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Literature summary extracted from

  • Okada, G.; Nisizawa, K.
    Enzymatic studies on a cellulase system of Trichoderma viride. III. Transglycosylation properties of two cellulase components of random type (1975), J. Biochem., 78, 297-306.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.4 0.04
-
cellotetraose cellulase II-A Trichoderma viride
3.2.1.4 0.15
-
cellopentaose cellulase II-A Trichoderma viride
3.2.1.4 0.28
-
cellopentaose cellulase II-B Trichoderma viride
3.2.1.4 0.33
-
cellohexaose cellulase II-A Trichoderma viride
3.2.1.4 0.42
-
cellotetraose cellulase II-B Trichoderma viride
3.2.1.4 0.46
-
cellopentaose cellulase II-A Trichoderma viride
3.2.1.4 1.63
-
cellotriose cellulase II-B Trichoderma viride

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Trichoderma viride
-
cellulase II-A and II-B
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 2 cellobiose transfer reaction Trichoderma viride cellotetraose + H2O
-
?
3.2.1.4 cellohexaose + H2O
-
Trichoderma viride additional information
-
?
3.2.1.4 cellopentaose + H2O beta-configuration of the anomeric carbon atoms is retained Trichoderma viride additional information
-
?
3.2.1.4 cellotriose + H2O
-
Trichoderma viride D-glucose + cellobiose
-
?
3.2.1.4 p-nitrophenyl beta-D-cellobioside + H2O cellulase II-A preferentially attacks the holoside linkage of p-nitrophenyl beta-D-cellobioside, cellulase II-B attacks mainly the aglycone linkage. Synthesis of cellotriose from p-nitrophenyl beta-D-cellobioside by transfer of a glucosyl residue, possibly to cellobiose produced in the reaction mixture Trichoderma viride glucose + cellobiose + ?
-
?