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Literature summary for 3.2.1.6 extracted from

  • Araki, R.; Ali, M.K.; Sakka, M.; Kimura, T.; Sakka, K.; Ohmiya, K.
    Essential role of the family-22 carbohydrate-binding modules for beta-1,3-1,4-glucanase activity of Clostridium stercorarium Xyn10B (2004), FEBS Lett., 561, 155-158.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant truncated proteins in Escherichia coli Thermoclostridium stercorarium

Protein Variants

Protein Variants Comment Organism
additional information construction of truncated proteins: a recombinant catalytic module polypeptide (rCD), a carbohydrate-binding module polypeptide composed of two family-22 carbohydrate-binding modules (rCBM) and a polypeptide composed of the family-22 carbohydrate-binding modules and the catalytic module (rCBM-CD). rCBM-CD is highly active towards beta-1,3-1,4-glucan, rCD is negligibly active towards the same substrate. The Vmax/KM value of rCBM-CD for beta-1,3-1,4-glucan is 7.8 times larger than that for oat-spelt xylan Thermoclostridium stercorarium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Thermoclostridium stercorarium

Organism

Organism UniProt Comment Textmining
Thermoclostridium stercorarium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermoclostridium stercorarium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
barley beta-glucan + H2O
-
Thermoclostridium stercorarium ?
-
?
lichenan + H2O
-
Thermoclostridium stercorarium ?
-
?

Synonyms

Synonyms Comment Organism
CBM-CD
-
Thermoclostridium stercorarium
Xyn10B modular enzyme comprising two family-22 carbohydrate-binding modules (CBMs), a family-10 catalytic module of glycoside hydrolases, a family-9 carbohydrate-binding module, and two S-layer homologous modules consecutively from the N-terminus Thermoclostridium stercorarium