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Literature summary extracted from

  • Cockburn, D.; Clarke, A.
    Modulating the pH-activity profile of cellulase A from Cellulomonas fimi by replacement of surface residues (2011), Protein Eng., 24, 429-437.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.4 expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3 pLysS), subcloning in strain DH5alpha Cellulomonas fimi

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.4 A211D site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 A253S site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 D287C site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 D287E site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 D287N site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 E368A site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 E368A/E407A site-directed mutagenesis, the double mutant shows decreased activity at pH 5.0 compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 E407A site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 K292A site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 K292A/E407A site-directed mutagenesis, the double mutant shows increased activity at pH 5.0 compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 L387P site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 additional information engineering of cellulase A from Cellulomonas fimi as a model to replace residues that potentially influence the pH-activity profile of the enzyme based on sequence alignments and analysis of the known three-dimensional structures of other CAZy family 6 glycoside hydrolases with the aim to lower its pH optimum, overview Cellulomonas fimi
3.2.1.4 N320C site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 N320D site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 N320E site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 N360D site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 N360H site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 N360K site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 N360R site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 Q256C site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 Q256D site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 Q256E site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 S319A site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 S319D site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 S319H site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 S319K site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 S319R site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 Y321A site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 Y321F site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 Y321F/E407A site-directed mutagenesis, the double mutant shows increased activity at pH 5.0 compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 Y321H site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
3.2.1.4 Y321K site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
3.2.1.4 Y321R site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.4 carboxymethyl cellulose + H2O Cellulomonas fimi
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Cellulomonas fimi
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 cellulase A
-
 Cellulomonas fimi
3.2.1.4 CenA
-
 Cellulomonas fimi

Temperature Optimum [°C]

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