Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.176 extracted from

  • Brady, S.; Sreelatha, S.; Feng, Y.; Chundawat, S.; Lang, M.
    Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps (2015), Nature Commun., 6, 10149.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis development of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei G0RVK1
-
-
Trichoderma reesei QM6a G0RVK1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information use of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion Trichoderma reesei ?
-
?
additional information use of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion Trichoderma reesei QM6a ?
-
?