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Literature summary for 3.2.1.4 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)

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

Protein Variants

Protein Variants Comment Organism
A211D site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
A253S site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
D287C site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
D287E site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
D287N site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
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
E368A/E407A site-directed mutagenesis, the double mutant shows decreased activity at pH 5.0 compared to the wild-type enzyme Cellulomonas fimi
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
K292A site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
K292A/E407A site-directed mutagenesis, the double mutant shows increased activity at pH 5.0 compared to the wild-type enzyme Cellulomonas fimi
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
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
N320C site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
N320D site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
N320E site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
N360D site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
N360H site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
N360K site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
N360R site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
Q256C site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
Q256D site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
Q256E site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
S319A site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
S319D site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
S319H site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
S319K site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
S319R site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
Y321A site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
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
Y321F/E407A site-directed mutagenesis, the double mutant shows increased activity at pH 5.0 compared to the wild-type enzyme Cellulomonas fimi
Y321H site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme Cellulomonas fimi
Y321K site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0 Cellulomonas fimi
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)

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

Organism

Organism UniProt Comment Textmining
Cellulomonas fimi
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
cellulase A
-
Cellulomonas fimi
CenA
-
Cellulomonas fimi

Temperature Optimum [°C]

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