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 S25A site-directed mutagenesis, almost inactive mutant Reticulitermes speratus
3.2.1.4 S90D site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 Y329F site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 Y97F site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Reticulitermes speratus
3.2.1.4 Y97W site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme Reticulitermes speratus
3.2.1.4 Y97W/K429A site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects Reticulitermes speratus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Reticulitermes speratus
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.4 109
-
 purified recombinant mutant K429A Reticulitermes speratus
3.2.1.4 137
-
 purified recombinant mutant G91A Reticulitermes speratus
3.2.1.4 154
-
 purified recombinant mutant Y97W Reticulitermes speratus
3.2.1.4 248
-
 purified recombinant mutant G91A/K429A Reticulitermes speratus
3.2.1.4 349
-
 purified recombinant mutant G91A/Y97W Reticulitermes speratus
3.2.1.4 357
-
 purified recombinant mutant Y97W/K429A Reticulitermes speratus
3.2.1.4 469
-
 purified recombinant mutant G91A/Y97W/K429A Reticulitermes speratus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 carboxymethyl cellulose + H2O
-
 Reticulitermes speratus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 endo-beta-1,4-glucanase
-
 Reticulitermes speratus
3.2.1.4 GH9 termite cellulase
-
 Reticulitermes speratus
3.2.1.4 More the enzyme belongs to the gylcosyl hydrolase family GH9 Reticulitermes speratus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.4 37
-
 assay at Reticulitermes speratus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.4 25 70
-
 Reticulitermes speratus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.4 5.5
-
 assay at Reticulitermes speratus