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Literature summary for 3.2.1.4 extracted from

  • Xiong, W.; Yang, J.K.; Chen, F.Y.; Han, Z.G.
    The catalytic domain of Penicillium crustosum endoglucanase EGL1 has cellulose-binding capacity and cellulolytic activity (2017), Enzyme Microb. Technol., 97, 71-81 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Penicillium crustosum

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modeling of the catalytic domain. The domain structurally belongs to the GH-A family Penicillium crustosum

Protein Variants

Protein Variants Comment Organism
additional information both the full-length enzyme and the catalytic domain have carboxymethylcellulase and filter paper hydrolase activity . The catalytic domain can also bind the cellulose substrate. The aromatic amino acids at the bottom of the barrel fold and those adjacent to the catalytic site significantly affect the cellulolytic activity and the cellulose binding affinity of the catalytic domain Penicillium crustosum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
carboxymethylcellulose Km value 9.2 mg/ml for full-length protein, 11.5 mG/ml for catalytic domain, respectively, pH 7.0, 45°C Penicillium crustosum

Organism

Organism UniProt Comment Textmining
Penicillium crustosum U6A8H3
-
-
Penicillium crustosum 601 U6A8H3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carboxymethylcellulose + H2O
-
Penicillium crustosum ?
-
?
carboxymethylcellulose + H2O
-
Penicillium crustosum 601 ?
-
?

Synonyms

Synonyms Comment Organism
Egl1
-
Penicillium crustosum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Penicillium crustosum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Penicillium crustosum