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Literature summary for 3.2.1.74 extracted from

  • Jagtap, S.; Rao, M.
    Fluorescence study on interactions of alpha-crystallin with the molten globule state of 1, 4-beta-D-glucan glucanohydrolase from Thermomonospora sp. induced by guanidine hydrochloride (2009), J. Fluoresc., 19, 967-973.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Thermomonospora sp.
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-
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Purification (Commentary)

Purification (Comment) Organism
TSC by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration Thermomonospora sp.

Renatured (Commentary)

Renatured (Comment) Organism
denaturation studies using GdnCl indicate that TSC folds through a partially folded state that resembles molten globule at 1.8 M GdnCl. alpha-Crystallin chaperone-mediated in vitro folding, molecular mechanism, overview. Reconstitution of the active TSC is observed in 50 mM sodium phosphate buffer, pH 7.0, on cooling the alpha-crystallin-TSC-m complex to 4°C. Addition of alpha-crystallin to the molten globule-like intermediate of TSC complex initiates the refolding of TSC with 69% recovery of the biological activity of the enzyme Thermomonospora sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carboxymethylcellulose + H2O
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Thermomonospora sp. ?
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?
additional information fluorescence study on interactions of chaperone alpha-crystallin with the molten globule state of the enzyme induced by guanidine hydrochloride Thermomonospora sp. ?
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?

Subunits

Subunits Comment Organism
More fluorescence study on interactions of alpha-crystallin with the molten globule state of the enzyme induced by guanidine hydrochloride Thermomonospora sp.

Synonyms

Synonyms Comment Organism
1,4-beta-D-glucan glucanohydrolase
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Thermomonospora sp.
Carboxymethyl cellulase
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Thermomonospora sp.
TSC
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Thermomonospora sp.