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Literature summary for 3.2.1.32 extracted from

  • Kiyohara, M.; Sakaguchi, K.; Yamaguchi, K.; Araki, T.; Ito, M.
    Characterization and application of carbohydrate-binding modules of beta-1,3-xylanase XYL4 (2009), J. Biochem., 146, 633-641.
    View publication on PubMed
Search for more literature for 3.2.1.32

Cloned(Commentary)

Cloned (Comment) Organism
gene xyl4, DNA and amino acid sequence determination and comparison, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Vibrio sp. AX-4

Protein Variants

Protein Variants Comment Organism
additional information construction of five different XYL4 deletion mutants, CBM-1, CBM-2, CBM-1-2, CM-CBM-1, and CM, possessing a catalytic module Vibrio sp. AX-4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information binding specificities and dissociation constants of XYL4 and its mutants with different polysaccharides and glycol-beta-1,3-xylan and beta-1,3-xylan, overview Vibrio sp. AX-4

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl both the enzyme and the binding activities for insoluble beta-1,3-xylan but not soluble glycol-beta-1,3-xylan, are enhanced by NaCl Vibrio sp. AX-4

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-1,3-xylan + H2O Vibrio sp. AX-4
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Vibrio sp. AX-4 D5MP61 gene xyl4
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL2(DE3) by nickel affinity and beta-1,3-xylan affinity chromatography and gel filtration Vibrio sp. AX-4

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-1,3-xylan + H2O
-
 Vibrio sp. AX-4 ?
-
 ?
additional information XYL4, an endo-type enzyme, contains two putative carbohydrate-binding modules, CBMs, belonging to family 31 in the C-terminal region. Repeating CBMs bind specifically to insoluble beta-1,3-xylan, but not to beta-1,4-xylan, Avicel, beta-1,4-mannan, curdlan, chitin or soluble glycol-beta-1,3-xylan, through hydrophobic interaction. Binding specificities of XYL4 and its mutants, overview Vibrio sp. AX-4 ?
-
 ?

Subunits

Subunits Comment Organism
More XYL4 is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules belonging to family 31 in the C-terminal region, sequence determination, overview Vibrio sp. AX-4

Synonyms

Synonyms Comment Organism
beta-1,3-xylanase
-
 Vibrio sp. AX-4
More XYL4 is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules belonging to family 31 in the C-terminal region Vibrio sp. AX-4
XYL4
-
 Vibrio sp. AX-4

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Vibrio sp. AX-4

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Vibrio sp. AX-4