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Literature summary for 3.2.1.8 extracted from

  • Sudo, M.; Sakka, M.; Kimura, T.; Ratanakhanokchai, K.; Sakka, K.
    Characterization of Paenibacillus curdlanolyticus intracellular xylanase Xyn10B encoded by the xyn10B gene (2010), Biosci. Biotechnol. Biochem., 74, 2358-2360.
    View publication on PubMed
Search for more literature for 3.2.1.8

Cloned(Commentary)

Cloned (Comment) Organism
gene xyn10B, DNA and amino acid sequence determination and analysis, expression in Escherichia coli Paenibacillus curdlanolyticus

Protein Variants

Protein Variants Comment Organism
additional information generation of a truncationmutant lacking the N-terminal domain, the mutant is catalytically inactive Paenibacillus curdlanolyticus

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
 Paenibacillus curdlanolyticus 5622
-

Organism

Organism UniProt Comment Textmining
Paenibacillus curdlanolyticus E3WF08 gene xyn10B
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
birch wood xylan + H2O
-
 Paenibacillus curdlanolyticus ?
-
 ?
additional information the enzyme hydrolyzes birchwood xylan and xylooligosaccharides, to produce mainly xylobiose, acting as an endoxylanase. Xyn10B also shows transglycosylation activity with xylooligosaccharides, overview Paenibacillus curdlanolyticus ?
-
 ?
oat spelt xylan + H2O
-
 Paenibacillus curdlanolyticus ?
-
 ?

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the family 10 xylanases Paenibacillus curdlanolyticus
xylanase
-
 Paenibacillus curdlanolyticus
Xyn10B
-
 Paenibacillus curdlanolyticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 recombinant enzyme Paenibacillus curdlanolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 recombinant enzyme Paenibacillus curdlanolyticus

General Information

General Information Comment Organism
additional information the N-terminal domain of the enzyme is required for catalytic activity Paenibacillus curdlanolyticus