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Literature summary for 3.2.1.8 extracted from

  • Sunna, A.; Gibbs, M.D.; Bergquist, P.L.
    A novel thermostable multidomain 1,4-beta-xylanase from Caldibacillus cellulovorans and effect of its xylan-binding domain on enzyme activity (2000), Microbiology, 146, 2947-2955.
    View publication on PubMed
Search for more literature for 3.2.1.8

Cloned(Commentary)

Cloned (Comment) Organism
gene xynA, DNA and amino acid sequence determination and analysis, expression of domains D1 + D2 or D2 alone in Escherichia coli [Caldibacillus] cellulovorans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 [Caldibacillus] cellulovorans

Organism

Organism UniProt Comment Textmining
[Caldibacillus] cellulovorans Q9L8L8 gene xynA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme domains from Escherichia coli [Caldibacillus] cellulovorans

Reaction

Reaction Comment Organism Reaction ID
(Xylbeta(1-4))n + H2O = (Xylbeta(1-4))n-m + (Xylbeta(1-4))m role of the thermostabilizing N-terminal domain XBD on enzyme activity, overview [Caldibacillus] cellulovorans
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 [Caldibacillus] cellulovorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate specificity and hydrolysis pattern [Caldibacillus] cellulovorans ?
-
 ?
xylan + H2O from oat spelt or birchwood [Caldibacillus] cellulovorans xylooligosaccharides recombinant N-terminal + catalytic domains produce mainl xylobiose, xylotriose and xylotetraose, while the single recombinant catalytic domain produces mainly xylotriose and xylotetraose, no further hydrolysis of the oligomeric products ?

Subunits

Subunits Comment Organism
More domain composition, the enzyme contains an N-termminal domain D1 which is the xylan-binding domain XBD, it is homologous to noncatalytic thermostabilizing domains of other xylanases, D1 is followed by the catalytic D2 domain, and 2 cellulose-binding domains D3 and D4, the latter linked via a proline-threonine-rich sequence [Caldibacillus] cellulovorans

Synonyms

Synonyms Comment Organism
1,4-beta-xylanase
-
 [Caldibacillus] cellulovorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 recombinant catalytic domain [Caldibacillus] cellulovorans
90
-
 recombinant N-terminal + catalytic domains [Caldibacillus] cellulovorans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 100 recombinant N-terminal + catalytic domains [Caldibacillus] cellulovorans
40 85 recombinant catalytic domain [Caldibacillus] cellulovorans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60 70 thermostability of the recombinant catalytic domain is decreased to 60°C in absence and increased to 70°C in presence of the recombinant N-terminal thermostabilizing domain D1 [Caldibacillus] cellulovorans
85
-
 12% remaining activity of recombinant catalytic domain [Caldibacillus] cellulovorans
95
-
 60% remaining activity of recombinant N-terminal + catalytic domains [Caldibacillus] cellulovorans
100
-
 15% remaining activity of recombinant N-terminal + catalytic domains [Caldibacillus] cellulovorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 recombinant catalytic domain at 70°C, and recombinant N-terminal + catalytic domains at 90°C [Caldibacillus] cellulovorans

pH Range

pH Minimum pH Maximum Comment Organism
6 8 40% activity at pH 8.0, no activity at pH 4.0 and pH 9.0 [Caldibacillus] cellulovorans