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Literature summary for 3.2.1.6 extracted from

  • Zhao, G.; Ali, E.; Araki, R.; Sakka, M.; Kimura, T.; Sakka, K.
    Function of the family-9 and family-22 carbohydrate-binding modules in a modular beta-1,3-1,4-glucanase/xylanase derived from Clostridium stercorarium Xyn10B (2005), Biosci. Biotechnol. Biochem., 69, 1562-1567.
    View publication on PubMed
Search for more literature for 3.2.1.6

Protein Variants

Protein Variants Comment Organism
additional information engineering of truncated enzyme composed of two family-22 carbohydrate-binding modules and the catalytic module (rCBM22-CM), an enzyme composed of the catalytic module and family-9 carbohydrate-binding module (rCM-CBM9), and the catalytic module polypeptide. Although the addition of family-9 carbohydrate-binding module to rCM and rCM22-CM does not significantly change catalytic activity towards xylan and beta-1,3-1,4-glucan, the addition of family-22 carbohydrate-binding module to rCM and rCM-CBM9 drastically enhances catalytic activity towards xylan and especially beta-1,3-1,4-glucan. The addition of family-22 carbohydrate-binding module to rCM and rCM-CBM9 shofts the optimum temperature from 65°C to 75°C, but that of family-9 carbohydrate-binding module to rCM and rCM-22-CM does not affect the optimum temperature 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
Xyn10B modular enzyme composed of two family-22 carbohydrate-binding modules, a family-9 carbohydrate-binding module, and two S-layer homologous modules Thermoclostridium stercorarium